Updated on 2025/05/09

写真a

 
SAWAI HITOMI
 
Organization
Graduate School of Science Department of Chemistry Professor
School of Science Department of Chemistry
Title
Professor
Affiliation
Institute of Science
Contact information
メールアドレス
Affiliation campus
Sugimoto Campus

Position

  • Graduate School of Science Department of Chemistry 

    Professor  2025.04 - Now

  • School of Science Department of Chemistry 

    Professor  2025.04 - Now

Degree

  • Ph.D. （ Himeji Institute of Technology ） (   Himeji Institute of Technology (currently known as University of Hyogo) )

Research Areas

  • Life Science / Structural biochemistry  / protein-metal interactions

  • Life Science / Functional biochemistry  / metals in biology

  • Life Science / Functional biochemistry  / Bioinorganic Chemistry

  • Life Science / Functional biochemistry  / Biochemistry

  • Life Science / Nutrition science and health science  / dietary iron, iron nutrients

  • Life Science / Molecular biology  / Protein Science

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Research Interests

  • Integrated Bio-Metal Science

  • Biological Inorganic Chemistry

  • Protein science

  • Nutritional iron

  • Heme

  • Membrane protein

  • LCP crystallization

  • X-ray microspope

  • Iron metabolism

  • Mass photometry

  • Hemoproteins

  • Sensor protein

  • SAXS

Research subject summary

  • Metals play important roles in living organisms! Our cells are mainly made up of water, proteins, and lipids, but they also contain small amounts of metals that help keep our bodies in good condition. The metal nutrients contained in food are used to reduce toxicity by binding to a wide variety of proteins. In other words, these metals are used as active centers of enzymes that carry out functions essential to sustaining life, e.g. transport and storage of oxygen, energy production, gene synthesis, has been known for many years. However, the series of molecular mechanisms underlying metal dynamics in the body (absorption, sensing, transport, storage, and excretion of metals) and selectivity for individual metals remain unknown. My research focuses on "iron", which is the most important metal among the essential metals for sustaining the life of living things, focusing on various proteins that play a role in the selective absorption, sensing, and intracellular transport of iron in food. We are not only elucidating the structure of related proteins, but also exploring the relationship with the functions in human cells.

Professional Memberships

  • International Society for the Study of Iron in Biology and Medicine (BIOIRON)

      Overseas

  • Society of Biological Inorganic Chemistry (SBIC)

      Overseas

  • THE JAPANESE BIOCHEMICAL SOCIETY

  • 生命金属科学研究会

  • The Japanese BioIron Society

  • PROTEIN SCIENCE SOCIETY OF JAPAN

  • Japan Society for Bioscience, Biotechnology, and Agrochemistry

  • THE CRYSTALLOGRAPHIC SOCIETY OF JAPAN

  • THE CHEMICAL SOCIETY OF JAPAN

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Committee Memberships (off-campus)

  • 常任幹事   生命金属科学研究会  

    2025.04 - Now 

  • 代議員   一般社団法人 日本鉄バイオサイエンス学会  

    2024.09 - Now 

  • 実行委員   第26回日本蛋白質科学会年会  

    2025.03 - Now 

  • LINXS Fellow, LINXS "Chemistry of Life" Core Group   Lund Institute of Advanced Neutron and X-ray Science (LINXS)  

    2023.06 - Now 

  • 九州シンクロトロン光大学間連携会議委員   佐賀シンクロトロン光応用研究センター  

    2023.04 - 2025.03 

  • 科学研究費委員会専門委員   独立行政法人日本学術振興会  

    2022.10 - 2025.03 

  • バイオメディカルモデル動物研究センター運営委員   長崎大学  

    2023.04 - 2025.03 

  • 先端ゲノム研究センター運営委員   長崎大学  

    2023.04 - 2025.03 

  • 副教務委員   長崎大学工学部化学物質工学コース  

    2024.04 - 2025.03 

  • 基礎実験代表委員   長崎大学  

    2023.04 - 2025.03 

  • 実行委員長   生物無機化学研究会（第35回生物無機化学夏季セミナー）  

    2022.09 - 2023.09 

  • Programme Committee   LINXS UK/Japan Meeting and Workshop  

    2023.05 - 2023.09 

  • Local Organizing Committee   10th Asian International Conference on Biological Inorganic Chemistry (AsBIC10)  

    2022.01 - 2022.12 

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Awards

  • Excellent Research Award

    2018   The Japanese BioIron Society  

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    Country：Japan

  • SHISEIDO Female Researcher Science Grant

    2012   SHISEIDO Company, Limited.  

    　More details

    Country：Japan

  • 山村富美記念女性自然科学者山村フェロー

    2010   中央三井信託銀行  

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    Country：Japan

  • Best Poster Prize

    2008   4th International Conference on Metals and Genetics  

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    Country：France

  • Poster Award

    2010   10th European Biological Inorganic Chemistry Conference  

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    Country：Greece

  • Outstanding Presentation Award

    2012   The Chemical Society of Japan  

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    Country：Japan

  • Poster Award

    2011   The Crystallographic Society of Japan  

    　More details

    Country：Japan

  • Excellent Research Award

    Hitomi Sawai

    2018   The Japanese BioIron Society  

  • Shiseido Female Researcher Science Grant

    Hitomi Sawai

    2012   SHISEIDO Company, Limited  

  • Outstanding Presentation Award

    Hitomi Sawai

    2012   The Chemical Society of Japan  

  • Poster Award

    2011   The Crystallographic Society of Japan  

  • Poster Award

    Hitomi Sawai

    2010   10th European Biological Inorganic Chemistry Conference  

  • 山村富美記念女性自然科学者山村フェロー

    澤井 仁美

    2010   中央三井信託銀行  

  • Best Poster Prize

    Hitomi Sawai

    2008   4th International conference on metals and genetics  

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Job Career (off-campus)

  • Institute for Molecular Science, National Institutes of Natural Sciences   Full Professor

    2025.04 - Now

  • LINXS Institute of Advanced Neutron and X-ray Science   Chemistry of Life   LINXS Fellow

    2023.09 - Now

  • Nagasaki University   Graduate School of Integrated Science and Technology   Visiting Professor

    2025.04 - Now

  • Institute for Molecular Science, National Institutes of Natural Sciences   Associate Professor

    2024.04 - 2025.03

  • Nagasaki University   Chemistry and Materials Engineering Program, Graduate School of Engineering   Associate Professor

    2022.05 - 2025.03

  • University of Liverpool   Institute of Integrative Biology   Visiting Scientist

    2015.05 - 2015.11

  • University of Maryland, College Park   Department of Animal and Avian Sciences   Visiting Professor

    2014.07 - 2014.08

  • University of Hyogo   Graduate School of Life Science   Assistant Professor

    2013.04 - 2022.04

  • University of Hyogo   Graduate School of Life Science

    2013.04 - 2022.04

  • Okazaki Institute for Integrative Bioscience, National Institutes of National Sciences   Research Assistant Professor

    2010.04 - 2013.03

  • National Institute of Natural Sciences   Okazaki Institute for Integrative Bioscience   Research Assistant Professor

    2010.04 - 2013.03

  • Institute for Molecular Science, National Institutes of Natural Sciences   JSPS Postdoctoral Researcher

    2007.04 - 2010.03

  • JSPS   Postdoctoral researcher

    2007.04 - 2010.03

  • RIKEN SPring-8 Center   Visiting Scientist

    2006.10 - 2025.03

  • Institute for Molecular Science, National Institutes of Natural Sciences   IMS Fellow

    2006.04 - 2007.03

  • National Institute of Natural Sciences   Institute for Molecular Science   IMS fellow

    2006.04 - 2007.03

  • RIKEN   Junior Research Associate

    2003.04 - 2006.03

  • RIKEN   Junior Research Associate

    2003.04 - 2006.03

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Papers

  • Architecture of the complete oxygen-sensing FixL-FixJ two-component signal transduction system Reviewed International coauthorship

    Gareth S. A. Wright, Akane Saeki, Takaaki Hikima, Yoko Nishizono, Tamao Hisano, Misaki Kamaya, Kohei Nukina, Hideo Nishitani, Hiro Nakamura, Masaki Yamamoto, Svetlana V. Antonyuk, S. Samar Hasnain, Yoshitsugu Shiro, Hitomi Sawai

    Science Signaling   11 ( 525 )   eaaq0825   2018.04

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    Authorship：Last author,　Corresponding author   Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    DOI： 10.1126/scisignal.aaq0825

    DOI： 10.1126/scisignal.aaq0825

  • Heme controls the structural rearrangement of its sensor protein mediating the hemolytic bacterial survival Reviewed

    Megumi Nishinaga, Hiroshi Sugimoto, Yudai Nishitani, Seina Nagai, Satoru Nagatoishi, Norifumi Muraki, Takehiko Tosha, Kouhei Tsumoto, Shigetoshi Aono, Yoshitsugu Shiro, Hitomi Sawai

    Communications Biology   4 ( 1 )   467   2021.04

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    Authorship：Last author,　Corresponding author   Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    DOI： 10.1038/s42003-021-01987-5

  • Structural basis for promotion of duodenal iron absorption by enteric ferric reductase with ascorbate Reviewed International coauthorship

    Menega Ganasen, Hiromi Togashi, Hanae Takeda, Honami Asakura, Takehiko Tosha, Keitaro Yamashita, Kunio Hirata, Yuko Nariai, Tekeshi Urano, Xiaojing Yuan, Iqbal Hamza, A. Grant Mauk, Yoshitsugu Shiro, Hiroshi Sugimoto, Hitomi Sawai

    Communications Biology   1 ( 1 )   120   2018.08

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    Authorship：Last author,　Corresponding author   Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    DOI： 10.1038/s42003-018-0121-8

  • Capturing an initial intermediate during the P450nor enzymatic reaction using time-resolved XFEL crystallography and caged-substrate. Reviewed

    Takehiko Tosha, Takashi Nomura, Takuma Nishida, Naoya Saeki, Kouta Okubayashi, Raika Yamagiwa, Michihiro Sugahara, Takanori Nakane, Keitaro Yamashita, Kunio Hirata, Go Ueno, Tetsunari Kimura, Tamao Hisano, Kazumasa Muramoto, Hitomi Sawai, Hanae Takeda, Eiichi Mizohata, Ayumi Yamashita, Yusuke Kanematsu, Yu Takano, Eriko Nango, Rie Tanaka, Osamu Nureki, Osami Shoji, Yuka Ikemoto, Hironori Murakami, Shigeki Owada, Kensuke Tono, Makina Yabashi, Masaki Yamamoto, Hideo Ago, So Iwata, Hiroshi Sugimoto, Yoshitsugu Shiro, Minoru Kubo

    Nature Communications   8 ( 1 )   1585   2017.11

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    Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    DOI： 10.1038/s41467-017-01702-1

  • Dynamics of nitric oxide controlled by protein complex in bacterial system. Reviewed International coauthorship

    Erina Terasaka, Kenta Yamada, Po-Hung Wang, Kanta Hosokawa, Raika Yamagiwa, Kimi Matsumoto, Shoko Ishii, Takaharu Mori, Kiyoshi Yagi, Hitomi Sawai, Hiroyuki Arai, Hiroshi Sugimoto, Yuji Sugita, Yoshitsugu Shiro, Takehiko Tosha

    Proceedings of the National Academy of Sciences of the United States of America (PNAS)   114 ( 37 )   9888 - 9893   2017.09

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    Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    DOI： 10.1073/pnas.1621301114

  • Capacity of extracellular globins to reduce liver fibrosis via scavenging reactive oxygen species and promoting MMP-1 secretion Reviewed International coauthorship

    Vu Ngoc Hieu, Le Thi Thanh Thuy, Hoang Hai, Ninh Quoc Dat, Dinh Viet Hoang, Ngo Vinh Hanh, Dong Minh Phuong, Truong Huu Hoang, Hitomi Sawai, Yoshitsugu Shiro, Misako Sato-Matsubara, Daisuke Oikawa, Fuminori Tokunaga, Katsutoshi Yoshizato, Norifumi Kawada

    Redox Biology   52   102286   2022.06

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    Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    DOI： 10.1016/j.redox.2022.102286

  • XFEL Crystal Structures of Peroxidase Compound II Reviewed International coauthorship

    Hanna Kwon, Jaswir Basran, Chinar Pathak, Mahdi Hussain, Samuel L Freeman, Alistair J Fielding, Anna J Bailey, Natalia Stefanou, Hazel A Sparkes, Takehiko Tosha, Keitaro Yamashita, Kunio Hirata, Hironori Murakami, Go Ueno, Hideo Ago, Kensuke Tono, Masaki Yamamoto, Hitomi Sawai, Yoshitsugu Shiro, Hiroshi Sugimoto, Emma L Raven, Peter C E Moody

    Angewandte Chemie International Edition   60 ( 26 )   14578 - 14585   2021.06

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    Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    DOI： 10.1002/ange.202103010

  • Drosophila melanogaster由来のDM9モチーフを含む組み換えタンパク質の炭水化物結合能の分析(Carbohydrate-binding ability of a recombinant protein containing the DM9 motif from Drosophila melanogaster)

    Hatakeyama Tomomitsu, Kojima Fuki, Ohkawachi Issei, Sawai Hitomi, Unno Hideaki

    The Journal of Biochemistry   175 ( 6 )   659 - 669   2024.06（ ISSN:0021-924X ）

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    Drosophila melanogaster由来のCG13321の組み換えタンパク質(rCG13321)を作製した。この分子は大腸菌を用いて作製し、4つのDM9モチーフを有していた。マンノースを固定したカラムを用いたアフィニティクロマトグラフィーの結果、rCG13321はマンノース結合能を示し、高親和性(HA)と低親和性(LA)の分画に分離された。HAはカラムに対する高親和性の他に自己オリゴマー形成能を示したことから、LAとは三次構造に違いがあると考えられた。LAとHA双方が赤血球凝集能を示し、オリゴマンノースを含むデンドリマーを凝集させたことから、両分子が多様な炭水化物結合部位を有することが示唆された。グリカンアレーによる分析の結果、rCG13321は主にD-マンノースとD-ラムノースを2-、3-および4-位の水酸基による水素結合を介して認識すると考えられた。等温滴定型カロリメトリーの結果、rCG13321は典型的なレクチンと同等の親和性を持つことが示された。以上より、CG13321は炭水化物結合タンパク質あるいはレクチンとして機能し、パターン認識分子として外来生物の表面上のマンノースおよび関連する炭水化物を含む分子を検知すると考えられた。

  • Mechanism of iron uptake into cells revealed by structural and functional analysis of the transmembrane iron reductase Dcytb Invited Reviewed

    Hitomi Sawai

    SEITAI NO KAGAKU   75 ( 2 )   112 - 115   2024（ ISSN:0370-9531 ） （ eISSN:1883-5503 ）

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    Authorship：Lead author,　Corresponding author  

    J-GLOBAL

    Other URL： https://ndlsearch.ndl.go.jp/books/R000000004-I033451899

  • Survival of Pathogenic Bacteria: The Molecular Mechanisms of the Heme-responsive Sensor Protein PefR Invited Reviewed

    Hitomi Sawai

    Seibutsu Butsuri   63 ( 2 )   102 - 103   2023.03（ ISSN:0582-4052 ） （ eISSN:1347-4219 ）

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  • Structural basis of heme-responsive sensor protein mediating the survival of hemolytic bacteria Invited Reviewed International coauthorship

    Hitomi Sawai, Yoshitsugu Shiro

    SPring-8/SACLA Research Frontiers 2021   26 - 27   2022.08

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    Authorship：Lead author,　Corresponding author   Publishing type：Research paper (bulletin of university, research institution)   International / domestic magazine：International journal  

  • XFEL Crystal Structures of Peroxidase Compound II Reviewed

    Hanna Kwon, Jaswir Basran, Chinar Pathak, Mahdi Hussain, Samuel L Freeman, Alistair J Fielding, Anna J Bailey, Natalia Stefanou, Hazel A Sparkes, Takehiko Tosha, Keitaro Yamashita, Kunio Hirata, Hironori Murakami, Go Ueno, Hideo Ago, Kensuke Tono, Masaki Yamamoto, Hitomi Sawai, Yoshitsugu Shiro, Hiroshi Sugimoto, Emma Raven, Peter C.E Moody

    Angewandte Chemie International Edition   60 ( 26 )   14578 - 14585   2021.04（ ISSN:1433-7851 ） （ eISSN:1521-3773 ）

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    Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    Oxygen activation in all heme enzymes requires the formation of high oxidation states of iron, usually referred to as ferryl heme. There are two known intermediates: Compound I and Compound II. The nature of the ferryl heme—and whether it is an FeIV=O or FeIV-OH species—is important for controlling reactivity across groups of heme enzymes. The most recent evidence for Compound I indicates that the ferryl heme is an unprotonated FeIV=O species. For Compound II, the nature of the ferryl heme is not unambiguously established. Here, we report 1.06 Å and 1.50 Å crystal structures for Compound II intermediates in cytochrome c peroxidase (CcP) and ascorbate peroxidase (APX), collected using the X-ray free electron laser at SACLA. The structures reveal differences between the two peroxidases. The iron-oxygen bond length in CcP (1.76 Å) is notably shorter than in APX (1.87 Å). The results indicate that the ferryl species is finely tuned across Compound I and Compound II species in closely related peroxidase enzymes. We propose that this fine-tuning is linked to the functional need for proton delivery to the heme.

