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Neutron diffraction experiments on [NiFe]-hydrogenase crystallized under H2 atmosphere
https://repo.qst.go.jp/records/78365
https://repo.qst.go.jp/records/783657461f924-2965-48c1-90c6-7566072ece56
| Item type | 会議発表用資料 / Presentation(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2019-10-03 | |||||
| タイトル | ||||||
| タイトル | Neutron diffraction experiments on [NiFe]-hydrogenase crystallized under H2 atmosphere | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_c94f | |||||
| 資源タイプ | conference object | |||||
| アクセス権 | ||||||
| アクセス権 | metadata only access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
| 著者 |
Hiromoto, Takeshi
× Hiromoto, Takeshi× Nishikawa, Koji× Matsuura, Hiroaki× Hirano, Yu× Kusaka, Katsuhiro× Cuneo, Matthew× Tamada, Taro× Higuchi, Yoshiki× Hiromoto, Takeshi× Hirano, Yuu× Tamada, Taro |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Hydrogenases that catalyze the reversible oxidation of molecular hydrogen (H2) are involved in energy metabolism in various prokaryotes and some eukaryotes. The “standard” type of [NiFe]-hydrogenases is composed of two (large and small) subunits. The active site Ni-Fe binuclear complex of the “standard” enzyme is located in the protein interior at the interface of the two subunits by coordination of four cysteine residues of the large subunit. In order to clarify how the inactive oxidized form is re-activated by H2 and to observe a bridged hydride in the Ni-Fe complex in the Ni-R form directly, structural analyses using neutron diffraction were undertaken on the crystals prepared in aerobic and anaerobic conditions, respectively. | |||||
| 会議概要（会議名, 開催地, 会期, 主催者等） | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | International Symposium on Diffraction Structure Biology 2019 | |||||
| 発表年月日 | ||||||
| 日付 | 2019-10-18 | |||||
| 日付タイプ | Issued | |||||
