High Resolution Crystal Structure Analysis of [NiFe] Hydrogenase
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- OGATA Hideaki
- Max Planck Institute for Chemical Energy Conversion
Bibliographic Information
- Other Title
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- ヒドロゲナーゼの超高分解能X線結晶構造解析
- ヒドロゲナーゼ ノ チョウコウブンカイノウ Xセン ケッショウ コウゾウ カイセキ
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Description
Hydrogen is known as an ultimate clean energy source and is thus discussed as a future sustainable energy carrier. Hydrogenases catalyze the reversible oxidation of the molecular hydrogen. We report the crystal structure analysis of [NiFe] hydrogenase from sulfate reducer at subatomic resolution. The structure reveals that the hydride bridge between nickel and iron at the active site and the possible proton bound site at the cysteine residue, resulting from the initial heterolytic splitting of dihydrogen by the enzyme. This finally clarifies the initial step in the mechanism of hydrogen conversion.
Journal
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- Nihon Kessho Gakkaishi
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Nihon Kessho Gakkaishi 57 (6), 344-349, 2015
The Crystallographic Society of Japan
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Details 詳細情報について
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- CRID
- 1390282679066431360
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- NII Article ID
- 130005115746
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- NII Book ID
- AN00188364
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- ISSN
- 18845576
- 03694585
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- NDL BIB ID
- 027051946
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed