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Kinetic and structural insight into a role of the re-face Tyr328 residue of the homodimer type ferredoxin-NADP+ oxidoreductase from Rhodopseudomonas palustris in the reaction with NADP+/NADPH
https://doi.org/10.24517/00059001
https://doi.org/10.24517/0005900197e655b1-db8c-452e-ae24-1a44d513cbff
| 名前 / ファイル | ライセンス | アクション |
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SC-PR-SEO-D-148140.pdf (9.6 MB)
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| アイテムタイプ | 学術雑誌論文 / Journal Article(1) | |||||||
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| 公開日 | 2020-08-03 | |||||||
| タイトル | ||||||||
| タイトル | Kinetic and structural insight into a role of the re-face Tyr328 residue of the homodimer type ferredoxin-NADP+ oxidoreductase from Rhodopseudomonas palustris in the reaction with NADP+/NADPH | |||||||
| 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 | |||||||
| ID登録 | ||||||||
| ID登録 | 10.24517/00059001 | |||||||
| ID登録タイプ | JaLC | |||||||
| 著者 |
Seo, Daisuke
× Seo, Daisuke× Muraki, Norifumi× Kurisu, Genji |
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| 著者別表示 |
瀬尾, 悌介
× 瀬尾, 悌介
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| 提供者所属 | ||||||||
| 内容記述タイプ | Other | |||||||
| 内容記述 | 金沢大学理工研究域物質化学系 | |||||||
| 書誌情報 |
Biochimica et Biophysica Acta (BBA) - Bioenergetics 巻 1861, 号 3, p. 148140, 発行日 2020-03-01 |
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| 収録物識別子タイプ | ISSN | |||||||
| 収録物識別子 | 0006-3002 | |||||||
| NCID | ||||||||
| 収録物識別子タイプ | NCID | |||||||
| 収録物識別子 | AA00564635 | |||||||
| DOI | ||||||||
| 関連タイプ | isVersionOf | |||||||
| 識別子タイプ | DOI | |||||||
| 関連識別子 | 10.1016/j.bbabio.2019.148140 | |||||||
| 出版者 | ||||||||
| 出版者 | Elsevier | |||||||
| 抄録 | ||||||||
| 内容記述タイプ | Abstract | |||||||
| 内容記述 | Among the thioredoxin reductase-type ferredoxin-NAD(P)+ oxidoreductase (FNR) family, FNR from photosynthetic purple non‑sulfur bacterium Rhodopseudomonas palustris (RpFNR) is distinctive because the predicted residue on the re-face of the isoalloxazine ring portion of the FAD prosthetic group is a tyrosine. Here, we report the crystal structure of wild type RpFNR and kinetic analyses of the reaction of wild type, and Y328F, Y328H and Y328S mutants with NADP+/NADPH using steady state and pre-steady state kinetic approaches. The obtained crystal structure of wild type RpFNR confirmed the presence of Tyr328 on the re-face of the isoalloxazine ring of the FAD prosthetic group through the unique hydrogen bonding of its hydroxyl group. In the steady state assays, the substitution results in the decrease of Kd for NADP+ and KM for NADPH in the diaphorase assay; however, the kcat values also decreased significantly. In the stopped-flow spectrophotometry, mixing oxidized RpFNRs with NADPH and reduced RpFNRs with NADP+ resulted in rapid charge transfer complex formation followed by hydride transfer. The observed rate constants for the hydride transfer in both directions were comparable (>400 s−1). The substitution did not drastically affect the rate of hydride transfer, but substantially slowed down the subsequent release and re-association of NADP+/NADPH in both directions. The obtained results suggest that Tyr328 stabilizes the stacking of C-terminal residues on the isoalloxazine ring portion of the FAD prosthetic group, which impedes the access of NADP+/NADPH on the isoalloxazine ring portions, in turn, enhancing the release of the NADP+/NADPH and/or reaction with electron transfer proteins. © 2019 Elsevier B.V. | |||||||
| 内容記述 | ||||||||
| 内容記述タイプ | Other | |||||||
| 内容記述 | Embargo Period 12 months | |||||||
| 権利 | ||||||||
| 権利情報 | Copyright © 2020 Elsevier B.V. (CC-BY NC ND) | |||||||
| 著者版フラグ | ||||||||
| 出版タイプ | AM | |||||||
| 出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||||
| 関連URI | ||||||||
| 識別子タイプ | URI | |||||||
| 関連識別子 | https://www.sciencedirect.com/science/article/pii/S000527281930194X?via%3Dihub | |||||||
| 関連名称 | https://www.sciencedirect.com/science/article/pii/S000527281930194X?via%3Dihub | |||||||
| 関連URI | ||||||||
| 識別子タイプ | URI | |||||||
| 関連識別子 | http://www.elsevier.com/locate/issn/00063002 | |||||||
| 関連名称 | http://www.elsevier.com/locate/issn/00063002 | |||||||