    DOI： 10.1002/anie.202103010

    PubMed

  • NO Dynamics in Microbial Denitrification System Invited Reviewed

    Takehiko Tosha, Raika Yamagiwa, Hitomi Sawai, Yoshitsugu Shiro

    Chemistry Letters - Highlight Review   50 ( 2 )   280 - 288   2020.11（ ISSN:0366-7022 ） （ eISSN:1348-0715 ）

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    Publishing type：Research paper (scientific journal)  

    Nitric oxide (NO) is generated in some biological systems. Due to its radical character, it exhibits high reactivity, but biological system can manage NO without sustaining any damage to bio-compounds in the cell. As a model system to understand how the NO dynamics is controlled in the cell, we have been studying denitrification of microbial respiration, in which NO is generated as an intermediate product. In denitrification, it was found that NO produced by the NO-generating enzyme (NiR: nitrite reductase) can be smoothly transferred to the NO-decomposing enzyme (NOR: nitric oxide reductase) by making a complex of the two enzymes. The chemical mechanism of the NO decomposition by NOR was also revealed by the time-resolved spectroscopic techniques.

    DOI： 10.1246/CL.200629

  • Integrated bio-metal science: New frontiers of bio-metal science opened with cutting-edge techniques Reviewed

    Hitomi Sawai, Koichiro Ishimori

    Biophysics and Physicobiology   17 ( 0 )   94 - 97   2020（ eISSN:2189-4779 ）

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    Authorship：Lead author,　Corresponding author   Publishing type：Research paper (scientific journal)   International / domestic magazine：Domestic journal  

    DOI： 10.2142/biophysico.bsj-2020017

    PubMed

  • Integrated bio-metal science: New frontiers of bio-metal science opened with cutting-edge techniques Comment

    Hitomi Sawai, Koichiro Ishimori

    BIOPHYSICS AND PHYSICOBIOLOGY   17   94 - 97   2020（ eISSN:2189-4779 ）

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  • Missing piece of two-component signal transduction systems unveiled by SEC-SAXS Invited Reviewed

    Hitomi Sawai, Yoshitsugu Shiro

    SPring-8/SACLA Research Frontiers 2018   30 - 31   2019.08

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    Authorship：Lead author,　Corresponding author  

  • STRUCTURAL BASIS OF ASCORBATE-DEPENDENT IRON REDUCTION BY HUMAN DCYTB INVOLVED IN INTESTINAL IRON ABSORPTION

    Hiroshi Sugimoto, Menega Ganasen, Hiromi Togashi, Hanae Takeda, Yoshitsugu Shiro, Grant Mauk, Hitomi Sawai

    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES   75   E147 - E147   2019（ ISSN:2053-2733 ）

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  • Pseudomonas aeruginosa overexpression system of nitric oxide reductase for in vivo and in vitro mutational analyses Reviewed

    Raika Yamagiwa, Takuya Kurahashi, Mariko Takeda, Mayuho Adachi, Hiro Nakamura, Hiroyuki Arai, Yoshitsugu Shiro, Hitomi Sawai, Takehiko Tosha

    Biochimica et Biophysica Acta - Bioenergetics   1859 ( 5 )   333 - 341   2018.05（ ISSN:1879-2650 ） （ eISSN:1879-2650 ）

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    Authorship：Corresponding author   Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    Membrane-integrated nitric oxide reductase (NOR) reduces nitric oxide (NO) to nitrous oxide (N2O) with protons and electrons. This process is essential for the elimination of the cytotoxic NO that is produced from nitrite (NO2 −) during microbial denitrification. A structure-guided mutagenesis of NOR is required to elucidate the mechanism for NOR-catalyzed NO reduction. We have already solved the crystal structure of cytochrome c-dependent NOR (cNOR) from Pseudomonas aeruginosa. In this study, we then constructed its expression system using cNOR-gene deficient and wild-type strains for further functional study. Characterizing the variants of the five conserved Glu residues located around the heme/non-heme iron active center allowed us to establish how the anaerobic growth rate of cNOR-deficient strains expressing cNOR variants correlates with the in vitro enzymatic activity of the variants. Since bacterial strains require active cNOR to eliminate cytotoxic NO and to survive under denitrification conditions, the anaerobic growth rate of a strain with a cNOR variant is a good indicator of NO decomposition capability of the variants and a marker for the screening of functionally important residues without protein purification. Using this in vivo screening system, we examined the residues lining the putative proton transfer pathways for NO reduction in cNOR, and found that the catalytic protons are likely transferred through the Glu57 located at the periplasmic protein surface. The homologous cNOR expression system developed here is an invaluable tool for facile identification of crucial residues in vivo, and for further in vitro functional and structural studies.

    DOI： 10.1016/j.bbabio.2018.02.009

    PubMed

  • Roles of N- and C-terminal domains in the ligand-binding properties of cytoglobin Reviewed

    Shumpei Hanai, Hirofumi Tsujino, Taku Yamashita, Ryo Torii, Hitomi Sawai, Yoshitsugu Shiro, Koji Oohora, Takashi Hayashi, Tadayuki Uno

    Journal of Inorganic Biochemistry   179   1 - 9   2018.02（ ISSN:1873-3344 ） （ eISSN:1873-3344 ）

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    Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    Cytoglobin (Cygb) is a member of the hexacoordinated globin protein family and is expressed ubiquitously in rat and human tissues. Although Cygb is reportedly upregulated under hypoxic conditions both in vivo and in vitro, suggesting a physiological function to protect cells under hypoxic/ischemic conditions by scavenging reactive oxygen species or by signal transduction, the mechanisms associated with this function have not been fully elucidated. Recent studies comparing Cygbs among several species suggest that mammalian Cygbs show a distinctly longer C-terminal domain potentially involved in unique physiological functions. In this study, we prepared human Cygb mutants (ΔC, ΔN, and ΔNC) with either one or both terminal domains truncated and investigated the enzymatic functions and structural features by spectroscopic methods. Evaluation of the superoxide-scavenging activity between Cygb variants showed that the ΔC and ΔNC mutants exhibited slightly higher activity involving superoxide scavenging as compared with wild-type Cygb. Subsequent experiments involving ligand titration, flash photolysis, and resonance Raman spectroscopic studies suggested that the truncation of the C- and N-terminal domains resulted in less effective to dissociation constants and binding rates for carbon monoxide, respectively. Furthermore, structural stability was assessed by guanidine hydrochloride and revealed that the C-terminal domain might play a vital role in improving structure, whereas the N-terminal domain did not exert a similar effect. These findings indicated that long terminal domains could be important not only in regulating enzymatic activity but also for structural stability, and that the domains might be relevant to other hypothesized physiological functions for Cygb.

    DOI： 10.1016/j.jinorgbio.2017.11.003

    PubMed

    Other URL： http://orcid.org/0000-0002-0714-8337

  • CHAPTER 3: Haem-based Sensors of Dioxygen Invited Reviewed

    Hitomi Sawai, Yoshitsugu Shiro

    RSC Metallobiology   2018- ( 11 )   47 - 83   2018（ ISSN:2045-547X ）

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    Publishing type：Part of collection (book)  

    Dioxygen (molecular oxygen, O2) is a dominant environmental molecule that affects the metabolic, physiological, and behavioural responses of living organisms, from micro-organisms to human. The regulation of biological systems requires all living organisms to be able to sense the environmental O2 concentration with O2-sensing protein systems or O2-sensor proteins. This chapter focuses on the haem-based O2 sensor in bacteria, archaea, nematodes and insects, and describes the mechanisms of O2 sensing (input) and subsequent functional expression (output) of these systems. The haem-based O2 sensors are the best characterized among all gas-sensor proteins. They contain a haem molecule in their sensor domains and can combine with O2 reversibly. Generally, the sensor domain is linked to regulator domains with various biological functions (e.g., histidine kinase, methyl accepting chemotaxis protein, diguanylate cyclase, phosphodiesterase, guanylate/adenylate cyclases) to transduce the signal into a specific output. In Section 3.2, the properties of general types of sensor domains are described, and the characteristics of each type of haem-based O2-sensor protein are explained in terms of each output function including issues on the studies of these proteins in Sections 3.3-3.6.

    DOI： 10.1039/9781788012836-00047

    Other URL： http://orcid.org/0000-0002-0714-8337

  • INTRA- AND INTER-MOLECULAR SIGNAL TRANSDUCTION MECHANISMS OF HEME SENSING SYSTEMS

    Hitomi Sawai, Gareth S. A. Wright, Akane Saeki, Takaaki Hikima, Masaki Yamamoto, Svetlana Antonyuk, S. Samar Hasnain, Yoshitsugu Shiro

    AMERICAN JOURNAL OF HEMATOLOGY   92 ( 8 )   E463 - E463   2017.08（ ISSN:0361-8609 ） （ eISSN:1096-8652 ）

  • STRUCTURAL INSIGHTS INTO ASCORBATE-DEPENDENT FERRIREDUCTASE, DCYTB, IN HUMAN

    Menega Ganasen, Hitomi Sawai, Hiromi Togashi, Hanae Takeda, Yoshitsugu Shiro, Hiroshi Sugimoto

    AMERICAN JOURNAL OF HEMATOLOGY   92 ( 8 )   E464 - E464   2017.08（ ISSN:0361-8609 ） （ eISSN:1096-8652 ）

  • Heme-Binding Properties of HupD Functioning as a Substrate-Binding Protein in a Heme-Uptake ABC-Transporter System in Listeria monocytogenes Reviewed

    Yasunori Okamoto, Hitomi Sawai, Mariko Ogura, Takeshi Uchida, Koichiro Ishimori, Takashi Hayashi, Shigetoshi Aono

    BULLETIN OF THE CHEMICAL SOCIETY OF JAPAN   87 ( 10 )   1140 - 1146   2014.10（ ISSN:0009-2673 ） （ eISSN:1348-0634 ）

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    Publishing type：Research paper (scientific journal)  

    The HupDCG protein complex is a putative ABC-transporter for heme in the pathogenic Gram-positive bacterium Listeria monocytogenes, where HupD functions as a heme-binding protein. UV-vis absorption, EPR, and resonance Raman spectroscopy have revealed that HupD binds a heme with two histidine residues as the axial ligands. His105 and His259 are identified as the axial ligands by site-directed mutagenesis. HupD is the first example of a heme-binding protein having a bis-histidine coordination environment among the heme-binding proteins working in bacterial heme acquisition systems. While mutation of His259 to Ala resulted in a loss in the heme-binding ability of HupD, the H105A variant of HupD retained its heme-binding ability with lower heme-binding affinity compared with the wild type. These results suggest that His259 is an essential ligand for heme acquisition by HupD and that His105 might be responsible for regulation of the heme-binding affinity of HupD during the heme-transport process.

    DOI： 10.1246/bcsj.20140166

    Other URL： http://orcid.org/0000-0002-0714-8337

  • Disulfide bonds regulate binding of exogenous ligand to human cytoglobin Reviewed

    Hirofumi Tsujino, Taku Yamashita, Azusa Nose, Kaori Kukino, Hitomi Sawai, Yoshitsugu Shiro, Tadayuki Uno

    JOURNAL OF INORGANIC BIOCHEMISTRY   135   20 - 27   2014.06（ ISSN:0162-0134 ） （ eISSN:1873-3344 ）

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    Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    Cytoglobin (Cgb) was discovered a decade ago and is a fourth member of the group of hexacoordinated globinfolded proteins. Although some crystal structures have been reported and several functions have been proposed for Cgb, its physiological role remains uncertain. In this study, we measured cyanide binding to the ferric state of the wild-type (WT) Cgb, and found that the binding consisted of multiple steps. These results indicated that Cgb may be comprised of several forms, and the presence of monomers, dimers, and tetramers was subsequently confirmed by SDS-PAGE. Remarkably, each species contained two distinguishable forms, and, in the monomer, analyses of alternative cysteine states suggested the presence of an intramolecular disulfide bond (monomer SS form) and a structure with unpaired thiol groups (monomer SH form). These confirmed that forms were separated by gel-exclusion chromatography, and that the cyanide binding of the separated fractions was again measured; they showed different affinities for cyanide, with the monomer fraction showing the highest affinity. In addition, the ferrous state in each fraction showed distinct carbon monoxide (CO)-binding properties, and the affinities for cyanide and CO suggested a linear correlation. Furthermore, we also prepared several variants involving the two cysteine residues. The C38S and C83S variants showed a binding affinity for cyanide similar to the value for the monomer SH form, and hence the fraction with the highest affinity for exogenous ligands was designated as a monomer SS form. We concluded that polymerization could be a mechanism that triggers the exertion of various physiological functions of this protein and that an appropriate disulfide bond between the two cysteine residues was critical for regulating the binding affinity of Cgb, which can act as a ROS scavenger, for exogenous ligands. (C) 2014 Elsevier Inc. All rights reserved.

    DOI： 10.1016/j.jinorgbio.2014.02.011

    PubMed

  • TRANSCRIPTIONAL REGULATION OF HEME HOMEOSTASIS IN LACTOCOCCUS LACTIS

    Shigetoshi Aono, Hitomi Sawai, Masaru Yamanaka, Hiroshi Sugimoto, Yoshitsugu Shiro

    AMERICAN JOURNAL OF HEMATOLOGY   88 ( 5 )   E21 - E22   2013.05（ ISSN:0361-8609 ）

  • Structural Basis for the Transcriptional Regulation of Heme Homeostasis in Lactococcus lactis Reviewed

    Hitomi Sawai, Masaru Yamanaka, Hiroshi Sugimoto, Yoshitsugu Shiro, Shigetoshi Aono

    JOURNAL OF BIOLOGICAL CHEMISTRY   287 ( 36 )   30755 - 30768   2012.08（ ISSN:0021-9258 ） （ eISSN:1083-351X ）

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    Authorship：Lead author   Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    Although heme is a crucial element for many biological processes including respiration, heme homeostasis should be regulated strictly due to the cytotoxicity of free heme molecules. Numerous lactic acid bacteria, including Lactococcus lactis, acquire heme molecules exogenously to establish an aerobic respiratory chain. A heme efflux system plays an important role for heme homeostasis to avoid cytotoxicity of acquired free heme, but its regulatory mechanism is not clear. Here, we report that the transcriptional regulator heme-regulated transporter regulator (HrtR) senses and binds a heme molecule as its physiological effector to regulate the expression of the heme-efflux system responsible for heme homeostasis in L. lactis. To elucidate the molecular mechanisms of how HrtR senses a heme molecule and regulates gene expression for the heme efflux system, we determined the crystal structures of the apo-HrtR.DNA complex, apo-HrtR, and holo-HrtR at a resolution of 2.0, 3.1, and 1.9 angstrom, respectively. These structures revealed that HrtR is a member of the TetR family of transcriptional regulators. The residue pair Arg-46 and Tyr-50 plays a crucial role for specific DNA binding through hydrogen bonding and a CH-pi interaction with the DNA bases. HrtR adopts a unique mechanism for its functional regulation upon heme sensing. Heme binding to HrtR causes a coil-to-helix transition of the alpha 4 helix in the heme-sensing domain, which triggers a structural change of HrtR, causing it to dissociate from the target DNA for derepression of the genes encoding the heme efflux system. HrtR uses a unique heme-sensing motif with bis-His (His-72 and His-149) ligation to the heme, which is essential for the coil-to-helix transition of the alpha 4 helix upon heme sensing.

    DOI： 10.1074/jbc.M112.370916

    PubMed

  • Site-specific Protein Dynamics in Communication Pathway from Sensor to Signaling Domain of Oxygen Sensor Protein, HemAT-Bs TIME-RESOLVED ULTRAVIOLET RESONANCE RAMAN STUDY Reviewed OA

    Samir F. El-Mashtoly, Minoru Kubo, Yuzong Gu, Hitomi Sawai, Satoru Nakashima, Takashi Ogura, Shigetoshi Aono, Teizo Kitagawa

    JOURNAL OF BIOLOGICAL CHEMISTRY   287 ( 24 )   19973 - 19984   2012.06（ ISSN:0021-9258 ） （ eISSN:1083-351X ）

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    Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    HemAT-Bs is a heme-based signal transducer protein responsible for aerotaxis. Time-resolved ultraviolet resonance Raman (UVRR) studies of wild-type and Y70F mutant of the full-length HemAT-Bs and the truncated sensor domain were performed to determine the site-specific protein dynamics following carbon monoxide (CO) photodissociation. The UVRR spectra indicated two phases of intensity changes for Trp, Tyr, and Phe bands of both full-length and sensor domain proteins. The W16 and W3 Raman bands of Trp, the F8a band of Phe, and the Y8a band of Tyr increased in intensity at hundreds of nanoseconds after CO photodissociation, and this was followed by recovery in similar to 50 mu s. These changes were assigned to Trp-132 (G-helix), Tyr-70 (B-helix), and Phe-69 (B-helix) and/or Phe-137 (G-helix), suggesting that the change in the heme structure drives the displacement of B- and G-helices. The UVRR difference spectra of the sensor domain displayed a positive peak for amide I in hundreds of nanoseconds after photolysis, which was followed by recovery in similar to 50 mu s. This difference band was absent in the spectra of the full-length protein, suggesting that the isolated sensor domain undergoes conformational changes of the protein backbone upon CO photolysis and that the changes are restrained by the signaling domain. The time-resolved difference spectrum at 200 mu s exhibited a pattern similar to that of the static (reduced - CO) difference spectrum, although the peak intensities were much weaker. Thus, the rearrangements of the protein moiety toward the equilibrium ligand-free structure occur in a time range of hundreds of microseconds.

