2012 Fiscal Year Final Research Report
Structural Study of the Mechanism of Hydrogen Activation on Ni-enzymes
| Project/Area Number |
22370061
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | University of Hyogo |
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Principal Investigator |
HIGUCHI Yoshiki 兵庫県立大学, 大学院・生命理学研究科, 教授 (90183574)
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| Co-Investigator(Renkei-kenkyūsha) |
SHOMURA Yasuhito 兵庫県立大学, 大学院・生命理学研究科, 助教 (50423900)
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| Project Period (FY) |
2010 – 2012
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| Keywords | ヒドロゲナーゼ / X線結晶解析 / 反応機構 / Ni酵素 / 燃料電池 |
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| Research Abstract |
We have studied newly found NAD+-reducing four subunits [NiFe] hydrogenase and O_2-tolerant membrane-bound [NiFe] hydrogenase (MBH) in this project. In 2010-2012, we have developed the new protocols for inoculation of the bacterium and purification for NAD+-reducing four subunits [NiFe] hydrogenase. For MBH, the x-ray crystal structures of as-isolated, H2-reduced and chemically super-oxidized MBH at high resolution has been successfully determined. Overall structure of the molecule and the coordination geometry of the Dinuclear Ni-Fe active site of the MBH are almost identical to those of the standard O_2-sensitive [NiFe] hydrogenase. The proximal iron-sulfur (Fe-S) cluster, however, has a [4Fe-3S]-6Cys structure. When the enzyme is chemically oxidized, the cluster supplies additional electrons to the Ni-Fe active site, and a deprotonated amide nitrogen of the polypeptide backbone coordinates the Fe atom stabilizing the super-oxidized state of the cluster.
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Research Products
(61 results)
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[Journal Article] The Three-dimensional Structure of Nylon Hydrolase and The Mechanism of Nylon-6 Hydrolysis2012
Author(s)
S. Negoro, N. Shibata., Y. Tanaka ,K. Yasuhira, H. Shibata, H. Hashimoto, Y.-H. Lee, S. Oshima, R. Santa, S. Oshima, K. Mochiji, Y. Goto, T. Ikegami, K. Nagai, D. Kato, M. Takeo and Y. Higuchi
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Journal Title
J. Biol. Chem
Volume: 287
Pages: 5079-5090
DOI
Peer Reviewed
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[Journal Article] S. Terawaki, K. Yano, T. Katsutani, K. Shiomi, K. Keino-Masu, M. Masu, Y. Shomura, H. Komori, N. Shibata and Y. Higuchi2011
Author(s)
S. Terawaki, K. Yano, T. Katsutani, K. Shiomi, K. Keino-Masu, M. Masu, Y. Shomura, H. Komori, N. Shibata and Y. Higuchi
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Journal Title
Acta Crystallgor.
Volume: F67
Pages: 758-761
DOI
Peer Reviewed
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[Journal Article] Cytochrome c polymerization by successive domain swapping at the C-terminal helix2010
Author(s)
S. Hirota, Y. Hattori, S. Nagao, M. Taketa, H. Komori, H. Kamikubo, Z. Wang, I. Takahashi, S. Negi, Y. Sugiura, M. Kataoka, Y. Higuchi
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Journal Title
Pro. Natl. Acad. Sci
Volume: 107(29)
Pages: 12854-12859
DOI
Peer Reviewed
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[Journal Article] Crystal Structures of Ethanolamine Ammonia-lyase complexed with Coenzyme B_12 Analogs and Substrates2010
Author(s)
N. Shibata, H. Tamagaki, N. Hieda, K. Akita, H. Komori, Y. Shomura, S. Terawaki, K. Mori, N. Yasuoka, Y. Higuchi, and T. Toraya
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Journal Title
J. Biol. Chem
Volume: 285 (34)
Pages: 26484-26493
DOI
Peer Reviewed
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[Journal Article] X-ray Crystallographic Analysis of the 6-aminohexanoate Cyclic Dimer Hydrolase: Catalytic Mechanism and Evolution of an Enzyme Responsible for Nylon-6 Byproduct Degradation2010
Author(s)
K. Yasuhira, N. Shibata, G. Mongami, Y. Uedo, Y. Atsumi, Y. Kawashima, A. Hibino, Y. Tanaka, Y-H. Lee, D. Kato, M. Takeo, Y. Higuchi, and S. Negoro
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Journal Title
J. Biol. Chem
Volume: 285
Pages: 1239-1248
DOI
Peer Reviewed
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[Journal Article] Expression, Crystallization and Preliminary X-ray Crystallographic Study of Ethanolamine Ammonia-lyase from Escherichia coli2010
Author(s)
N. Shibata, H. Tamagaki, S. Ohtsuki, N. Hieda, K. Akita, H. Komori, Y. Shomura, S. Terawaki, T. Toraya, N. Yasuoka and Y. Higuchi
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Journal Title
Acta Crystallogr.
Volume: F66
Pages: 709-711
DOI
Peer Reviewed
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