X-ray structural study of the membrane-bound[NiFe]-hydrogenase
Project/Area Number |
22770111
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Single-year Grants |
Research Field |
Structural biochemistry
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Research Institution | University of Hyogo |
Principal Investigator |
SHOMURA Yasuhito 兵庫県立大学, 大学院・生命理学研究科, 助教 (50423900)
|
Project Period (FY) |
2010 – 2011
|
Project Status |
Completed (Fiscal Year 2011)
|
Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2011: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2010: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
|
Keywords | 水素代謝 / 金属タンパク質 / ヒドロゲナーゼ / X線結晶構造解析 / 膜タンパク質 |
Research Abstract |
Hydrogenases play key roles in hydrogen metabolism by catalyzing synthesis and decomposition of molecular hydrogen. While most of the hydrogenases exhibit no activity in the presence of O2, the membrane-bound[NiFe]-hydrogenase is known to be O2-tolerant, of which mechanism had been poorly understood. In this study, X-ray crystal structures of the membrane-bound[NiFe]-hydrogenase have been determined for three different redox states at resolutions of 1.2-1.4 A. One of the Fe-S clusters showed an unprecedented structure and its redox dependent conformational changes, to which the O2-tolerant property of this hydrogenase should be ascribable.
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Report
(3 results)
Research Products
(13 results)
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[Journal Article] Structural and Enzymatic Characterization of BacD, An L-amino Acid Dipeptide Ligase from Bacillus subtilis2012
Author(s)
Shomura, Y., Hinokuchi, E., Ikeda, H., Senoo, A., Takahashi, Y., Saito, J., Komori, H., Shibata, N., Yonetani, Y., Higuchi, Y.
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Journal Title
Protein Sci.
Volume: 21(5)
Pages: 707-716
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