    DOI： 10.1074/jbc.M112.357855

    PubMed

    Other URL： http://orcid.org/0000-0002-0714-8337

  • Structural basis for oxygen sensing and signal transduction of the heme-based sensor protein Aer2 from Pseudomonas aeruginosa Reviewed

    Hitomi Sawai, Hiroshi Sugimoto, Yoshitsugu Shiro, Haruto Ishikawa, Yasuhisa Mizutani, Shigetoshi Aono

    CHEMICAL COMMUNICATIONS   48 ( 52 )   6523 - 6525   2012（ ISSN:1359-7345 ） （ eISSN:1364-548X ）

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    Authorship：Lead author   Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    The crystal structure of a truncated Aer2, a signal transducer protein from Pseudomonas aeruginosa, consisting of the heme-containing PAS and di-HAMP domains revealed that a distal tryptophan residue (Trp283) plays an important role in stabilizing the heme-bound O-2 and intra-molecular signal transduction upon O-2 binding.

    DOI： 10.1039/c2cc32549g

    PubMed

    Other URL： http://orcid.org/0000-0002-0714-8337

  • Aldoxime Dehydratase: Probing the Heme Environment Involved in the Synthesis of the Carbon-Nitrogen Triple Bond Reviewed

    Eftychia Pinakoulaki, Constantinos Koutsoupakis, Hitomi Sawai, Andrea Pavlou, Yasuo Kato, Yasuhisa Asano, Shigetoshi Aono

    JOURNAL OF PHYSICAL CHEMISTRY B   115 ( 44 )   13012 - 13018   2011.11（ ISSN:1520-6106 ） （ eISSN:1520-5207 ）

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    Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    Fourier transform infrared (FTIR) spectra, "light" minus "dark" difference FTIR spectra, and time-resolved step-scan (TRS2) FTIR spectra are reported for carbonmonoxy aldoxime dehydratase. Two C-O modes of heme at 1945 and 1964 cm(-1) have been identified and remained unchanged in H2O/D2O exchange and in the pH 5.6-8.5 range, suggesting the presence of two conformations at the active site. The observed C-O frequencies are 5 and 16 cm(-1) lower and higher, respectively, than that obtained previously (Oinuma, K-I.; et al. FEBS Lett. 2004, 568, 44-48). We suggest that the strength of the Fe-His bond and the neutralization of the negatively charged propionate groups modulate the v(Fe-CO)/v(CO) back-bonding correlation. The "light" minus "dark" difference FTIR spectra indicate that the heme propionates are in both the protonated and deprotonated forms, and the photolyzed CO becomes trapped within a ligand docking site (v(CO) = 2138 cm(-1)). The TRS2-FTIR spectra show that the rate of recombination of CO to the heme is k(1945) (cm-1) = 126 +/- 20 s(-1) and k(1964) (cm-1) = 122 +/- 20 s(-1) at pH 5.6, and k(1945) (cm-1) = 148 +/- 30 s(-1) and k(1964) (cm-1) = 158 +/- 32 s(-1) at pH 8.5. The rate of decay of the heme propionate vibrations is on a time scale coincident with the rate of rebinding, suggesting that there is a coupling between ligation dynamics in the distal heme environment and the environment sensed by the heme propionates. The implications of these results with respect to the proximal His-Fe heme environment including the propionates and the positively charged or proton-donating residues in the distal pocket which are crucial for the synthesis of nitriles are discussed.

    DOI： 10.1021/jp205944e

    PubMed

    Other URL： http://orcid.org/0000-0002-0714-8337

  • Crystal structure of the carbon monoxide complex of human cytoglobin Reviewed

    Masatomo Makino, Hitomi Sawai, Yoshitsugu Shiro, Hiroshi Sugimoto

    PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS   79 ( 4 )   1143 - 1153   2011.04（ ISSN:0887-3585 ） （ eISSN:1097-0134 ）

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    Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    Cytoglobin (Cgb) is a vertebrate heme-containing globin-protein expressed in a broad range of mammalian tissues. Unlike myoglobin, Cgb displays a hexa-coordinated (bis-hystidyl) heme iron atom, having the heme distal His81(E7) residue as the endogenous sixth ligand. In the present study, we crystallized human Cgb in the presence of a reductant Na2S2O4 under a carbon monoxide (CO) atmosphere, and determined the crystal structure at 2.6 angstrom resolution. The CO ligand occupies the sixth axial position of the heme ferrous iron. Eventually, the imidazole group of His81(E7) is expelled from the sixth position and swings out of the distal heme pocket. The flipping motion of the His81 imidazole group accompanies structural readjustments of some residues (Gln62, Phe63, Gln72, and Ser75) in both the CD-corner and D-helix regions of Cgb. On the other hand, no significant structural changes were observed in other Cgb regions, for example, on the proximal side. These structural alterations that occurred as a result of exogenous ligand (CO) binding are clearly different from those observed in other vertebrate hexa-coordinated globins (mouse neuroglobin, Drosophila melanogaster hemoglobin) and penta-coordinated sperm whale myoglobin. The present study provides the structural basis for further discussion of the unique ligand-binding properties of Cgb.

    DOI： 10.1002/prot.22950

    PubMed

    Other URL： http://orcid.org/0000-0002-0714-8337

  • Molecular oxygen regulates the enzymatic activity of a heme-containing diguanylate cyclase (HemDGC) for the synthesis of cyclic di-GMP Reviewed

    Hitomi Sawai, Shiro Yoshioka, Takeshi Uchida, Mamoru Hyodo, Yoshihiro Hayakawa, Koichiro Ishimori, Shigetoshi Aono

    BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS   1804 ( 1 )   166 - 172   2010.01（ ISSN:1570-9639 ） （ eISSN:1878-1454 ）

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    Authorship：Lead author   Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    We have studied the structural and enzymatic properties of a diguanylate cyclase from an obligatory anaerobic bacterium Desulfotalea psychrophila, which consists of the N-terminal sensor domain and the C-terminal diguanylate cyclase domain. The sensor domain shows an amino acid sequence homology and spectroscopic properties similar to those of the sensor domains of the globin-coupled sensor proteins containing a protoheme. This heme-containing diguanylate cyclase catalyzes the formation of cyclic di-GMP from GTP only when the heme in the sensor domain binds molecular oxygen. When the heme is in the ferric, deoxy, CO-bound, or NO-bound forms, no enzymatic activity is observed. Resonance Raman spectroscopy reveals that Tyr55 forms a hydrogen bond with the heme-bound O(2), but not with CO. Instead, Gln81 interacts with the heme-bound CO. These differences of a hydrogen bonding network will play a crucial role for the selective O(2) sensing responsible for the regulation of the enzymatic activity. (C) 2009 Elsevier B.V. All rights reserved.

    DOI： 10.1016/j.bbapap.2009.09.028

    PubMed

    Other URL： http://orcid.org/0000-0002-0714-8337

  • X-ray Crystal Structure of Michaelis Complex of Aldoxime Dehydratase Reviewed OA

    Hitomi Sawai, Hiroshi Sugimoto, Yasuo Kato, Yasuhisa Asano, Yoshitsugu Shiro, Shigetoshi Aono

    JOURNAL OF BIOLOGICAL CHEMISTRY   284 ( 46 )   32089 - 32096   2009.11（ ISSN:0021-9258 ） （ eISSN:1083-351X ）

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    Authorship：Lead author   Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    Aldoxime dehydratase (Oxd) catalyzes the dehydration of aldoximes (R-CH=N-OH) to their corresponding nitrile (R-C N). Oxd is a heme-containing enzyme that catalyzes the dehydration reaction as its physiological function. We have determined the first two structures of Oxd: the substrate-free OxdRE at 1.8 angstrom resolution and the n-butyraldoxime- and propionaldoxime-bound OxdREs at 1.8 and 1.6 angstrom resolutions, respectively. Unlike other heme enzymes, the organic substrate is directly bound to the heme iron in OxdRE. We determined the structure of the Michaelis complex of OxdRE by using the unique substrate binding and activity regulation properties of Oxd. The Michaelis complex was prepared by x-ray cryoradiolytic reduction of the ferric dead-end complex in which Oxd contains a Fe(3+) heme form. The crystal structures reveal the mechanism of substrate recognition and the catalysis of OxdRE.

    DOI： 10.1074/jbc.M109.018762

    PubMed

    Other URL： http://orcid.org/0000-0002-0714-8337

  • Effect of dimerization on the regulation of gas binding to human cytoglobin

    Tadayuki Uno, Azusa Nose, Kaori Kukino, Yoshikazu Tomisugi, Hiroshi Aoyama, Norifumi Kawada, Katsutoshi Yoshizato, Hitomi Sawai, Yoshitsugu Shiro

    YAKUGAKU ZASSHI-JOURNAL OF THE PHARMACEUTICAL SOCIETY OF JAPAN   128   56 - 56   2008（ ISSN:0031-6903 ）

  • Structure and function of a globin-coupled enzyme that catalyzes the formation of a bacterial second messenger, c-di-GMP

    Shigetoshi Aono, Shiro Yoshioka, Hitomi Sawai

    YAKUGAKU ZASSHI-JOURNAL OF THE PHARMACEUTICAL SOCIETY OF JAPAN   128   42 - 42   2008（ ISSN:0031-6903 ）

  • High-resolution structure of human cytoglobin: identification of extra N- and C-termini and a new dimerization mode Reviewed

    M Makino, H Sugimoto, H Sawai, N Kawada, K Yoshizato, Y Shiro

    ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY   62 ( 6 )   671 - 677   2006.06（ ISSN:0907-4449 ） （ eISSN:1399-0047 ）

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    Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    Cytoglobin ( Cgb) is a recently discovered member of the vertebrate haem-containing globin family. The structure of a new crystal form of wild-type human Cgb ( space group C2) was determined at a resolution of 1.68 (A) over circle. The results show the presence of an additional helix in the N-terminal residues ( 4-20) prior to the A helix and an ordered loop structure in the C-terminal region ( 168-188), while these extended peptides were invisible owing to disorder in the previously reported structures using a P3(2)21 crystal at a resolution of 2.4 (A) over circle. A detailed comparison of the two crystal structures shows differences in the conformation of the residues ( i.e. Arg84) in the haem environment owing to a different dimeric arrangement.

    DOI： 10.1107/S0907444906013813

    PubMed

    Other URL： http://orcid.org/0000-0002-0714-8337

  • 1P162 Exogenous Ligand Binding Mechanism of Cytoglobin(5. Heme protein,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

    Uno Tadayuki, Kukino Kaori, Maeda Hatsuo, Tomisugi Yoshikazu, Ishikawa Yoshinobu, Kawada Norifumi, Yoshizato Katsutoshi, Sawai Hitomi, Shiro Yoshitsugu

    Seibutsu Butsuri   46 ( 2 )   S187   2006

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  • High Resolution Structure of Cytoglobin Reveals the Extra Helix in N-terminus

    Masatomo Makino, Hiroshi Sugimoto, Hitomi Sawai, Norihumi Kawada, Katsutoshi Yoshizato, Yoshitsugu Shiro

    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES   61   C215 - C215   2005（ ISSN:2053-2733 ）

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  • Structural Characterization of the Proximal and Distal Histidine Environment of Cytoglobin and Neuroglobin Reviewed

    SAWAI Hitomi, SAWAI Hitomi, MAKINO Masatomo, MAKINO Masatomo, MIZUTANI Yasuhisa, OHTA Takehiro, SUGIMOTO Hiroshi, UNO Tadayuki, KAWADA Norifumi, YOSHIZATO Katsutoshi, YOSHIZATO Katsutoshi, KITAGAWA Teizo, SHIRO Yoshitsugu

    Biochemistry   44 ( 40 )   13257 - 13265   2005（ ISSN:0006-2960 ）

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    Authorship：Lead author   Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    Cytoglobin (Cgb) and neuroglobin (Ngb) are the first examples of hexacoordinated globins from humans and other vertebrates in which a histidine (His) residue at the sixth position of the heme iron is an endogenous ligand in both the ferric and ferrous forms. Static and time-resolved resonance Raman and FT-IR spectroscopic techniques were applied in examining the structures in the heme environment of these globins. Picosecond time-resolved resonance Raman (ps-TR3) spectroscopy of transient five-coordinate heme species produced by the photolysis of carbon monoxide (CO) adducts of Cgb and Ngb showed Fe-His stretching (VFe-His) bands at 229 and 221 cm(-1), respectively. No time-dependent shift in the VFe-His band of Cgb and Ngb was detected in the 20-1000 ps time domain, in contrast to the case of myoglobin (Mb). These spectroscopic data, combined with previously reported crystallographic data, suggest that the structure of the heme pocket in Cgb and Ngb is altered upon CO binding in a manner different from that of Mb and that the scales of the structural alteration are different for Cgb and Ngb. The structural property of the heme distal side of the ligand-bound forms was investigated by observing the sets of (v(Fe-CO), v(C-O), delta(Fe-C-O)) and (v(Fe-NO), v(N-O), delta(Fe-N-O)) for the CO and nitric oxide (NO) complexes of Cgb and Ngb. A comparison of the spectra of some distal mutants of Cgb (H81A, H81V, R84A, R84K, and R84T) and Ngb (H64A, H64V, K67A, K67R, and K67T) showed that the CO adducts of Cgb and Ngb contained three conformers and that the distal His (His81 in Cgb and His64 in Ngb) mainly contributes to the interconversion of the conformers. These structural characteristics of Cgb and Ngb are discussed in relation to their ligand binding and physiological properties.

    DOI： 10.1021/bi050997o

    PubMed

    J-GLOBAL

    Other URL： http://orcid.org/0000-0002-0714-8337

  • Structural basis of human cytoglobin for ligand binding Reviewed

    H Sugimoto, M Makino, H Sawai, N Kawada, K Yoshizato, Y Shiro

    JOURNAL OF MOLECULAR BIOLOGY   339 ( 4 )   873 - 885   2004.06（ ISSN:0022-2836 ） （ eISSN:1089-8638 ）

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    Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    Cytoglobin (Cgb), a newly discovered member of the vertebrate globin family, binds O-2 reversibly via its heme, as is the case for other mammalian globins (hemoglobin (Hb), myoglobin (Mb) and neuroglobin (Ngb)). While Cgb is expressed in various tissues, its physiological role is not clearly understood. Here, the X-ray crystal structure of wild type human Cgb in the ferric state at 2.4 Angstrom resolution is reported. In the crystal structure, ferric Cgb is dimerized through two intermolecular disulfide bonds between Cys38(B2) and Cys83(E9), and the dimerization interface is similar to that of lamprey Hb and Ngb. The overall backbone structure of the Cgb monomer exhibits a traditional globin fold with a three-over-three a-helical sandwich, in which the arrangement of helices is basically the same among all globins studied to date. A detailed comparison reveals that the backbone structure of the CD corner to D helix region, the N terminus of the E-helix and the F-helix of Cgb resembles more closely those of pentacoordinated globins (Mb, lamprey Hb), rather than hexa-coordinated globins (Ngb, rice Hb). However, the His81(E7) imidazole group coordinates directly to the heme iron as a sixth axial ligand to form a hexcoordinated heme, like Ngb and rice Hb. The position and orientation of the highly conserved residues in the heme pocket (Phe(CD1), Val(E11), distal His(E7) and proximal His(F8)) are similar to those of other globin proteins. Two alternative conformations of the Arg84(E10) guanidium group were observed, suggesting that it participates in ligand binding to Cgb, as is the case for Arg(E10) of Aplysia Mb and Lys(E10) of Ngb. The structural diversities and similarities among globin proteins are discussed with relevance to molecular evolutionary relationships. (C) 2004 Elsevier Ltd. All rights reserved.

    DOI： 10.1016/j.jmb.2004.04.024

    PubMed

    Other URL： http://orcid.org/0000-0002-0714-8337

  • Characterization of the heme environmental structure of cytoglobin, a fourth globin in humans Reviewed

    H Sawai, N Kawada, K Yoshizato, H Nakajima, S Aono, Y Shiro

    BIOCHEMISTRY   42 ( 17 )   5133 - 5142   2003.05（ ISSN:0006-2960 ）

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    Authorship：Lead author   Publishing type：Research paper (scientific journal)   International / domestic magazine：International journal  

    Cytoglobin (Cgb) represents a fourth member of the globin superfamily in mammals, but its function is unknown. Site-directed mutagenesis, in which six histidine residues were replaced with alanine, was carried out, and the results indicate that the imidazoles of His81 (E7) and His113 (F8) bind to the heme iron as axial ligands in the hexacoordinate and the low-spin state. The optical absorption, resonance Raman, and IR spectral results are consistent with this conclusion. The redox potential measurements revealed an E' of 20 mV (vs NHE) in the ferric/ferrous couple, indicating that the imidazole ligands of His81 and His 113 are electronically neutral. On the basis of the upsilon(Fe-CO) and upsilon(C-O) values in the resonance Raman and infrared spectra of the ferrous-CO complexes of Cgb and its mutants, it was found that CO binds to the ferrous iron after the His8l imidazole is dissociated, and three conformers are present in the resultant CO coordination structure. Two are in closed conformations of the heme pocket, in which the bound CO ligand interacts with the dissociated His81 imidazole, while the third is in an open conformation. The upsilon(Fe-O2) in the resonance Raman spectra of oxy Cgb can be observed at 572 cm(-1), suggesting a polar heme environment. These structural properties of the heme pocket of Cgb are discussed with respect to its proposed in vivo oxygen storage function.

