ダウンロード数: 44
このアイテムのファイル:
| ファイル | 記述 | サイズ | フォーマット | |
|---|---|---|---|---|
| s2052252523006437.pdf | 1.55 MB | Adobe PDF | 見る/開く |
| タイトル: | Structure and function relationship of formate dehydrogenases: an overview of recent progress |
| 著者: | Kobayashi, Ami Taketa, Midori Sowa, Keisei    https://orcid.org/0000-0001-9767-4922 (unconfirmed)Kano, Kenji Higuchi, Yoshiki Ogata, Hideaki |
| 著者名の別形: | 小林, 亜美 宋和, 慶盛 加納, 健司 |
| キーワード: | formate dehydrogenases biotechnological applications Methylorubrum extorquens AM1 Mo/W enzymes |
| 発行日: | Sep-2023 |
| 出版者: | International Union of Crystallography (IUCr) |
| 誌名: | IUCrJ |
| 巻: | 10 |
| 号: | 5 |
| 開始ページ: | 544 |
| 終了ページ: | 554 |
| 抄録: | Formate dehydrogenases (FDHs) catalyze the two-electron oxidation of formate to carbon dioxide. FDHs can be divided into several groups depending on their subunit composition and active-site metal ions. Metal-dependent (Mo- or W-containing) FDHs from prokaryotic organisms belong to the superfamily of molybdenum enzymes and are members of the dimethylsulfoxide reductase family. In this short review, recent progress in the structural analysis of FDHs together with their potential biotechnological applications are summarized. |
| 記述: | This article is part of a collection of articles from the IUCr 2023 Congress in Melbourne, Australia, and commemorates the 75th anniversary of the IUCr. |
| 著作権等: | This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
| URI: | http://hdl.handle.net/2433/285570 |
| DOI(出版社版): | 10.1107/s2052252523006437 |
| PubMed ID: | 37668215 |
| 出現コレクション: | 学術雑誌掲載論文等 |
このアイテムは次のライセンスが設定されています: クリエイティブ・コモンズ・ライセンス
