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dc.contributor.author | Suzuki, Yohei | en |
dc.contributor.author | Makino, Fumiaki | en |
dc.contributor.author | Miyata, Tomoko | en |
dc.contributor.author | Tanaka, Hideaki | en |
dc.contributor.author | Namba, Keiichi | en |
dc.contributor.author | Kano, Kenji | en |
dc.contributor.author | Sowa, Keisei | en |
dc.contributor.author | Kitazumi, Yuki | en |
dc.contributor.author | Shirai, Osamu | en |
dc.contributor.alternative | 鈴木, 洋平 | ja |
dc.contributor.alternative | 牧野, 文信 | ja |
dc.contributor.alternative | 宮田, 知子 | ja |
dc.contributor.alternative | 田中, 秀明 | ja |
dc.contributor.alternative | 難波, 啓一 | ja |
dc.contributor.alternative | 加納, 健司 | ja |
dc.contributor.alternative | 宋和, 慶盛 | ja |
dc.contributor.alternative | 北隅, 優希 | ja |
dc.contributor.alternative | 白井, 理 | ja |
dc.date.accessioned | 2023-10-23T01:40:19Z | - |
dc.date.available | 2023-10-23T01:40:19Z | - |
dc.date.issued | 2023-10-20 | - |
dc.identifier.uri | http://hdl.handle.net/2433/285571 | - |
dc.description | 電極を基質認識できる酵素の反応メカニズムを解明 --次世代バイオセンシングにつながる基盤技術--. 京都大学プレスリリース. 2023-10-16. | ja |
dc.description.abstract | Flavin adenine dinucleotide-dependent d-fructose dehydrogenase (FDH) from Gluconobacter japonicus NBRC3260, a membrane-bound heterotrimeric flavohemoprotein capable of direct electron transfer (DET)-type bioelectrocatalysis, was investigated from the perspective of structural biology, bioelectrochemistry, and protein engineering. DET-type reactions offer several benefits in biomimetics (e.g., biofuel cells, bioreactors, and biosensors) owing to their mediator-less configuration. FDH provides an intense DET-type catalytic signal; therefore, extensive research has been conducted on the fundamental principles and applications of biosensors. Structural analysis using cryo-electron microscopy and single-particle analysis has revealed the entire FDH structures with resolutions of 2.5 and 2.7 Å for the reduced and oxidized forms, respectively. The electron transfer (ET) pathway during the catalytic oxidation of d-fructose was investigated by using both thermodynamic and kinetic approaches. Structural analysis has shown the localization of the electrostatic surface charges around heme 2c in subunit II, and experiments using functionalized electrodes with a controlled surface charge support the notion that heme 2c is the electrode-active site. Furthermore, two aromatic amino acid residues (Trp427 and Phe489) were located in a possible long-range ET pathway between heme 2c and the electrode. Two variants (W427A and F489A) were obtained by site-directed mutagenesis, and their effects on DET-type activity were elucidated. The results have shown that Trp427 plays an essential role in accelerating long-range ET and triples the standard rate constant of heterogeneous ET according to bioelectrochemical analysis. | en |
dc.language.iso | eng | - |
dc.publisher | American Chemical Society (ACS) | en |
dc.rights | © 2023 The Authors. Published by American Chemical Society. | en |
dc.rights | This publication is licensed under CC-BY-NC-ND 4.0. | en |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/4.0/ | - |
dc.subject | bioelectrocatalysis | en |
dc.subject | direct electron transfer | en |
dc.subject | cryo-electron microscopy | en |
dc.subject | membrane-bound d-fructose dehydrogenase | en |
dc.subject | intramolecular electron transfer | en |
dc.title | Essential Insight of Direct Electron Transfer-Type Bioelectrocatalysis by Membrane-Bound d-Fructose Dehydrogenase with Structural Bioelectrochemistry | en |
dc.type | journal article | - |
dc.type.niitype | Journal Article | - |
dc.identifier.jtitle | ACS Catalysis | en |
dc.identifier.volume | 13 | - |
dc.identifier.issue | 20 | - |
dc.identifier.spage | 13828 | - |
dc.identifier.epage | 13837 | - |
dc.relation.doi | 10.1021/acscatal.3c03769 | - |
dc.textversion | publisher | - |
dc.address | Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University | en |
dc.address | Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan; JEOL Ltd. | en |
dc.address | Graduate School of Frontier Biosciences, Osaka University | en |
dc.address | Institute for Protein Research, Osaka University | en |
dc.address | Graduate School of Frontier Biosciences, Osaka University; RIKEN Center for Biosystems Dynamics Research; RIKEN SPring-8 Center; JEOL YOKOGUSHI Research Alliance Laboratories, Osaka University | en |
dc.address | Center for Advanced Science and Innovation, Kyoto University | en |
dc.address | Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University | en |
dc.address | Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University | en |
dc.address | Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University | en |
dc.relation.url | https://www.kyoto-u.ac.jp/ja/research-news/2023-10-16 | - |
dcterms.accessRights | open access | - |
datacite.awardNumber | 21H01961 | - |
datacite.awardNumber | 22K14831 | - |
datacite.awardNumber.uri | https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-21H01961/ | - |
datacite.awardNumber.uri | https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-22K14831/ | - |
dc.identifier.eissn | 2155-5435 | - |
jpcoar.funderName | 日本学術振興会 | ja |
jpcoar.funderName | 日本学術振興会 | ja |
jpcoar.awardTitle | 多孔質構造の制御を基盤とする拡散律速型バイオセンシング | 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 |
出現コレクション: | 学術雑誌掲載論文等 |
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