| アイテムタイプ |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2026-01-28 |
| タイトル |
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タイトル |
Structural basis of hydride and proton transfer reactions revealed by the detection of hydrogen atoms in mammalian NADH-cytochrome b5 reductase |
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言語 |
en |
| 言語 |
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言語 |
eng |
| 資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
| 著者 |
Hirano Yuu
Kurihara Kazuo
Katsuhiro Kusaka
Andreas Osterman
Masahide Hikita
Shigenobu Kimura
Kunio Miki
Tamada Taro
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| 抄録 |
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内容記述タイプ |
Abstract |
|
内容記述 |
Many structural studies have been reported for ferredoxin:NADP+ reductase family members, but an experimental validation of the catalytic hydride and proton transfer steps through a direct detection of the involved hydrogen atoms has not been achieved so far. Here, we determined high-resolution X-ray and neutron crystal structures of NADH-cytochrome b5 reductase, which acts as an electron supplier for various metabolic processes and mediates hydride and proton transfer reactions via its FAD and NADH cofactors. The X-ray structures identify the FADH--NAD+ and FAD-NADH complexes based on the electron densities of the hydrogen atoms bound to the cofactors. The neutron structures determined at different pD-values show a difference in the protonation state of the histidine residue in the hydrogen-bond network from FAD to the protein surface. The observation of the hydrogen atoms reveals the structural basis for the hydride and proton transfer reactions catalyzed by NADH-cytochrome b5 reductase. |
| 書誌情報 |
Structure
巻 34,
号 1,
p. 76-86000,
発行日 2026-01
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| DOI |
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識別子タイプ |
DOI |
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関連識別子 |
10.1016/j.str.2025.10.006 |
