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s2052252523006437.pdf | 1.55 MB | Adobe PDF | 見る/開く |
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DCフィールド | 値 | 言語 |
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dc.contributor.author | Kobayashi, Ami | en |
dc.contributor.author | Taketa, Midori | en |
dc.contributor.author | Sowa, Keisei | en |
dc.contributor.author | Kano, Kenji | en |
dc.contributor.author | Higuchi, Yoshiki | en |
dc.contributor.author | Ogata, Hideaki | en |
dc.contributor.alternative | 小林, 亜美 | ja |
dc.contributor.alternative | 宋和, 慶盛 | ja |
dc.contributor.alternative | 加納, 健司 | ja |
dc.date.accessioned | 2023-10-23T01:39:48Z | - |
dc.date.available | 2023-10-23T01:39:48Z | - |
dc.date.issued | 2023-09 | - |
dc.identifier.uri | http://hdl.handle.net/2433/285570 | - |
dc.description | 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. | en |
dc.description.abstract | 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. | en |
dc.language.iso | eng | - |
dc.publisher | International Union of Crystallography (IUCr) | en |
dc.rights | 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. | en |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | - |
dc.subject | formate dehydrogenases | en |
dc.subject | biotechnological applications | en |
dc.subject | Methylorubrum extorquens AM1 | en |
dc.subject | Mo/W enzymes | en |
dc.title | Structure and function relationship of formate dehydrogenases: an overview of recent progress | en |
dc.type | journal article | - |
dc.type.niitype | Journal Article | - |
dc.identifier.jtitle | IUCrJ | en |
dc.identifier.volume | 10 | - |
dc.identifier.issue | 5 | - |
dc.identifier.spage | 544 | - |
dc.identifier.epage | 554 | - |
dc.relation.doi | 10.1107/s2052252523006437 | - |
dc.textversion | publisher | - |
dc.identifier.pmid | 37668215 | - |
dcterms.accessRights | open access | - |
datacite.awardNumber | 22K14831 | - |
datacite.awardNumber | 18H05516 | - |
datacite.awardNumber | 19H00984 | - |
datacite.awardNumber.uri | https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-22K14831/ | - |
datacite.awardNumber.uri | https://kaken.nii.ac.jp/grant/KAKENHI-PLANNED-18H05516/ | - |
datacite.awardNumber.uri | https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-19H00984/ | - |
dc.identifier.eissn | 2052-2525 | - |
jpcoar.funderName | 日本学術振興会 | ja |
jpcoar.funderName | 日本学術振興会 | ja |
jpcoar.funderName | 日本学術振興会 | ja |
jpcoar.awardTitle | 生物電気化学と立体構造解析を組み合わせた直接電子移動型酵素の反応機構解明 | ja |
jpcoar.awardTitle | 高速・局所移動水素と電子とのカップリングによる新発想デバイスの設計 | ja |
jpcoar.awardTitle | ヒドロゲナーゼの触媒反応機構と高効率プロトン伝達機構の構造基盤解明 | ja |
出現コレクション: | 学術雑誌掲載論文等 |
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