    DOI： 10.1021/bi027067e

    PubMed

    Other URL： http://orcid.org/0000-0002-0714-8337

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Books and Other Publications

  • Gas Sensing in Cells Reviewed International journal

    Hitomi Sawai, Yoshitsugu Shiro（ Role： Contributor ,  Chapter 3: Heme-Based Sensors of Dioxygen）

    Royal Society of Chemistry  2017.11 

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    Total pages：303   Responsible for pages：47-83   Book type：Scholarly book Participation form：First Author

  • 生命金属ダイナミクス : 生体内における金属の挙動と制御 Reviewed

    城 宜嗣、澤井 仁美、當舎 武彦（ Role： Contributor ,  第4章 維持 -分子- 第2節 生体鉄の分子科学と細胞生物学）

    エヌ・ティー・エス  2021.01  （ ISBN:9784860437060 ）

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    Total pages：564   Responsible for pages：126-138   Book type：Scholarly book Participation form：Second Author

  • Iron in Biology: Molecular Structures, Cellular Processes and Living Systems Reviewed

    Yoshitsugu Shiro, Hitomi Sawai, Takehiko Tosha（ Role： Edit）

    Royal Society of Chemistry  2025.06  （ ISBN:9781837677986 ）

  • Iron in Biology: Molecular Structures, Cellular Processes and Living Systems Reviewed

    Hitomi Sawai, Hiroshi Sugimoto, Yoshitsugu Shiro（Chapter 6 - Iron Absorption in Human Duodenum by Dcytb and DMT1）

    Royal Society of Chemistry  2025.06  （ ISBN:9781837677986 ）

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    Book type：Scholarly book Participation form：Corresponding Author

  • Iron in Biology: Molecular Structures, Cellular Processes and Living Systems Reviewed

    Izumi Yanatori, Hitomi Sawai（ Role： Contributor ,  Chapter 1 - Introduction to Iron Dynamics in Human Cells: Fundamental Mechanisms and Recent Developments ）

    Royal Society of Chemistry  2025.06 

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    Book type：Scholarly book Participation form：Second Author

  • ヘムタンパク質の科学 生理機能の理解とその展開に向けて Reviewed

    澤井仁美（ Role： Contributor ,  第3章 情報変換：情報伝達に関与するヘムタンパク質 第2節シグナル分子として機能するヘム）

    エヌ・ティー・エス  2022.05  （ ISBN:9784860437787 ）

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    Total pages：472   Book type：Scholarly book

  • ヘムタンパク質の科学 生理機能の理解とその展開に向けて Reviewed

    澤井仁美（ Role： Contributor ,  第3章 情報変換：情報伝達に関与するヘムタンパク質 第2節シグナル分子として機能するヘム）

    エヌ・ティー・エス  2022.05 

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    Total pages：472   Responsible for pages：121-128   Book type：Scholarly book Participation form：Corresponding Author

  • ヘムタンパク質の科学 : 生理機能の理解とその展開に向けて Reviewed

    澤井仁美（ Role： Contributor ,  第4章ヘム輸送とヘム代謝 第3節金属イオンの取り込みに関与するヘム含有酵素）

    エヌ・ティー・エス  2022.05  （ ISBN:9784860437787 ）

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    Total pages：472   Responsible for pages：169-180   Book type：Scholarly book Participation form：Corresponding Author

  • 生命金属ダイナミクス : 生体内における金属の挙動と制御 Reviewed

    城宜嗣, 澤井仁美, 當舎武彦（ Role： Contributor ,  第4章 維持 -分子- 第2節 生体鉄の分子科学と細胞生物学 (126-138ページ)）

    エヌ・ティー・エス  2021.01  （ ISBN:9784860437060 ）

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    Total pages：564   Responsible for pages：126-138   Book type：Scholarly book

    CiNii Books

  • Gas Sensing in Cells Reviewed International journal

    Hitomi Sawai, Yoshitsugu Shiro（ Role： Contributor ,  Chapter 3: Heme-Based Sensors of Dioxygen, pp. 47-83）

    Royal Society of Chemistry  2017.11  （ ISBN:9781782628958 ）

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    Total pages：303   Book type：Scholarly book

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MISC

  • 分子研で生きている細胞の金属動態を探る

    澤井 仁美

    分子研レターズ   90   19 - 20   2024.09

  • 【生命現象を駆動する生体内金属動態の理解と展開】細胞が金属種を選別して取り込むメカニズム　膜貫通型鉄還元酵素Dcytbの構造機能解析により明らかになった細胞への鉄取り込みメカニズム

    澤井 仁美

    生体の科学   75 ( 2 )   112 - 115   2024.04（ ISSN:0370-9531 ）

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    ＜文献概要＞鉄はすべての生物の生命維持に必須の金属元素であるため,鉄なしで生きていける生物はいない。ヒトは食物に含まれる鉄イオンやヘム鉄などを栄養素として小腸上部(十二指腸)の粘膜上皮細胞から吸収し,酸素の運搬貯蔵,エネルギー産生,物質代謝などの重要な生理機能をつかさどる酵素などの活性中心として活用している。本稿では,筆者らが明らかにした膜貫通型鉄還元酵素(duodenal cytochrome b;Dcytb)の構造と機能を中心に,鉄栄養素としての鉄イオンの取り込み機構について概説する。

  • 生体内におけるヘムおよび鉄イオンの動態と制御について

    澤井 仁美

    人工血液   32 ( 1 )   13 - 13   2024（ ISSN:1341-1594 ）

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  • Differences of the iron acquisition mechanisms of plants and animals at the molecular level

    澤井仁美

    日本植物生理学会年会(Web)   65th   2024

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  • Mechanism of iron uptake into cells revealed by structural and functional analysis of the transmembrane iron reductase Dcytb

    澤井仁美

    生体の科学   75 ( 2 )   112 - 115   2024（ ISSN:0370-9531 ） （ eISSN:1883-5503 ）

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  • Molecular Science for Good Health by Iron Uptake

    澤井仁美

    日本農芸化学会大会講演要旨集(Web)   2024   2024（ ISSN:2186-7976 ）

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  • 鉄還元機能を持つ6回膜貫通型タンパク質101F6の大腸菌での発現と機能解析

    阪口 智哉, 澤井 仁美, 城 宜嗣, 鍔木 基成, 當舎 武彦, 木村 哲就, 杉本 宏

    日本生化学会大会プログラム・講演要旨集   96回   [2P - 656]   2023.10

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  • 細胞内鉄輸送に関わる鉄シャペロンと鉄貯蔵タンパク質の複合体形成の分子機構

    佐藤 渚, 浦 敦人, 簗取 いずみ, 當舎 武彦, 城 宜嗣, 澤井 仁美

    日本生化学会大会プログラム・講演要旨集   96回   [2P - 193]   2023.10

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  • 病原菌の生存戦略 ヘム濃度センサータンパク質PefRの作動メカニズム

    澤井 仁美

    生物物理   63 ( 2 )   102 - 103   2023.03（ ISSN:0582-4052 ） （ eISSN:1347-4219 ）

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  • 病原菌の生存戦略 ヘム濃度センサータンパク質PefRの作動メカニズム International journal

    澤井 仁美

    生物物理   63 ( 2 )   102 - 103   2023.03（ ISSN:0582-4052 ） （ eISSN:1347-4219 ）

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  • 蛋白質間相互作用による鉄ホメオスタシスの制御

    澤井仁美

    日本蛋白質科学会年会プログラム・要旨集   23rd (CD-ROM)   2023

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  • Functional analysis of FixL-FixJ two-component signalling system by solution NMR

    菱倉直樹, 渡邉吏輝, 大久保里佳, 堀川皓央, 伊藤かおり, 三島正規, 三島正規, 猪股晃介, 小手石泰康, 澤井仁美, 澤井仁美, 城宣嗣, 池谷鉄兵, 伊藤隆

    Abstracts. Annual Meeting of the NMR Society of Japan   62nd (CD-ROM)   2023

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  • 鉄シャペロンタンパク質PCBPによる鉄イオン輸送機構の解明

    浦敦人, 簗取いずみ, 城宜嗣, 澤井仁美

    日本蛋白質科学会年会プログラム・要旨集   23rd (CD-ROM)   2023

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  • 無脊椎動物の自然免疫に関与するDM9ドメインタンパク質の構造と糖結合活性

    小嶋芙季, 澤井仁美, 海野英昭, 畠山智充

    日本生化学会大会(Web)   96th   2023

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  • 細胞内のヘム濃度を感知するタンパク質の構造機能相関

    澤井仁美

    分子研レターズ   87   2023（ ISSN:0385-0560 ）

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  • Survival of Pathogenic Bacteria: The Molecular Mechanism of the Heme-responsive Sensor Protein PefR

    澤井仁美

    生物物理(Web)   63 ( 2 )   2023（ ISSN:1347-4219 ）

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  • Structural analysis of the rhizobial multi-domain protein FixJ by heteronuclear multidimensional NMR spectroscopy

    大久保里佳, 堀川皓央, 伊藤かおり, 菱倉直樹, 渡邉吏輝, 三島正規, 三島正規, 猪股晃介, 小手石泰康, 澤井仁美, 澤井仁美, 城宣嗣, 池谷鉄兵, 伊藤隆

    Abstracts. Annual Meeting of the NMR Society of Japan   62nd (CD-ROM)   2023

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  • 生命の階層構造の観点から生命金属の役割を探る 鉄栄養素の細胞内動態を分子と細胞の階層で探る

    澤井 仁美

    日本生化学会大会プログラム・講演要旨集   95回   1S01m - 02   2022.11

  • 細胞内鉄輸送タンパク質PCBP1における鉄イオンの結合と輸送の分子メカニズム

    浦 敦人, 簗取 いずみ, 城 宜嗣, 澤井 仁美

    日本生化学会大会プログラム・講演要旨集   95回   2T05a - 05   2022.11

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  • 細胞内鉄輸送タンパク質PCBP1における鉄イオンの結合と輸送の分子メカニズム

    浦 敦人, 簗取 いずみ, 城 宜嗣, 澤井 仁美

    日本生化学会大会プログラム・講演要旨集   95回   2T05a - 05   2022.11

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  • 生命の階層構造の観点から生命金属の役割を探る 鉄栄養素の細胞内動態を分子と細胞の階層で探る Invited Reviewed

    澤井 仁美

    日本生化学会大会プログラム・講演要旨集   95回   1S01m - 02   2022.11

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    Authorship：Corresponding author  

    J-GLOBAL

  • 鉄の生体内動態:栄養素あるいは細胞毒としての鉄を制御する仕組み

    澤井仁美

    日本農芸化学会西日本支部大会およびシンポジウム講演要旨集   2022   2022

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  • ヒト由来鉄シャペロンタンパク質PCBPによる細胞内鉄イオン輸送・貯蔵の制御機構

    浦敦人, 簗取いずみ, 城宜嗣, 澤井仁美, 澤井仁美

    生体分子科学討論会講演要旨集   48th   2022

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  • ヒト由来二価金属輸送体DMT1の構造解析にむけた精製法の確立

    柴田晃利, 藤宇将吾, 簗取いずみ, 西谷雄大, 西谷雄大, 高原教代, 城宜嗣, 澤井仁美, 澤井仁美

    生体分子科学討論会講演要旨集   48th   2022

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  • ヒトの細胞内における鉄イオンの輸送と貯蔵の分子メカニズム

    浦敦人, 簗取いずみ, 城宜嗣, 澤井仁美

    日本農芸化学会西日本支部大会およびシンポジウム講演要旨集   2022   2022

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  • センサータンパク質による鉄毒性の回避メカニズム

    澤井仁美

    Fundamental Toxicological Sciences (Web)   9 ( Supplement )   2022（ ISSN:2189-115X ）

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  • Capacity of extracellular globins to reduce liver fibrosis via scavenging reactive oxygen species and promoting MMP-1 secretion Reviewed

    澤井 仁美, 松原 三佐子, 及川 大輔, 徳永 文稔, 河田 則文

    Redox Biology   52   102286   2022

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  • A paramagnetic NMR study on a rhizobial multi-domain protein, FixJ

    大久保里佳, 大久保里佳, 池谷鉄兵, 渡邉吏輝, 菱倉直樹, 三島正規, 猪股晃介, 小手石泰康, 澤井仁美, 城宣嗣, 伊藤隆

    Abstracts. Annual Meeting of the NMR Society of Japan   61st   2022

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  • ヒト腸管細胞モデル系を用いた鉄イオンの吸収を向上させる食品成分の探索とそれらの成分が鉄輸送関連タンパク質に作用する分子機構 Invited Reviewed

    高原 教代, 杉本 宏, 神戸 大朋, 城 宜嗣, 澤井 仁美

    日本生化学会大会プログラム・講演要旨集   94回   [P - 705]   2021.11

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    Authorship：Corresponding author  

    J-GLOBAL

  • Structure-function relation of membrane proteins for human iron absorption, and screening of new compounds for iron supply by the duodenal enterocyte model

    澤井仁美, 澤井仁美

    日本薬学会年会要旨集(Web)   141年会   S23 - 3   2021.03（ ISSN:0918-9823 ）

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  • Structure-function relation of membrane proteins for human iron absorption, and screening of new compounds for iron supply by the duodenal enterocyte model

    澤井仁美, 澤井仁美

    日本薬学会年会要旨集(Web)   141年会   S23 - 3   2021.03（ ISSN:0918-9823 ）

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  • 生命金属の新潮流 ヘム応答性センサータンパク質による溶血性細菌の生存の構造的機序(Structural basis for the survival of hemolytic bacteria by a heme-responsive sensor protein)

    澤井 仁美

    日本細菌学雑誌   76 ( 1 )   23 - 23   2021.02（ ISSN:0021-4930 ） （ eISSN:1882-4110 ）

  • Investigation of the molecular mechanisms of food additives for the improvement of iron deficiency

    澤井仁美

    日本食品化学研究振興財団研究成果報告書   ( 27 )   2021

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  • 細菌性ヘム応答性センサータンパク質へのCO結合に関する構造的および反応速度論的分析(Structural and kinetic analysis of CO binding to bacterial heme-responsive sensor protein)

    西谷 雄大, 西永 惠, 長井 聖奈, 杉本 宏, 當舎 武彦, 城 宣嗣, 澤井 仁美

    日本生化学会大会プログラム・講演要旨集   93回   [1Z07 - 758)]   2020.09

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  • Structural basis for multifunctionality of a sensor protein involved in hemolytic bacterial iron acquisition

    澤井仁美, 澤井仁美

    日本薬学会年会要旨集(CD-ROM)   140年会   S21 - 3   2020.03（ ISSN:0918-9823 ）

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  • Structural basis for multifunctionality of a sensor protein involved in hemolytic bacterial iron acquisition

    澤井仁美, 澤井仁美

    日本薬学会年会要旨集(Web)   140年会   S21 - 3   2020.03（ ISSN:0918-9823 ）

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  • Structural and kinetic analysis of CO binding to bacterial heme-responsive sensor protein

    西谷雄大, 西永惠, 長井聖奈, 杉本宏, 杉本宏, 當舎武彦, 當舎武彦, 城宣嗣, 澤井仁美, 澤井仁美

    日本生化学会大会(Web)   93rd   [1Z07 - 758)]   2020

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  • Dual Function of the Heme Ligation in a Heme-responsive Sensor Protein, PefR

    NISHITANI Yudai, NISHINAGA Megumi, NAGAI Seina, SUGIMOTO Hiroshi, SUGIMOTO Hiroshi, TOSHA Takehiko, TOSHA Takehiko, SHIRO Yoshitsugu, SAWAI Hitomi, SAWAI Hitomi

    日本蛋白質科学会年会プログラム・要旨集   20th (Web)   2020

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  • Functional Analysis Of Membrane Proteins Involved In Iron Absorption Using Human Intestinal Model Cell System

    TAKAHARA Michiyo, FUJISHIRO Hitomi, KAMBE Taiho, SUGIMOTO Hiroshi, SUGIMOTO Hiroshi, SHIRO Yoshitsugu, SAWAI Hitomi, SAWAI Hitomi

    日本蛋白質科学会年会プログラム・要旨集   20th (Web)   2020

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  • ヘムセンサータンパク質における転写調節の分子機構

    西永 惠, 長井 聖奈, 村木 則文, 青野 重利, 杉本 宏, 城 宜嗣, 澤井 仁美

    日本生化学会大会プログラム・講演要旨集   92回   [1T13a - 05]   2019.09

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  • ヘムセンサータンパク質における転写調節の分子機構

    西永 惠, 長井 聖奈, 村木 則文, 青野 重利, 杉本 宏, 城 宜嗣, 澤井 仁美

    日本生化学会大会プログラム・講演要旨集   92回   [1T13a - 05]   2019.09

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  • 生体内におけるSingularity Elementsとしての生体金属の利用と制御 原子から細胞レベルの研究による鉄イオンの吸収メカニズムの理解と有効な鉄栄養強化食品成分の探索

