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Distribution of valence electrons of the flavin cofactor in NADH-cytochrome b5 reductase
https://repo.qst.go.jp/records/47747
https://repo.qst.go.jp/records/47747be29e54c-74e7-4419-8d6a-fa69a12cde91
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2017-04-20 | |||||
| タイトル | ||||||
| タイトル | Distribution of valence electrons of the flavin cofactor in 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_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 |
玉田, 太郎
× 玉田, 太郎× 高場, 圭章(京都大学大学院理学研究科)× 竹田, 一旗(京都大学大学院理学研究科)× 小杉, 正幸(京都大学大学院理学研究科)× 三木, 邦夫(京都大学大学院理学研究科)× 玉田 太郎 |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Flavin compounds such as flavin adenine dinucleotide (FAD), flavin mononucleotide and riboflavin make up the active centers in flavoproteins that facilitate various oxidoreductive processes. The fine structural features of the hydrogens and valence electrons of the flavin molecules in the protein environment are critical to the functions of the flavoproteins. Here we report the charge density analysis of a flavoenzyme, NADH-cytochrome b5 reductase (b5R), at an ultra-high resolution of 0.78 Å. Valence electrons on the FAD cofactor as well as the peptide portion, which are clearly visualized even after the conventional refinement, are analyzed by the multipolar atomic model refinement. The topological analysis for the determined electron density reveals the valence electronic structure of the isoalloxazine ring of FAD and hydrogen-bonding interactions with the protein environment. | |||||
| 書誌情報 |
Scientific Reports (Online Only URL:http://www.nature.com/srep/index.html) 号 7, p. 43162-1-43162-10, 発行日 2017-02 |
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| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 2045-2322 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1038/srep43162 | |||||
