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Towards cryogenic neutron crystallography on the reduced form of [NiFe]-hydrogenase
https://repo.qst.go.jp/records/80463
https://repo.qst.go.jp/records/80463ef4bdd51-96c3-4722-8c45-f78fc97b8b5a
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2020-09-10 | |||||
| タイトル | ||||||
| タイトル | Towards cryogenic neutron crystallography on the reduced form of [NiFe]-hydrogenase | |||||
| 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_6501 | |||||
| 資源タイプ | journal article | |||||
| 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× Inoue, Seiya× Matsuura, Hiroaki× Hirano, Yu× Kurihara, Kazuo× Kusaka, Katsuhiro× Cuneo, Matthew× Coates, Leighton× Tamada, Taro× Higuchi, Yoshiki× Takeshi, Hiromoto× Yuu, Hirano× Kazuo, Kurihara× Taro, Tamada |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | A membrane-bound hydrogenase from Desulfovibrio vulgaris Miyazaki F is a metalloenzyme that contains a binuclear Ni–Fe complex in its active site and mainly catalyzes the oxidation of molecular hydrogen to generate a proton gradient in the bacterium. The active-site Ni–Fe complex of the aerobically purified enzyme shows its inactive oxidized form, which can be reactivated through reduction by hydrogen. Here, in order to understand how the oxidized form is reactivated by hydrogen and further to directly evaluate the bridging of a hydride ligand in the reduced form of the Ni–Fe complex, a neutron structure determination was undertaken on single crystals grown in a hydrogen atmosphere. Cryogenic crystallography is being introduced into the neutron diffraction research field as it enables the trapping of short-lived intermediates and the collection of diffraction data to higher resolution. To optimize the cooling of large crystals under anaerobic conditions, the effects on crystal quality were evaluated by X-rays using two typical methods, the use of a cold nitrogen gas stream and plunge-cooling into liquid nitrogen, and the former was found to be more effective in cooling the crystals uniformly than the latter. Neutron diffraction data for the reactivated enzyme were collected at the Japan Photon Accelerator Research Complex under cryogenic conditions, where the crystal diffracted to a resolution of 2.0 angstroms. A neutron diffraction experiment on the reduced form was carried out at Oak Ridge National Laboratory under cryogenic conditions and showed diffraction peaks to a resolution of 2.4 angstroms. | |||||
| 書誌情報 |
Acta Crystallographica Section D 巻 D76, p. 946-953, 発行日 2020-09 |
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| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 2059-7983 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1107/S2059798320011365 | |||||
| 関連サイト | ||||||
| 識別子タイプ | URI | |||||
| 関連識別子 | http://scripts.iucr.org/cgi-bin/paper?S2059798320011365 | |||||
