8 0 0 0 OA 金属酵素の結晶構造化学的研究:ヒドロゲナーゼの反応機構について
- 著者
- 緒方 英明
- 出版者
- 日本結晶学会
- 雑誌
- 日本結晶学会誌 (ISSN:03694585)
- 巻号頁・発行日
- vol.63, no.2, pp.97-104, 2021-05-31 (Released:2021-06-05)
- 参考文献数
- 32
The metalloenzyme ‘hydrogenase’ catalyzes the reversible oxidation of dihydrogen. Crystallographic structures of[NiFe]hydrogenases from sulfate-reducing bacteria have been determined and give detailed insight into pathways for the transfer of electrons, protons and hydrogen molecules.[NiFe]hydrogenases contain one nickel and one iron in the active site, the latter carries non-protein diatomic ligands, one CO and two CN-s. A possible catalytic mechanism of the oxygen-sensitive[NiFe]hydrogenases for the heterolytic dihydrogen splitting is proposed.
1 0 0 0 OA ヒドロゲナーゼの超高分解能X線結晶構造解析
- 著者
- 緒方 英明
- 出版者
- 日本結晶学会
- 雑誌
- 日本結晶学会誌 (ISSN:03694585)
- 巻号頁・発行日
- vol.57, no.6, pp.344-349, 2015-12-31 (Released:2015-12-27)
- 参考文献数
- 21
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.