    澤井 仁美

    日本生化学会大会プログラム・講演要旨集   92回   [1S06m - 01]   2019.09

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  • 酸素センサータンパク質FixLのセンサーモジュールの構造解析

    鎌屋美咲, 小手石泰康, 當舎武彦, 當舎武彦, 馬場清喜, 杉本宏, 杉本宏, 城宜嗣, 澤井仁美, 澤井仁美

    日本細胞生物学会大会(Web)   71st   2019

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  • Missing piece of two-component signal transduction systems unveiled by SEC-SAXS

    SAWAI Hitomi, SHIRO Yoshitsugu

    SPring-8/SACLA Research Frontiers   2018   2019（ ISSN:2433-5126 ）

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  • Structural basis for the intramolecular signal transduction of oxygen sensor protein FixL from Bradyrhizobium japonicum

    KAMAYA Misaki, KOTEISHI Hiroyasu, TOSHA Takehiko, TOSHA Takehiko, BABA Seiki, SUGIMOTO Hiroshi, SUGIMOTO Hiroshi, SHIRO Yoshitsugu, SAWAI Hitomi, SAWAI Hitomi

    生物物理(Web)   59 ( Supplement 1-2 )   2019（ ISSN:1347-4219 ）

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  • 原子から細胞レベルの研究による鉄イオンの吸収メカニズムの理解と有効な鉄栄養強化食品成分の探索

    澤井仁美

    日本生化学会大会(Web)   92nd   [1S06m - 01]   2019

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  • 病原菌の鉄獲得システムで機能するヘムセンサー蛋白質の多機能性とその構造的機序

    西永惠, 長井聖奈, 村木則文, 青野重利, 杉本宏, 杉本宏, 城宜嗣, 澤井仁美, 澤井仁美

    日本細胞生物学会大会(Web)   71st   2019

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  • 病原菌の鉄獲得システムで機能するヘムセンサータンパク質の構造機能相関の解明

    澤井仁美, 澤井仁美, 西永惠, 長井聖奈, 長門石暁, 長門石暁, 津本浩平, 津本浩平, 杉本宏, 杉本宏, 城宜嗣

    日本鉄バイオサイエンス学会学術集会プログラム・抄録集   43rd   2019

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  • 病原菌の鉄源としてのヘムの濃度を感知するタンパク質の分子機構解析

    澤井仁美

    ひょうご科学技術協会研究成果報告書(Web)   2019   2019

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  • ヘムセンサータンパク質のヘムの結合に伴う構造変化

    西永 惠, 長井 聖奈, 杉本 宏, 村木 則文, 青野 重利, 城 宜嗣, 澤井 仁美

    日本生化学会大会プログラム・講演要旨集   91回   [1T11e - 090)]   2018.09

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  • ヘムセンサータンパク質のヘムの結合に伴う構造変化

    西永 惠, 長井 聖奈, 杉本 宏, 村木 則文, 青野 重利, 城 宜嗣, 澤井 仁美

    日本生化学会大会プログラム・講演要旨集   91回   [1T11e - 090)]   2018.09

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  • 一酸化窒素還元酵素のプロトン輸送におけるAsp198の役割

    倉橋 拓也, 山際 来佳, 新井 博之, 澤井 仁美, 當舎 武彦, 城 宜嗣

    日本生化学会大会プログラム・講演要旨集   91回   [3P - 127]   2018.09

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  • 生体金属のMagical Powerとその研究最前線 ヒトの鉄吸収機構を「膜タンパク質」と「生きた細胞」の研究により理解する

    澤井 仁美

    日本生化学会大会プログラム・講演要旨集   91回   [3S09m - 04]   2018.09

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  • 一酸化窒素還元酵素のプロトン輸送におけるAsp198の役割

    倉橋 拓也, 山際 来佳, 新井 博之, 澤井 仁美, 當舎 武彦, 城 宜嗣

    日本生化学会大会プログラム・講演要旨集   91回   [3P - 127]   2018.09

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  • 酸素センサータンパク質FixLにおける分子内シグナル伝達機構の解析

    鎌屋美咲, 杉本宏, 杉本宏, 城宜嗣, 澤井仁美, 澤井仁美

    日本蛋白質科学会年会プログラム・要旨集   18th   2018

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  • ヘムセンサータンパク質PefRにおける転写調節の分子メカニズム

    西永惠, 杉本宏, 杉本宏, 村木則文, 青野重利, 城宜嗣, 澤井仁美, 澤井仁美

    日本蛋白質科学会年会プログラム・要旨集   18th   2018

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  • ヒト小腸の細胞膜でDcytbが鉄分吸収を促進するメカニズム

    GANASEN Menega, 冨樫ひろ美, 山下恵太郎, 山下恵太郎, 平田邦生, MAUK Grant A., 城宜嗣, 澤井仁美, 杉本宏, 杉本宏

    日本結晶学会年会講演要旨集   2018   2018

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  • Structural insight into the dietary non-heme iron absorption in human duodenum

    GANASEN Menega, ASAKURA Honami, TOSHA Takehiko, YUAN Xiaojing, HAMZA Iqbal, MAUK Grant A., SHIRO Yoshitsugu, SUGIMOTO Hiroshi, SAWAI Hitomi

    日本蛋白質科学会年会プログラム・要旨集   18th   2018

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  • ヒトの鉄吸収機構を「膜タンパク質」と「生きた細胞」の研究により理解する

    澤井仁美

    日本生化学会大会(Web)   91st   [3S09m - 04]   2018

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  • ヒトの鉄吸収に関わる膜貫通型鉄還元酵素の立体構造に基づく生きた細胞での機能解析

    GANASEN Menega, 藤代瞳, YUAN Xiaojing, HAMZA Iqbal, 杉本宏, 杉本宏, 姫野誠一郎, 城宜嗣, 澤井仁美, 澤井仁美

    日本蛋白質科学会年会プログラム・要旨集   18th   2018

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  • ヒトの鉄イオン吸収に関わる膜タンパク質の立体構造を基盤とした機能と構造の相互解析

    GANASEN Menega, 藤代瞳, YUAN Xiaojing, HAMZA Iqbal, 姫野誠一郎, 杉本宏, 城宜嗣, 澤井仁美, 澤井仁美

    日本鉄バイオサイエンス学会学術集会プログラム・抄録集   42nd   2018

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  • ヒトの鉄イオン吸収に関わる膜タンパク質の立体構造に基づく生きた細胞での機能解析

    GANASEN Menega, 藤代瞳, YUAN Xiaojing, HAMZA Iqbal, 姫野誠一郎, MAUK A. Grant, 杉本宏, 城宜嗣, 澤井仁美, 澤井仁美

    Fundamental Toxicological Sciences (Web)   5 ( Supplement )   2018（ ISSN:2189-115X ）

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  • ダイズ根粒菌由来酸素センサータンパク質FixLのタンデムPASドメインにおけるシグナル伝達機構

    鎌屋美咲, 杉本宏, 杉本宏, 城宜嗣, 澤井仁美, 澤井仁美

    日本生化学会大会(Web)   91st   2018

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  • Understanding the mechanism of dietary iron absorption at atomic level

    GANASEN Menega, ASAKURA Honami, TOSHA Takehiko, URANO Takeshi, YUAN Xiaojing, HAMZA Iqbal, MAUK Grant A., SHIRO Yoshitsugu, SUGIMOTO Hiroshi, SAWAI Hitomi

    日本生化学会大会(Web)   91st   2018

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  • 緑膿菌由来一酸化窒素還元酵素の保存されたグルタミン酸残基の役割

    倉橋 拓也, 山際 来佳, 武田 真理子, 新井 博之, 澤井 仁美, 當舎 武彦, 城 宣嗣

    生命科学系学会合同年次大会   2017年度   [3AT12 - 0221)]   2017.12

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  • 新規なヘムセンサータンパク質による転写調節の分子メカニズム

    西永 惠, 杉本 宏, 青野 重利, 城 宜嗣, 澤井 仁美

    生命科学系学会合同年次大会   2017年度   [4LT15 - 0625)]   2017.12

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  • 緑膿菌由来一酸化窒素還元酵素の保存されたグルタミン酸残基の役割

    倉橋拓也, 山際来佳, 武田真理子, 新井博之, 澤井仁美, 澤井仁美, 當舎武彦, 城宜嗣, 城宜嗣

    日本生化学会大会(Web)   90th   [3AT12 - 0221)]   2017

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  • Structural analysis of a human duodenal ferrireductase, Dcytb

    GANASEN Menega, SAWAI Hitomi, NAGATOISHI Satoru, TOGASHI Hiromi, TAKEDA Hanae, TSUMOTO Kohei, SHIRO Yoshitsugu, SUGIMOTO Hiroshi

    日本蛋白質科学会年会プログラム・要旨集   17th   2017

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  • 膜内在性一酸化窒素還元酵素における効率的なNO還元反応のための仕組み

    山際来佳, 山際来佳, 澤井仁美, 當舎武彦, 中村寛夫, 新井博之, 城宜嗣

    日本蛋白質科学会年会プログラム・要旨集   17th   2017

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  • Functional roles of a conserved valine residue in membrane-integrated nitric oxide reductase, cNOR

    YAMAGIWA Raika, YAMAGIWA Raika, SAWAI Hitomi, TOSHA Takehiko, NAKAMURA Hiro, ARAI Hiroyuki, SHIRO Yoshitsugu

    生物物理(Web)   57 ( Supplement 1-2 )   2017（ ISSN:1347-4219 ）

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  • Intra- and inter-molecular signal transduction mechanisms in a complete oxygen sensing system

    WRIGHT Gareth S. A., SAEKI Akane, HIKIMA Takaaki, NISHIZONO Yoko, HISANO Tamao, YAMAMOTO Masaki, ANTINYUK Svetlana, HASNAIN S. Samar, SHIRO Yoshitsugu, SAWAI Hitomi

    日本蛋白質科学会年会プログラム・要旨集   17th   2017

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  • 新規なヘムセンサータンパク質による転写調節の分子メカニズム

    西永惠, 杉本宏, 青野重利, 城宜嗣, 城宜嗣, 澤井仁美, 澤井仁美

    日本生化学会大会(Web)   90th   [4LT15 - 0625)]   2017

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  • Intra- and inter-molecular signal transduction mechanisms in a complete oxygen sensing system

    WRIGHT Gareth S. A., SAEKI Akane, HIKIMA Takaaki, NISHIZONO Yoko, HISANO Tamao, YAMAMOTO Masaki, ANTINYUK Svetlana, HASNAIN S. Samar, SHIRO Yoshitsugu, SAWAI Hitomi

    日本蛋白質科学会年会プログラム・要旨集   17th   2017

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  • 緑膿菌由来一酸化窒素還元酵素のNOおよびH+の輸送に関わるアミノ酸残基の役割

    山際 来佳, 武田 真梨子, 澤井 仁美, 當舎 武彦, 中村 寛夫, 新井 博之, 城 宜嗣

    日本生化学会大会プログラム・講演要旨集   89回   [3P - 150]   2016.09

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  • X線小角散乱法により決定したマルチドメイン酸素センサータンパク質の全長構造から見出した分子内シグナル伝達機構

    澤井 仁美, 佐伯 茜子, ライト・ギャレス, 引間 孝明, アントニューク・スベトラーナ, 山本 雅貴, ハスネイン・サマー, 城 宜嗣

    日本生化学会大会プログラム・講演要旨集   89回   [3P - 125]   2016.09

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  • X線小角散乱法により決定したマルチドメイン酸素センサータンパク質の全長構造から見出した分子内シグナル伝達機構

    澤井 仁美, 佐伯 茜子, ライト・ギャレス, 引間 孝明, アントニューク・スベトラーナ, 山本 雅貴, ハスネイン・サマー, 城 宜嗣

    日本生化学会大会プログラム・講演要旨集   89回   [3P - 125]   2016.09

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  • 緑膿菌由来一酸化窒素還元酵素のNOおよびH+の輸送に関わるアミノ酸残基の役割

    山際 来佳, 武田 真梨子, 澤井 仁美, 當舎 武彦, 中村 寛夫, 新井 博之, 城 宜嗣

    日本生化学会大会プログラム・講演要旨集   89回   [3P - 150]   2016.09

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  • 膜貫通型一酸化窒素還元酵素の変異体解析によるNOおよびH+輸送経路の解明

    山際来佳, 澤井仁美, 當舎武彦, 中村寛夫, 新井博之, 城宜嗣, 城宜嗣

    日本蛋白質科学会年会プログラム・要旨集   16th   2016

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  • Structural Analysis of Human Duodenal Cytochrome b561

    GANASEN Menega, SAWAI Hitomi, SHIRO Yoshitsugu, SHIRO Yoshitsugu, SUGIMOTO Hiroshi

    日本生化学会大会(Web)   89th   2016

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  • 全長FixJのX線結晶構造解析による二成分情報伝達系における転写調節機構の解明

    西園陽子, 佐伯茜子, 久野玉雄, 城宜嗣, 城宜嗣, 澤井仁美

    日本蛋白質科学会年会プログラム・要旨集   16th   2016

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  • 窒素固定を制御する酸素適応システムFixL/FixJにおける分子内および分子間情報伝達機構

    佐伯茜子, WRIGHT Gareth S. A., 引間孝明, ANTONYUK Svetlana V., HASNAIN S. Samar, 山本雅貴, 城宜嗣, 城宜嗣, 澤井仁美

    日本蛋白質科学会年会プログラム・要旨集   16th   2016

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  • 後生動物の鉄獲得に関わる新規なヘムトランスポーターの性質

    澤井仁美, GANASEN Menega, 伊藤達矢, YUAN Xiaojing, HAMZA Iqbal, 城宜嗣, 城宜嗣

    日本蛋白質科学会年会プログラム・要旨集   16th   2016

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  • 緑膿菌を用いた一酸化窒素還元酵素の組換え体調製と変異体解析

    山際 来佳, 澤井 仁美, 當舎 武彦, 中村 寛夫, 新井 博之, 城 宜嗣

    日本生化学会大会・日本分子生物学会年会合同大会講演要旨集   88回・38回   [1P0495] - [1P0495]   2015.12

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  • 酸素センサータンパク質のリガンド結合に伴う構造変化

    佐伯 茜子, 引間 孝明, Wright Gareth S.A., Antonyuk Svetlana, 山本 雅貴, Hasnain S. Samar, 城 宜嗣, 澤井 仁美

    日本生化学会大会・日本分子生物学会年会合同大会講演要旨集   88回・38回   [1P0384] - [1P0384]   2015.12

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  • 生体金属の最前線 気体分子センサータンパク質における機能制御メカニズムの革新的理解のために

    澤井 仁美

    日本生化学会大会・日本分子生物学会年会合同大会講演要旨集   88回・38回   [4W8 - 6]   2015.12

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  • 生体金属の最前線 気体分子センサータンパク質における機能制御メカニズムの革新的理解のために

    澤井 仁美

    日本生化学会大会・日本分子生物学会年会合同大会講演要旨集   88回・38回   [4W8 - 6]   2015.12

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  • Mutagenesis of Nitric Oxide Reductase in Pseudomonas aeruginosa

    YAMAGIWA Raika, SAWAI Hitomi, TOSHA Takehiko, NAKAMURA Hiro, ARAI Hiroyuki, SHIRO Yoshitsugu, SHIRO Yoshitsugu

    Metals in Biology in Wako. RIKEN Symposium, 2015   2015

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  • Small-Angle X-ray Scattering (SAXS) Measurements of a Heme-based Oxygen Sensor Protein, FixL

    SAEKI Akane, HIKIMA Takaaki, WRIGHT Gareth S. A., ANTONYUK Svetlana, HASNAIN S. Samar, YAMAMOTO Masaki, SHIRO Yoshitsugu, SHIRO Yoshitsugu, SAWAI Hitomi

    Metals in Biology in Wako. RIKEN Symposium, 2015   2015

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  • 酸素センサータンパク質のリガンド結合に伴う構造変化

    佐伯茜子, 引間孝明, WRIGHT Gareth S.A., ANTONYUK Svetlana, 山本雅貴, RHASNAIN S. Sama, 城宜嗣, 城宜嗣, 澤井仁美

    日本生化学会大会(Web)   88th   [1P0384] - [1P0384]   2015

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  • 酸素センサータンパク質FixLのX線小角散乱法による構造解析

    佐伯茜子, 澤井仁美, 引間孝明, WRIGHT Gareth S. A., ANTONYUK Svetlana V., HASNAIN Samar S., 城宜嗣, 城宜嗣

    日本蛋白質科学会年会プログラム・要旨集   15th   2015

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  • 緑膿菌由来一酸化窒素還元酵素組換え体の調製と変異体解析

    山際来佳, 澤井仁美, 當舎武彦, 中村寛夫, 新井博之, 城宜嗣, 城宜嗣

    日本蛋白質科学会年会プログラム・要旨集   15th   2015

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  • 緑膿菌を用いた一酸化窒素還元酵素の組換え体調製と変異体解析

    山際来佳, 澤井仁美, 當舎武彦, 中村寛夫, 新井博之, 城宜嗣, 城宜嗣

    日本生化学会大会(Web)   88th   [1P0495] - [1P0495]   2015

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  • Characterization of A Novel Heme Transporter in Animals

