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Neutron crystal structure studies of the oxidized form of NADH-cytochrome b5 reductase
https://repo.qst.go.jp/records/73076
https://repo.qst.go.jp/records/730767fe8ff66-5313-4a4f-9241-7363f041c196
| Item type | 会議発表用資料 / Presentation(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2018-12-10 | |||||
| タイトル | ||||||
| タイトル | Neutron crystal structure studies of the oxidized form of NADH-cytochrome b5 reductase | |||||
| 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 |
平野, 優
× 平野, 優× 栗原, 和男× Ostermann, Andreas× Kusaka, Katsuhiro× Kimura, Shigenobu× Miki, Kunio× 玉田, 太郎× 平野 優× 栗原 和男× 玉田 太郎 |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Many redox proteins possess cofactors, such as heme, FAD, and Fe-S cluster and the cofactors are involved in the chemical reactions of redox proteins. The redox reactions in proteins usually associate with the movement of hydrogen atoms and/or valence electrons through the cofactors. High-resolution neutron and X-ray structure analyses can provide the information about hydrogen atoms and valence electrons and are important for understanding molecular mechanisms of redox reactions in proteins. NADH-cytochrome b5 reductase (b5R) catalyzes the electron transfer from two-electron carriers of NADH to one-electron acceptor of cytochrome b5 (b5). High-resolution X-ray structure analyses have been reported for b5R and b5 from porcine liver. We prepared large crystals (> 1mm3) of the oxidized form of b5R for neutron diffraction experiments in the different pH conditions (6.5 and 7.5). We have successfully collected neutron diffraction data sets at high-resolutions of 1.40 Å (at iBIX in J-PARC) and 1.45 Å (at BIODIFF in FRM II). The diffraction data sets of iBIX were collected by the TOF-Laue method which utilizes white-pulsed neutrons. The integrated intensities of the iBIX data were corrected by applying wavelength normalization. The neutron structures obtained in different pH conditions show small structural changes in the hydrogen-bond network from FAD to the protein surface. | |||||
| 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 | Asian Crystallographic Association Conference 2018 | |||||
| 発表年月日 | ||||||
| 日付 | 2018-12-03 | |||||
| 日付タイプ | Issued | |||||