    GANASEN Menega, HAMZA Iqbal, SHIRO Yoshitsugu, SHIRO Yoshitsugu, SAWAI Hitomi

    日本生化学会大会(Web)   88th   2015

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  • 緑膿菌由来一酸化窒素還元酵素の組換え体の調製とVal206の役割

    山際 来佳, 澤井 仁美, 中村 寛夫, 當舎 武彦, 城 宜嗣

    日本生化学会大会プログラム・講演要旨集   87回   [3T09p - 05]   2014.10

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  • 緑膿菌由来一酸化窒素還元酵素の組換え体の調製とVal206の役割

    山際来佳, 澤井仁美, 中村寛夫, 當舎武彦, 城宜嗣, 城宜嗣

    日本生化学会大会(Web)   87th   2014

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  • Molecular structure of cytoglobin Reviewed

    サワイ ヒトミ, シロ ヨシツグ

    45 ( 13 )   605 - 608   2013.12（ ISSN:1346-7557 ）

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  • 【第4のグロビン-サイトグロビンの機能-】サイトグロビンの分子構造

    澤井 仁美, 城 宜嗣

    細胞   45 ( 13 )   605 - 608   2013.12（ ISSN:1346-7557 ）

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    高分解能X線結晶構造解析法により、野生型サイトグロビンの分子構造を世界で初めて明らかにした。その全体構造は、ミオグロビン・ヘモグロビンなどの既知のグロビンタンパク質と非常に良く似ているが、活性部位であるヘム鉄の配位構造は全く異なっていた。本稿では、サイトグロビンの分子構造の詳細を紹介するとともに、その構造から予測される生理機能について概説する。(著者抄録)

  • 【第4のグロビン-サイトグロビンの機能-】サイトグロビンの分子構造 Reviewed

    澤井 仁美, 城 宜嗣

    細胞   45 ( 13 )   605 - 608   2013.12（ ISSN:1346-7557 ）

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    高分解能X線結晶構造解析法により、野生型サイトグロビンの分子構造を世界で初めて明らかにした。その全体構造は、ミオグロビン・ヘモグロビンなどの既知のグロビンタンパク質と非常に良く似ているが、活性部位であるヘム鉄の配位構造は全く異なっていた。本稿では、サイトグロビンの分子構造の詳細を紹介するとともに、その構造から予測される生理機能について概説する。(著者抄録)

    J-GLOBAL

  • 走化性シグナルトランスデューサータンパク質Aer2の構造と機能

    澤井仁美, 杉本宏, 城宜嗣, 青野重利

    生体分子科学討論会講演要旨集   40th   2013

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  • ヘム含有センサータンパク質Aer2による選択的酸素センシングの分子機構

    澤井仁美, 澤井仁美, 杉本宏, 城宜嗣, 青野重利

    触媒討論会討論会A予稿集   112th   2013（ ISSN:1343-9936 ）

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  • Listeria monocytogenesのヘム取込み系におけるヘム結合タンパク質HupDの性質

    岡本泰典, 岡本泰典, 林高史, 澤井仁美, 青野重利

    日本化学会講演予稿集   93rd ( 3 )   2013（ ISSN:0285-7626 ）

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  • ヘムをエフェクター分子とする転写調節因子HrtRの構造と機能

    澤井仁美, 杉本宏, 山中優, 城宜嗣, 青野重利

    錯体化学会討論会講演要旨集   62nd   2012

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  • ヘム濃度の恒常性維持に関わる転写調節因子の構造と機能

    澤井仁美, 杉本宏, 山中優, 城宜嗣, 青野重利

    日本蛋白質科学会年会プログラム・要旨集   12th   2012

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  • ヘム分子により機能制御される転写調節因子HrtRの構造と機能

    澤井仁美, 山中優, 杉本宏, 城宜嗣, 青野重利

    生体分子科学討論会講演要旨集   39th   2012

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  • ヘムをセンシングする転写調節因子HesRの機能制御機構

    山中優, 澤井仁美, 青野重利

    日本化学会講演予稿集   92nd ( 3 )   2012（ ISSN:0285-7626 ）

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  • 新規な転写調節因子HesRのヘムによる機能制御の分子機構

    澤井仁美, 杉本宏, 山中優, 城宜嗣, 青野重利

    日本化学会講演予稿集   92nd ( 3 )   2012（ ISSN:0285-7626 ）

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  • 細胞内ヘム濃度の恒常性維持に関わる転写制御の分子機構

    澤井仁美, 杉本宏, 山中優, 城宜嗣, 青野重利

    日本結晶学会年会講演要旨集   2012   2012

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  • ヘムにより機能制御される新規な転写調節因子HesRのX線結晶構造

    澤井仁美, 杉本宏, 山中優, 城宜嗣, 青野重利

    日本結晶学会年会講演要旨集   2011   2011

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  • ヘム分子により機能制御される新規な転写調節因子HesRのX線結晶構造

    澤井仁美, 山中優, 杉本宏, 城宜嗣, 青野重利

    日本化学会バイオテクノロジー部会シンポジウム講演要旨集   14th   2011

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  • ヘムセンサー機能を有する転写調節因子の構造と機能

    澤井仁美, 山中優, 杉本宏, 城宜嗣, 青野重利

    錯体化学会討論会講演要旨集   61st   2011

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  • ヘムセンサーとして機能する転写調節因子YgfCの構造と機能

    山中優, 澤井仁美, 青野重利

    日本化学会講演予稿集   91st ( 3 )   2011（ ISSN:0285-7626 ）

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  • ヘムを生理的エフェクターとする転写調節因子HesRの機能制御

    山中優, 澤井仁美, 青野重利

    日本化学会バイオテクノロジー部会シンポジウム講演要旨集   14th   2011

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  • ヘムをセンシングする転写調節因子YgfCの構造と機能

    山中優, 澤井仁美, 青野重利

    日本蛋白質科学会年会プログラム・要旨集   11th   2011

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  • ヘムをシグナル分子とする遺伝子発現制御の分子機構

    山中優, 澤井仁美, 青野重利

    生体分子科学討論会講演要旨集   38th   2011

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  • ヘム含有PASドメインを有するシグナルトランスデューサータンパク質Aer2による酸素センシング

    澤井仁美, 石川春人, 石川春人, 水谷泰久, 水谷泰久, 青野重利

    生体分子科学討論会講演要旨集   37th   2010

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  • ヘム含有PASドメインを有する新規な走化性制御蛋白質Aer2の酸素感知機構

    澤井仁美, 石川春人, 石川春人, 水谷泰久, 青野重利

    日本化学会バイオテクノロジー部会シンポジウム講演要旨集   13th   2010

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  • ヘム含有PASドメインを有する新規なセンサー蛋白質の性質

    青野重利, 澤井仁美, 石川春人

    日本化学会講演予稿集   90th ( 3 )   2010（ ISSN:0285-7626 ）

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  • ヘム蛋白質の新規な構造と機能:アルドキシム脱水酵素の活性制御機構

    澤井仁美, 杉本宏, 加藤康夫, 浅野泰久, 城宜嗣, 青野重利

    日本蛋白質科学会年会プログラム・要旨集   10th   2010

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  • 低温X線照射還元によるアルドキシム脱水酵素の結晶内におけるミカエリス複合体の生成およびその構造決定

    澤井仁美, 杉本宏, 加藤康夫, 浅野泰久, 城宜嗣, 青野重利

    日本結晶学会年会講演要旨集   2009   2009

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  • 新規なヘム酵素(アルドキシム脱水酵素)の酵素基質複合体のX線結晶構造

    澤井仁美, 杉本宏, 加藤康夫, 浅野泰久, 城宜嗣, 青野重利

    日本蛋白質科学会年会プログラム・要旨集   9th   2009

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  • 新規なヘム酵素(アルドキシム脱水酵素)のX線結晶構造

    澤井仁美, 杉本宏, 加藤康夫, 浅野泰久, 城宜嗣, 青野重利

    生体分子科学討論会講演要旨集   36th   2009

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  • FT-IR分光法による一酸化炭素結合型NeuroglobinおよびCytoglobinのConformational Substates解析

    安本英敏, 石山知沙, 加藤稔, 杉本宏, 澤井仁美, 牧野正知, 城宜嗣

    日本化学会講演予稿集   88th ( 1 )   2008（ ISSN:0285-7626 ）

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  • ヘムを活性中心とするアルドキシム脱水酵素の性質

    青野重利, 小林克彰, 澤井仁美, 吉岡資郎, 加藤康夫, 浅野泰久

    触媒討論会討論会A予稿集   102nd   2008（ ISSN:1343-9936 ）

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  • Effect of Dimerization on the Regulation of Gas Binding to Human Cytoglobin

    UNO Tadayuki, NOSE Azusa, KUKINO Kaori, TOMISUGI Yoshikazu, AOYAMA Hiroshi, KAWADA Norifumi, YOSHIZATO Katsutoshi, SAWAI Hitomi, SHIRO Yoshitsugu

    薬学雑誌   128 ( Suppl.1 )   56 - 56   2008（ ISSN:0031-6903 ）

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    Publishing type：Research paper, summary (international conference)  

    J-GLOBAL

  • 新規なヘム含有型アルドキシム脱水酵素の反応機構

    澤井仁美, 杉本宏, 小林克彰, 加藤康夫, 浅野泰久, 城宜嗣, 青野重利

    日本化学会バイオテクノロジー部会シンポジウム講演要旨集   11th   2008

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  • Structure and function of a globin-coupled enzyme that catalyzes the formation of a bacterial second messenger, c-di-GMP

    AONO Shigetoshi, YOSHIOKA Shiro, SAWAI Hitomi

    薬学雑誌   128 ( Suppl.1 )   42 - 42   2008（ ISSN:0031-6903 ）

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    Publishing type：Research paper, summary (international conference)  

    J-GLOBAL

  • グロビン型センサードメインを有するセカンドメッセンジャー(c-di-GMP)合成酵素の酸素による活性制御

    澤井仁美, 吉岡資郎, 内田毅, 兵藤守, 早川芳宏, 石森浩一郎, 青野重利

    生体分子科学討論会講演要旨集   34th   2007

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  • セカンドメッセンジャー(c-di-GMP)合成を制御する新規な酸素センサータンパク質の構造と性質

    吉岡資郎, 澤井仁美, 内田毅, 兵藤守, 早川芳宏, 石森浩一郎, 青野重利

    酸化反応討論会講演要旨集   40th   2007

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  • Exogenous Ligand Binding Mechanism of Cytoglobin

    UNO Tadayuki, KUKINO Kaori, KUKINO Kaori, MAEDA Hatsuo, TOMISUGI Yoshikazu, ISHIKAWA Yoshinobu, KAWADA Norifumi, YOSHIZATO Katsutoshi, SAWAI Hitomi, SHIRO Yoshitsugu

    生物物理   46 ( Supplement 2 )   2006（ ISSN:0582-4052 ）

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  • 2P003 Ligand binding mechanism of human Cytoglobin based on X-ray crystal structure

    Makino M., Sugimoto H., Sawai H., Kawada N., Yoshizato K., Shiro Y.

    Seibutsu Butsuri   44 ( Suppl.1 )   S110 - S110   2004.11（ ISSN:0582-4052 ） （ eISSN:1347-4219 ）

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  • Structural Basis of Human Cytoglobin for Ligand Binding

    MAKINO Masatomo, MAKINO Masatomo, SUGIMOTO Hiroshi, SAWAI Hitomi, SAWAI Hitomi, KAWADA Norifumi, YOSHIZATO Katsutoshi, SHIRO Yoshitsugu

    金属の関与する生体関連反応シンポジウム講演要旨集   14th   2004（ ISSN:0919-2093 ）

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  • Biochemical analysis of a novel oxygen sensor protein in the N-2-fixing cyanobacterium Anabaena sp PCC 7120

    R Narikawa, H Miyatake, SH Kim, H Sawai, H Kumita, Y Shiro, K Miki, M Ikeuchi, M Ohmori

    PLANT AND CELL PHYSIOLOGY   44 ( 0 )   S81 - S81   2003（ ISSN:0032-0781 ）

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    Publishing type：Research paper, summary (international conference)  

    An oxygen sensor may play an important role in the N<SUB>2</SUB>-fixing cyanobacterium <I>Anabaena</I> sp. PCC 7120. FixL of rhizobia and DOS of <I>Escherichia coli</I> have a heme PAS domain as an oxygen sensor. We detected in the <I>Anabaena</I> genome a gene <I>alr2428</I> that encodes a homologous heme PAS domain in addition to various signaling and DNA-binding domains. To analyze this heme PAS domain, we expressed this domain as a His-tagged protein. The purified protein was found to bind a heme. We prepared met, deoxy, O<SUB>2</SUB>-binding and CO-binding forms and measured their absorption spectra and resonance raman spectra. The properties were very similar to those of DOS from <I>E. coli</I>, whose deoxy and met forms have hexacoordinate heme iron. However, no clear sixth ligand to iron was detected in Alr2428, when aligned with DOS from <I>E. coli</I>. Possible structure of the heme PAS domain in Alr2428 will be discussed.

    DOI： 10.14841/jspp.2003.0.227.0

    CiNii Article

  • Biochemical Analysis Of A Novel Oxygen Sensor Protein In The N<SUB>2</SUB>-Fixing Cyanobacterium <I>Anabaena</I> sp. PCC 7120

    Narikawa Rei, Miyatake Hideyuki, Kim Seong-Hoon, Sawai Hitomi, Kumita Hideyuki, Shiro Yoshitsugu, Miki Kunio, Ikeuchi Masahiko, Ohmori Masayuki

    Plant and Cell Physiology Supplement   2003   227 - 227   2003

    　More details

    An oxygen sensor may play an important role in the N<SUB>2</SUB>-fixing cyanobacterium <I>Anabaena</I> sp. PCC 7120. FixL of rhizobia and DOS of <I>Escherichia coli</I> have a heme PAS domain as an oxygen sensor. We detected in the <I>Anabaena</I> genome a gene <I>alr2428</I> that encodes a homologous heme PAS domain in addition to various signaling and DNA-binding domains. To analyze this heme PAS domain, we expressed this domain as a His-tagged protein. The purified protein was found to bind a heme. We prepared met, deoxy, O<SUB>2</SUB>-binding and CO-binding forms and measured their absorption spectra and resonance raman spectra. The properties were very similar to those of DOS from <I>E. coli</I>, whose deoxy and met forms have hexacoordinate heme iron. However, no clear sixth ligand to iron was detected in Alr2428, when aligned with DOS from <I>E. coli</I>. Possible structure of the heme PAS domain in Alr2428 will be discussed.

    DOI： 10.14841/jspp.2003.0.227.0

    CiNii Article

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Presentations

  • Sensing of Iron Nutrients as a New Target for Antibiotic Development [Keynote Lecture] Invited International conference

    Hitomi Sawai

    The 11th Asian Biological Inorganic Chemistry Conference (AsBIC11)  2024.12 

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    Presentation type：Oral presentation (keynote)  

    Venue：Guilin, China  

  • Structural Insights into the Sensing of Iron Nutrients as a Basis for the Development of New Drugs [Invited Lecture] Invited International conference

    Hitomi Sawai

    Gordon Research Conference - Metals in Medicine  2024.06 

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    Presentation type：Oral presentation (invited, special)  

  • Thinking about iron: the molecular and cellular mechanisms of dietary iron absorption [Keynote Lecture] Invited International conference

    Hitomi Sawai

    20th International Conference on Biological Inorganic Chemistry (ICBIC20)  2023.07  Society of Biological Inorganic Chemistry

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    Presentation type：Oral presentation (keynote)  

    Venue：Adelaide, Australia  

  • Heme controls the structural rearrangement of its sensor protein mediating the survival of hemolytic bacteria [Invited Lecture] Invited International conference

    Hitomi Sawai

    Gordon Research Conference: Chemistry and Biology of Tetrapyrroles  2022.07 

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    Presentation type：Oral presentation (invited, special)  

    Venue：USA  

  • Iron as a nutrient: the molecular and cellular mechanisms of dietary iron absorption in humans [Keynote Lecture] Invited International conference

    Hitomi Sawai

    French-Japanses Symposium in BioInorganic Chemistry and FrenchBIC annual meeting  2024.04 

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    Presentation type：Oral presentation (keynote)  

  • 病原菌のヘム応答センサータンパク質を標的とする抗菌薬の開発

    澤井仁美

    生物無機化学シンポジウム2025  2025.01 

  • Role of heme and iron ion in the body [Educational Lecture] Invited Domestic conference

    Hitomi Sawai

    The 31th Annual Meeting of the Society of Blood Substitutes, Japan  2024.12 

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    Presentation type：Oral presentation (invited, special)  

  • 生体内におけるヘムおよび鉄イオンの動態と制御について

    澤井 仁美

    人工血液  2024.11  日本血液代替物学会

  • Molecular Science for Good Health by Iron Uptake [Invited Lecture] Invited

    Hitomi Sawai

    100th Anniversary Meeting of Japan Society for Bioscience, Biotechnology, and Agrochemistry  2024.03 

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    Presentation type：Oral presentation (invited, special)  

  • Differences of the iron acquisition mechanisms of plants and animals at the molecular level [Invited Lecture] Invited Domestic conference

    Hitomi Sawai

    The 65th Annual Meeting of the Japanese Society of Plant Physiologists  2024.03 

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    Presentation type：Oral presentation (invited, special)  

  • Molecular mechanisms of the absorption and transport of iron nutrients via proteins in humans

    Hitomi Sawai

    Symposium on Biological Inorganic Chemistry 2024  2024.01 

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    Presentation type：Oral presentation (general)  

  • Synchrotorn Structural Biology for Metalloproteins [Invited Lecture] Invited Domestic conference

    Hitomi Sawai

    2023.11 

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    Presentation type：Oral presentation (invited, special)  

  • Food for thought: the protein interactions for dietary iron absorption in humans. [Invited Lecture] Invited International conference

    Hitomi Sawai

    UK-Japan meeting on dynamic and time-resolved crystallography 2023  2023.09  LINXS

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    Presentation type：Oral presentation (invited, special)  

    Venue：Leicester, UK  

  • Food for thought: the protein interactions for dietary iron absorption in humans Invited International coauthorship International conference

    Hitomi Sawai

    UK-Japan meeting on dynamic and time-resolved crystallography 2023  2023.09  Leicester Institute for Structural and Chemical Biology

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    Presentation type：Oral presentation (invited, special)  

    Venue：Leicester  

  • ヒトの鉄栄養吸収に関わる膜タンパク質の構造機能解析 [招待講演] Invited Domestic conference

    澤井仁美

    第13回トランスポーター研究会九州部会  2023.08  トランスポーター研究会

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    Presentation type：Oral presentation (invited, special)  

    Venue：福岡  

  • ヒトの鉄栄養吸収に関わる膜タンパク質の構造機能解析 Invited Domestic conference

    澤井 仁美

    第13回トランスポーター研究会九州部会  2023.08  トランスポーター研究会

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    Presentation type：Oral presentation (invited, special)  

    Venue：福岡  

  • Thinking about iron: the molecular and cellular mechanisms of dietary iron absorption [Keynote Lecture] Invited International coauthorship International conference

    Hitomi Sawai

    20th International Conference on Biological Inorganic Chemistry (ICBIC20)  2023.07  The Society of Biological Inorganic Chemistry

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    Presentation type：Oral presentation (keynote)  

    Venue：Adelaide  

  • 蛋白質間相互作用による鉄ホメオスタシスの制御 [招待講演] Invited Domestic conference

    澤井仁美

    第23回日本蛋白質科学会年会  2023.07  日本蛋白質科学会

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    Presentation type：Oral presentation (invited, special)  

  • Regulation of iron homeostasis by protein-protein interactions Invited

    Hitomi Sawai

    The 23th Annual Meeting of the Protein Science Society of Japan  2023.07 

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    Presentation type：Oral presentation (invited, special)  

  • Heme Controls the Structural Rearrangement of Its Sensor Protein Mediating Survival of Pathogenic Bacteria [Invited Lecture] Invited International conference

    Hitomi Sawai

    10th Asian Biological Inorganic Chemistry Conference (AsBIC10)  2022.11  Society of Biological Inorganic Chemistry

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    Presentation type：Oral presentation (invited, special)  

    Venue：Kobe  

  • Structural Rearrangement of Its Sensor Protein Mediating Survival of Pathogenic Bacteria Invited International coauthorship International conference

    Hitomi Sawai

    10th Asian Biological Inorganic Chemistry Conference (AsBIC10)  2022.11  The Society of Biological Inorganic Chemistry

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    Presentation type：Oral presentation (invited, special)  

    Venue：Kobe  

  • 鉄栄養素の細胞内動態を分子と細胞の階層で探る [招待講演] Invited Domestic conference

    第95回日本生化学会大会 新学術領域研究「生命金属科学」共催シンポジウム『生命の階層構造の観点から生命金属の役割を探る』  2022.11  日本生化学会

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    Presentation type：Oral presentation (invited, special)  

    Venue：名古屋  

  • 鉄栄養素の細胞内動態を分子と細胞の階層で探る Invited Domestic conference

    澤井仁美

    第95回日本生化学会大会 新学術領域研究「生命金属科学」共催シンポジウム『生命の階層構造の観点から生命金属の役割を探る』  2022.11  日本生化学会

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    Presentation type：Oral presentation (invited, special)  

    Venue：名古屋  

  • メタルバイオサイエンスの未来を拓く生物無機化学への招待『センサータンパク質による鉄毒性の回避メカニズム』[招待講演] Invited Domestic conference

    澤井仁美

    メタルバイオサイエンス研究会2022  2022.10  日本毒性学会 生体金属部会

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    Presentation type：Oral presentation (invited, special)  

    Venue：京都  

  • メタルバイオサイエンスの未来を拓く生物無機化学への招待『センサータンパク質による鉄毒性の回避メカニズム』 Invited Domestic conference

    澤井仁美

    日本毒性学会 生体金属部会主催 メタルバイオサイエンス研究会2022  2022.10  日本毒性学会

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    Presentation type：Oral presentation (invited, special)  

    Venue：京都  

  • 鉄の生体内動態：栄養素あるいは細胞毒としての鉄を制御する仕組み [招待講演] Invited Domestic conference

    澤井仁美

    日本農芸化学会2022年度西日本支部大会  2022.09  日本農芸化学会西日本支部

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    Presentation type：Oral presentation (invited, special)  

    Venue：長崎  

  • 鉄の生体内動態：栄養素あるいは細胞毒としての鉄を制御する仕組み Invited

    澤井仁美

    日本農芸化学会2022年度西日本支部大会  2022.09 

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    Presentation type：Oral presentation (invited, special)  

  • 生体内の鉄の動態と機能 [招待講演] Invited Domestic conference

    澤井仁美

    第34回生物無機化学夏季セミナー  2022.08  生物無機化学研究会

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    Presentation type：Oral presentation (invited, special)  

    Venue：大阪  

  • 生体内の鉄の動態と機能 Invited

    澤井仁美

    第34回生物無機化学夏季セミナー  2022.08 

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    Presentation type：Oral presentation (invited, special)  

  • Heme controls the structural rearrangement of its sensor protein mediating the survival of hemolytic bacteria. Invited International coauthorship International conference

    Hitomi Sawai

    Gordon Research Conference: Chemistry and Biology of Tetrapyrroles - The Roles of Tetrapyrroles in Catalysis, Regulation, Metabolism and Disease  2022.07  Gordon Research Conference

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    Presentation type：Oral presentation (invited, special)  

    Venue：Salve Regina University  

  • Structural insights into the multifunctionality of the heme-responsive sensor protein for detoxification in hemolytic bacteria. [Invited Lecture] Invited International conference

    Hitomi Sawai

    International Chemical Congress of Pacific Basin Societies 2021 (Pacifichem2021)  2021.12 

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    Presentation type：Oral presentation (invited, special)  

    Venue：Honolulu, USA  

  • Structural insights into the multifunctionality of the heme-responsive sensor protein for detoxification in hemolytic bacteria Invited

    Hitomi Sawai

    International Chemical Congress of Pacific Basin Societies 2021 (Pacifichem2021)  2021.12 

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    Presentation type：Oral presentation (invited, special)  

  • 鉄イオンの吸収に関わる膜タンパク質の立体構造と腸管モデル細胞を用いた機能解析 [招待講演] Invited Domestic conference

    澤井仁美

    第１回トランスポーター研究会関西部会～トランスポーター研究のかけ橋～  2021.10  トランスポーター研究会関西支部

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    Presentation type：Oral presentation (invited, special)  

  • 鉄イオンの吸収に関わる膜タンパク質の立体構造と腸管モデル細胞を用いた機能解析 Invited

    澤井仁美

    第１回トランスポーター研究会関西部会～トランスポーター研究のかけ橋～  2021.10 

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    Presentation type：Oral presentation (invited, special)  

  • 膜タンパク質の立体構造を基盤とする腸管モデル細胞を用いた鉄イオン吸収メカニズムの解析 [招待講演] Invited Domestic conference

    澤井仁美

    2021年度生理研研究会『上皮膜輸送の多様性・調和機構を基盤とする異分野融合研究の創出』  2021.09  生理学研究所

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    Presentation type：Oral presentation (invited, special)  

  • 膜タンパク質の立体構造を基盤とする腸管モデル細胞を用いた鉄イオン吸収メカニズムの解析 Invited

    澤井仁美

    2021年度生理研研究会『上皮膜輸送の多様性・調和機構を基盤とする異分野融合研究の創出』  2021.09 

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    Presentation type：Oral presentation (invited, special)  

  • Structural basis for the multifunctionality of the heme-responsive sensor protein for heme detoxification in hemolytic bacteria [Invited Lecture] Invited International conference

    Hitomi Sawai

    11th International Conference on Porphyrins and Phthalocyanines (ICPP-11)  2021.06 

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    Presentation type：Oral presentation (invited, special)  

  • Structural basis for the multifunctionality of the heme-responsive sensor protein for heme detoxification in hemolytic bacteria Invited

    Hitomi Sawai

    11th International Conference on Porphyrins and Phthalocyanines (ICPP-11)  2021.06 

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    Presentation type：Oral presentation (invited, special)  

  • ヒトにおける鉄イオンの吸収に関わる膜タンパク質の構造機能相関と腸管細胞モデルでの機能評価系を用いた鉄イオン吸収を向上させる新たな化合物スクリーニング [招待講演] Invited Domestic conference

    澤井仁美

    日本薬学会 第141年会 環境・衛生部会若手研究者シンポジウム ～金属研究の新たな切り口：分子からヒトを対象とした研究最前線～  2021.03  日本薬学会

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    Presentation type：Oral presentation (invited, special)  

  • Structure-function relation of membrane proteins involved in human iron absorption, and screening of new compounds for iron supplementation using the duodenal enterocyte model system Invited

    Hitomi Sawai

    New perspective on metal research: forefront of research targeting humans from molecules  2021.03 

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    Presentation type：Oral presentation (invited, special)  

  • ヘム応答性センサータンパク質による溶血性細菌の生存の構造的機序 [招待講演] Invited Domestic conference

    澤井仁美

    第94回日本細菌学会総会  2021.03  日本細菌学会

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    Presentation type：Oral presentation (invited, special)  

  • Structural basis for the survival of hemolytic bacteria by a heme-responsive sensor protein Invited

    Hitomi Sawai

    2021.03 

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    Presentation type：Oral presentation (invited, special)  

  • 原子から細胞レベルの研究による鉄イオンの吸収メカニズムの理解と有効な鉄栄養強化食品成分の探索 [招待講演] Invited Domestic conference

    澤井仁美

    第92回日本生化学会大会  2019.09  日本生化学会

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    Presentation type：Oral presentation (invited, special)  

  • 原子から細胞レベルの研究による鉄イオンの吸収メカニズムの理解と有効な鉄栄養強化食品成分の探索 Invited

    澤井仁美

    第92回日本生化学会大会 シンポジウム「生体内におけるSingularity Elementsとしての生体金属の利用と制御」  2019.09 

  • Structural basis for enhancement of human iron absorption by duodenal membrane proteins with ascorbate and dietary metal chelators [Invited Lecture] Invited International conference

    Hitomi Sawai

    Chemistry and Biochemistry Department Seminar in University of Bristol  2019.07  University of Bristol

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    Presentation type：Oral presentation (invited, special)  

    Venue：Bristol, UK  

  • Structural basis for enhancement of human iron absorption by duodenal membrane proteins with ascorbate and dietary metal chelators Invited

    Hitomi Sawai

    Chemistry and Biochemistry Department Seminar in University of Bristol  2019.07 

  • Structural basis for enhancement of human iron absorption by duodenal membrane proteins with some dietary metal-chelators [Invited Lecture] Invited International conference

    Hitomi Sawai

    7th International Symposium on Metallomics  2019.07 

    　More details

    Presentation type：Oral presentation (invited, special)  

    Venue：Warsow, Poland  

  • Structural basis for enhancement of human iron absorption by duodenal membrane proteins with some dietary metal-chelators Invited

    Hitomi Sawai

    7th International Symposium on Metallomics  2019.07 

  • 病原菌の鉄獲得システムで機能するヘムセンサー蛋白質の多機能性とその構造的機序 [招待講演] Invited Domestic conference

    澤井仁美

    第19回日本蛋白質科学会年会／第71回日本細胞生物学会大会合同年次大会  2019.06  日本蛋白質科学会・日本細胞生物学会

    　More details

    Presentation type：Oral presentation (invited, special)  

  • 病原菌の鉄獲得システムで機能するヘムセンサー蛋白質の多機能性とその構造的機序 Invited

    澤井仁美

    第19回日本蛋白質科学会年会／第71回日本細胞生物学会大会合同年次 大会ワークショップCooperative regulation of cellular functions by bio-metals and proteins  2019.06 

  • 「鉄」のバイオサイエンス Invited

    澤井仁美

    兵庫県異分野融合Science & Technologyクラブ  2019.01 

  • Structural basis for enhancement of human iron uptake by duodenal ferric reductase with ascorbate Invited International conference

    Hitomi Sawai

    9th Asian Biological Inorganic Chemistry (AsBIC-9)  2018.12 

    　More details

    Presentation type：Oral presentation (invited, special)  

  • Structural basis for enhancement of human iron uptake by duodenal ferric reductase with ascorbate

    Hitomi Sawai

    9th Asian Biological Inorganic Chemistry (AsBIC-9)  2018.12 

  • Structural basis for promotion of human iron absorption by duodenal ferric reductase with ascorbate and some dietary metal-chelators Invited

    Hitomi Sawai

    Cold Spring Harbor Asia Meeting: Iron, Reactive Oxygen Species & Ferroptosis in Life, Death & Disease  2018.11 

  • ヒトの鉄吸収機構を「膜タンパク質」と「生きた細胞」の研究により相互に理解する [招待講演] Invited Domestic conference

    澤井仁美

    第91回日本生化学会年会   2018.09 

    　More details

    Presentation type：Oral presentation (invited, special)  

  • ヒトの鉄吸収機構を「膜タンパク質」と「生きた細胞」の研究により相互に理解する Invited

    澤井仁美

    第91回日本生化学会年会 ワークショップ「生体金属のMagical Powerとその研究最前線」  2018.09 

  • SEC-SAXS法を用いることで解明できた酸素センサータンパク質システムFixL/FixJの全体像とシグナル伝達機構 [招待講演] Invited Domestic conference

    澤井仁美

    大阪大学蛋白質研究所セミナー／SPring-8先端利用技術ワークショップ 「第２回SPring-8における蛋白質構造生物学研究の現状と将来」  2018.08  大阪大学蛋白質研究所

    　More details

    Presentation type：Oral presentation (invited, special)  

    Venue：大阪  

  • SEC-SAXS法を用いることで解明できた酸素センサータンパク質システムFixL/FixJの全体像とシグナル伝達機構 Invited

    澤井仁美

    大阪大学蛋白質研究所セミナー／SPring-8先端利用技術ワークショップ 「第２回SPring-8における蛋白質構造生物学研究の現状と将来」  2018.08 

  • ヒトの鉄吸収に関わる膜貫通型鉄還元酵素の立体構造に基づく生きた細胞での機能解析 [招待講演] Invited Domestic conference

    澤井仁美

    第18回日本蛋白質科学会年会  2018.06  日本蛋白質科学会

    　More details

    Presentation type：Oral presentation (invited, special)  

  • ヒトの鉄吸収に関わる膜貫通型鉄還元酵素の立体構造に基づく生きた細胞での機能解析 Invited

    澤井仁美

    第18回日本蛋白質科学会年会 ワークショップ「金属イオンとタンパク質: その密接な関係が破綻するとき」  2018.06 

  • 完全な酸素センシングシステムにおける分子内および分子間のシグナル伝達機構 [招待講演] Invited Domestic conference

    澤井仁美

    第17回蛋白質科学会年会  2017.06  日本蛋白質科学会

    　More details

    Presentation type：Oral presentation (invited, special)  

  • 完全な酸素センシングシステムにおける分子内および分子間のシグナル伝達機構 Invited

    澤井仁美

    第17回蛋白質科学会年会 新学術領域研究 「酸素生物学」共催ワークショップ「酸素センシングの蛋白質科学」  2017.06 

  • Biometal Science of Membrane Proteins [Invited Lecture] Invited International conference

    Hitomi Sawai

    University of Strasbourg-RIKEN Workshop on Membrane Lipidology  2017.03  University of Strasbourg & RIKEN

    　More details

    Presentation type：Oral presentation (invited, special)  

    Venue：Strasbourg, France  

  • Biometal Science of Membrane Proteins Invited

    University of Strasbourg-RIKEN Workshop on Membrane Lipidology  2017.03 

  • Overall Architectures of Two-Component Signal Transduction Proteins [Invited Lecture] Invited International conference

    Hitomi Sawai

    9th Korea-Japan Seminars on Biomolecular Sciences: Experiments and Simulations  2016.11 

    　More details

    Presentation type：Oral presentation (invited, special)  

    Venue：Gyeongju, South Korea  

  • Overall Architectures of Two-Component Signal Transduction Proteins Invited

    Hitomi Sawai

    9th Korea-Japan Seminars on Biomolecular Sciences: Experiments and Simulations  2016.11 

  • Architecture of Full-Length Oxygen Sensor Protein Revealed by Small-Angle X-ray Scattering [Invited Lecture] Invited International conference

    Hitomi Sawai

    RIKEN SPring-8 Center/University of Hyogo/University of Liverpool Mini Symposium  2016.04  RIKEN SPring-8 Center

    　More details

    Presentation type：Oral presentation (invited, special)  

    Venue：RIKEN SPring-8 Center  

  • Architecture of Full-Length Oxygen Sensor Protein Revealed by Small-Angle X-ray Scattering Invited

    Hitomi Sawai

    RIKEN SPring-8 Center/University of Hyogo/University of Liverpool Mini Symposium  2016.04 

  • 気体分子センサータンパク質における機能制御メカニズムの革新的理解のために [招待講演] Invited Domestic conference

    澤井仁美

    第38回日本分子生物学会年会 第88回日本生化学会大会 合同大会 (BMB2015)   2015.12  日本分子生物学会ならびに日本生化学会

    　More details

    Presentation type：Oral presentation (invited, special)  

  • 気体分子センサータンパク質における機能制御メカニズムの革新的理解のために Invited

    第38回日本分子生物学会年会 第88回日本生化学会大会 合同大会 (BMB2015) ワークショップ「生体金属の最前線」  2015.12 

  • ヘムセンサー蛋白質を介した細胞内ヘムの恒常性維持機構 [招待講演] Invited Domestic conference

    澤井仁美

    分子研研究会  2013.02  分子科学研究所

    　More details

    Presentation type：Oral presentation (invited, special)  

    Venue：愛知  

  • ヘムセンサー蛋白質を介した細胞内ヘムの恒常性維持機構 Invited

    澤井仁美

    分子研研究会  2013.02 

  • Structural characterization of Aer2 that employs a heme as an oxygen sensor for aerotaxis control [Invited Lecture] Invited International conference

    Hitomi Sawai

    4th Japan-Korea Seminars on Biomolecular Sciences: Experiments and Simulations  2012.01 

    　More details

    Presentation type：Oral presentation (invited, special)  

  • Structural characterization of Aer2 that employs a heme as an oxygen sensor for aerotaxis control Invited

    Hitomi Sawai

    4th Japan-Korea Seminars on Biomolecular Sciences: Experiments and Simulations  2012.01 

  • X-ray crystal structure of the Michaelis complex of a novel heme enzyme, aldoxime dehydratase [Invited Lecture] Invited International conference

    Hitomi Sawai

    3rd Korea-Japan Seminars on Biomolecular Sciences: Experiments and Simulations  2011.02 

    　More details

    Presentation type：Oral presentation (invited, special)  

    Venue：Jeju, South Korea  

  • X-ray crystal structure of the Michaelis complex of a novel heme enzyme, aldoxime dehydratase Invited

    Hitomi Sawai

    3rd Korea-Japan Seminars on Biomolecular Sciences: Experiments and Simulations  2011.02 

  • X-ray crystal structure of the Michaelis complex of a novel heme enzyme, aldoxime dehydratase. [Invited Lecture] Invited International conference

    Hitomi Sawai

    2010 International Chemical Congress of Pacific Basin Societies (PACIFICHEM 2010)  2010.12 

    　More details

    Presentation type：Oral presentation (invited, special)  

    Venue：Honolulu, USA  

  • X-ray crystal structure of the Michaelis complex of a novel heme enzyme, aldoxime dehydratase Invited

    Hitomi Sawai

    2010 International Chemical Congress of Pacific Basin Societies (PACIFICHEM 2010)  2010.12 

  • Structural basis for promotion of human iron absorption by duodenal ferric reductase with ascorbate and some dietary metal-chelators [Invited Lecture] Invited

    Hitomi Sawai

    Cold Spring Harbor Asia Meeting: Iron, Reactive Oxygen Species & Ferroptosis in Life, Death & Disease  Cold Spring Harbor Asia

    　More details

    Presentation type：Oral presentation (invited, special)  

    Venue：Suzhou, China  

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Grant-in-Aid for Scientific Research

  • 生命金属動態に関与するタンパク質分子の構造機能ダイナミクス研究

    Grant-in-Aid for Scientific Research on Innovative Areas  2019.06

  • 生体金属イオンの輸送システムで機能する膜タンパク質の構造解析

    Grant-in-Aid for Scientific Research(B)  2018.04

  • 一酸化窒素の生体内動態の分子科学

    Grant-in-Aid for Scientific Research(S)  2014.05

  • 腸管上皮細胞内における鉄イオン輸送の分子機序の解明

    Grant-in-Aid for Scientific Research(C)  2021.04

  • ヒトの鉄吸収に関わる膜タンパク質の立体構造を基盤とした生細胞での構造機能相関解析

    Grant-in-Aid for Scientific Research(C)  2018.04

  • ヘムシャペロンHRG-3による細胞間ヘム輸送の分子機構 研究課題

    Grant-in-Aid for Early-Career Scientists  2013.04

  • ヘム含有PASドメインをセンサーとする新規なシグナル伝達タンパク質の構造と機能

    Grant-in-Aid for Research Activity Start-up  2010

  • ヘムを活性中心とする気体センサータンパク質の構造と機能の相関

    Grant-in-Aid for JSPS Fellows  2007.04

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Incentive donations / subsidies

  • 鉄栄養素の吸収効率を高める新たな食品成分の探索とその作用機序の解明

    公益財団法人アサヒグループ財団  学術研究助成 食・生活部門  2024.04

  • 細胞内ヘム濃度の恒常性維持に関わる分子機構の解明

    株式会社資生堂  資生堂女性研究者サイエンスグラント研究助成金   2013

  • 新規な酸素センサータンパク質Aer2の構造機能解析および細胞内酸素濃度センサーの創製

    中央三井信託銀行  公益信託山村富美記念女性自然科学者研究助成基金   2010

  • 鉄トランスポーターと鉄輸送シャペロンの相互作用による安全で効率的な細胞内Fe2+制御機構の解明

    公益財団法人 旭硝子財団  2024年度研究助成プログラム  2024.04

  • 鉄欠乏症改善のための食品添加物の利用効果の検証とその作用機序の解明

    公益財団法人日本食品化学研究振興財団  令和２年度研究助成金   2020.04

  • 病原菌の鉄源としてのヘムの濃度を感知するタンパク質の分子機構解析

    公益財団法人ひょうご科学技術協会  学術研究助成   2019.04

  • 脂質-膜タンパク質の分子間相互作用の研究

    理化学研究所  独創的課題「脂質の統合的理解」   2014.04

  • 高分解能Ｘ線結晶構造解析によるヘム輸送機構の解明

    公益財団法人ひょうご科学技術協会  学術研究助成   2014

  • ヒトおよび寄生原虫由来ヘム輸送蛋白質のＸ線結晶構造解析

    公益財団法人兵庫県立大学科学技術後援財団  教育研究助成   2014

  • 生体内ヘム輸送の分子科学を基盤とする寄生原虫に特異的な阻害剤の設計

    公立大学法人兵庫県立大学  特別研究助成金  2013

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Charge of off-campus class subject

  • 化学・物質工学特別演習Ⅱ

    2024.04
    -
    Now

  • 医工連携B：先端医用材料・創薬

    2024.04
    -
    Now

  • Protein Engineering

    2024.04
    -
    Now
    Institution：School of Engineering, Nagasaki University

  • 細胞機能生化学特論

    2024.04
    -
    Now

  • 特別研究

    2024.04
    -
    Now

  • 機能性錯体化学特論

    2024.04
    -
    Now

  • Advanced Functional Molecular Chemistry

    2024.04
    -
    Now
    Institution：Graduate School of Integrated Science and Technology, Nagasaki University

  • Special Lectures on Science and Technology

    2023.08
    -
    Now
    Institution：Graduate School of Engineering, Nagasaki University

  • Structure and Function of Biological Molecules

    2023.06
    -
    Now
    Institution：Nagasaki University

  • First-Year Seminar

    2023.04
    -
    Now
    Institution：Nagasaki University

  • Biochemistry I

    2023.04
    -
    Now
    Institution：Nagasaki University

  • Advance course of Integrated Bio-metal Science

    2023
    -
    Now
    Institution：Graduate School of Engineering, Nagasaki University

  • Lab Course for Chemistry and Materials Engineering C: Biochemistry

    2022.09
    -
    Now
    Institution：Nagasaki University

  • Technical English III

    2022.09
    -
    Now
    Institution：Nagasaki University

  • 化学・物質工学総合演習

    2022.05
    -
    Now

  • Technical English A, B, C, D

    2022.05
    -
    Now
    Institution：Nagasaki University

  • 英語科学問題演習「生化学」

    2021
    Institution：University of Hyogo

  • Purification and functional analysis of egg white lysozyme and mushroom tyrosinase

    2020
    -
    2022
    Institution：University of Hyogo

  • Purification and activity assay of cytochrome c oxidase from bovine heart

    2013
    -
    2022
    Institution：University of Hyogo

  • Functional properties of urease from beans

    2013
    -
    2022
    Institution：University of Hyogo

  • Purification and crystallization of lactate dehydrogenase from bovine heart

    2013
    -
    2019
    Institution：University of Hyogo

▼display all

Social Activities　⇒ Link to the list of Social Activities

  • からだの中ではたらく「鉄」～生きるために必要な金属～

    Role(s)： Guest,　Media coverage,　Lecturer,　Official expert

    Type： Internet

    フロムページ  夢ナビライブ講義  2024.06

  • 在マルセイユ日本国総領事公邸を訪問

    Type： Other

    https://www.nagasaki-u.ac.jp/ja/news/news4289.html  2024.04

  • Gordon Research Conference: Chemistry and Biology of Tetrapyrroles対面参加のご報告

    Role(s)： Official expert,　Report author,　Contributor

    Type： Promotional material

    新学術領域研究「生命金属科学」分野の創成による生体内金属動態の統合的研究  新学術領域研究「生命金属科学」ニュースレター 第4巻・第6号（通算第37号）  2022.09

  • お仕事インタビュー企画③ ～ 金属触媒で地球に優しいクルマづくりに挑戦する女性研究者に会ってきました！～

    Role(s)： Interviewer,　Edit,　Official expert,　Planner,　Contributor

    Type： Promotional material

    新学術領域研究「生命金属科学」ニュースレター 第3巻・第10号（通算第29号）  2022.01

  • ラジオ関西に出演！

    Type： Internet

    兵庫県立大学  ケンダイツウシン（兵庫県立大学通信）  2022.01

  • Let's understand how iron works in our body!

    Role(s)： Guest

    Type： TV or radio program

    Radio KANSAI  Radio KANSAI  2022.01

  • お仕事インタビュー企画① ～シオノギ製薬で生命金属関連のお薬を創った化学者に会ってきました！～

    Role(s)： Interviewer,　Official expert,　Planner,　Contributor

    Type： Promotional material

    新学術領域研究「生命金属科学」ニュースレター 第3巻・第8号（通算第27号）  2021.11

  • 身体の中にある金属のはたらき

    Role(s)： Lecturer

    Type： Visiting lecture

    兵庫県立川西明峰高校  2021.07

  • 夏の自由研究 ～暑さに負けるな！鉄分補給のすすめ～

    Role(s)： Official expert,　Contributor

    Type： Promotional material

    新学術領域研究「生命金属科学」ニュースレター 第3巻・第3号（通算第22号）  2021.06

  • 身体の中で金属がはたらく仕組み

    Role(s)： Lecturer

    Type： Visiting lecture

    兵庫県立宝塚北高校  2019.08

  • 女性研究者とおしゃべりしよう！資生堂サイエンスカフェ in 分子研

    Role(s)： Guest,　Panelist,　Media coverage

    Type： Science cafe

    株式会社 資生堂  2012.10

  • Hyogo EYE 科学研究の第一線をたずねて～病原菌が菌体内のヘム濃度を感知するメカニズムを原子レベルで解明～

    Role(s)： Media coverage,　Official expert,　Contributor

    Type： Promotional material

    公益財団法人ひょうご科学技術協会  ひょうごサイエンス38号 

  • 研究最前線ビデオシリーズ①「生体内の鉄の動態と機能」

    Role(s)： Guest,　Edit,　Official expert,　Planner

    Type： Internet

    新学術領域研究「生命金属科学」分野の創成による生体内金属動態の統合的研究 

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Media Coverage

  • 東大・兵庫県立大・理研など、ヘム濃度センサータンパク質の立体構造を決定し作動機序を原子レベルで解明 Newspaper, magazine

    日本経済新聞  2021.04

  • 兵庫県立大と理研など、ビタミンCが鉄分の吸収を促進するメカニズムを原子レベルで解明 Newspaper, magazine

    日本経済新聞  2018.08

  • 酸素感知システムの構成: 根粒菌のタンパク質形状を解明 Newspaper, magazine

    科学新聞  2018.04

  • 理研と兵庫県立大など、土壌中の酸素濃度を感知して植物に窒素栄養を 供給するタンパク質の全体像を解明 Newspaper, magazine

    日本経済新聞  2018.04

  • 合成酵素と分解酵素が複合体形成 – 生体内 効率的にNO分解 Newspaper, magazine

    科学新聞  2017.09

  • 女性科学者が高校生らと語る Newspaper, magazine

    中日新聞  2012.10

  • 細胞内ヘム濃度を維持 – 原子レベルで仕組み解明 Newspaper, magazine

    科学新聞  2012.09

  • 鉄分の体内濃度 – 鍵はタンパク質 Newspaper, magazine

    中日新聞  2012.08

  • 生命維持に欠かせぬ「ヘム」濃度 – 調節たんぱく質特定 Newspaper, magazine

    日刊工業新聞  2012.08

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Academic Activities

  • 第98回日本生化学会大会シンポジウム:「知る」から「探る」生命金属 ～生物40億年の知恵を活用できるか～

    Role(s)： Planning, management, etc.,　Panel moderator, session chair, etc.

    石森 浩一郎、澤井 仁美  （ 京都 ） 2025.11

    　More details

    Type：Competition, symposium, etc. 

  • Next generation of Life Science with metals: Regulation of lives, foods, and environments by metals

    Role(s)： Planning, management, etc.,　Panel moderator, session chair, etc.

    Japan Society for Bioscience, Biotechnology, and Agrochemistry  2024.03

    　More details

    Type：Competition, symposium, etc. 

  • 「第35回生物無機化学夏季セミナー」企画・運営代表

    Role(s)： Planning, management, etc.,　Panel moderator, session chair, etc.,　Review, evaluation,　Peer review

    生物無機化学研究会  2023.09

    　More details

    Type：Academic society, research group, etc. 

  • Workshop on "Metal homeostasis – Mechanisms regulating physiological phenomena through bio-metals in vivo"

    Role(s)： Planning, management, etc.,　Panel moderator, session chair, etc.

    Hitomi Sawai, Yoshiaki Furukawa  2023.07

    　More details

    Type：Competition, symposium, etc. 

  • Local Organizing Committee, Session Organizera and Chair in 10th Asian Biological Inorganic Chemistry Conference (AsBIC-10)

    Role(s)： Planning, management, etc.,　Panel moderator, session chair, etc.

    2022.11 - 2022.12

    　More details

    Type：Academic society, research group, etc. 

  • 第95回日本生化学会大会 新学術領域研究「生命金属科学」共催シンポジウム『生命の階層構造の観点から生命金属の役割を探る』

    Role(s)： Panel moderator, session chair, etc.

    神戸大朋、津本浩平  2022.11

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    Type：Academic society, research group, etc. 

  • メタルバイオサイエンス研究会2022 新学術領域研究「生命金属科学」共催シンポジウム "メタルバイオサイエンスの未来を拓く生物無機化学への招待" オーガナイザー

    Role(s)： Planning, management, etc.,　Panel moderator, session chair, etc.

    日本毒性学会生体金属部会  2022.10

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    Type：Competition, symposium, etc. 

  • メタルバイオサイエンス研究会2022シンポジウム「メタルバイオサイエンスの未来を拓く生物無機化学への招待」オーガナイザー

    Role(s)： Planning, management, etc.,　Panel moderator, session chair, etc.

    Hitomi Sawai, Norifumi Muraki  2022.10

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  • 日本農芸化学会2022年度西日本支部大会 実行委員

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    日本農芸化学会西日本支部  2022.09

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    Type：Academic society, research group, etc. 

  • 第58回日本生物物理学会年会 新学術領域共催シンポジウム "New Frontiers of 'Bio-metal Science' Opened with Cutting-Edge Techniques (最先端計測技術で拓く「生命金属科学」の新たなフロンティア）"

    Role(s)： Planning, management, etc.,　Panel moderator, session chair, etc.

    石森浩一郎、澤井仁美  2020.09

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    Type：Competition, symposium, etc. 

  • 第92回日本生化学会大会 公募シンポジウム「生体内におけるSingularity Elementsとしての生体金属の利用と制御」

    Role(s)： Planning, management, etc.,　Panel moderator, session chair, etc.

    石森浩一郎、澤井仁美  2019.09

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    Type：Competition, symposium, etc. 

  • Kick-off Symposium of Integrated Bio-metal Science - Young Scientist Satellite Workshop

    Role(s)： Planning, management, etc.,　Panel moderator, session chair, etc.

    澤井仁美、村木則文  2019.09

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    Type：Competition, symposium, etc. 

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