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-Structure paper
タイトル | Multiple electron transfer pathways of tungsten-containing formate dehydrogenase in direct electron transfer-type bioelectrocatalysis. |
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ジャーナル・号・ページ | Chem Commun (Camb), Vol. 58, Issue 45, Page 6478-6481, Year 2022 |
掲載日 | 2022年6月1日 |
著者 | Tatsushi Yoshikawa / Fumiaki Makino / Tomoko Miyata / Yohei Suzuki / Hideaki Tanaka / Keiichi Namba / Kenji Kano / Keisei Sowa / Yuki Kitazumi / Osamu Shirai / |
PubMed 要旨 | Tungsten-containing formate dehydrogenase from AM1 (FoDH1)-a promising biocatalyst for the interconversion of carbon dioxide/formate and nicotine adenine dinucleotide (NAD)/NADH redox couples-was ...Tungsten-containing formate dehydrogenase from AM1 (FoDH1)-a promising biocatalyst for the interconversion of carbon dioxide/formate and nicotine adenine dinucleotide (NAD)/NADH redox couples-was investigated using structural biology and bioelectrochemistry. FoDH1 is reported to be an enzyme that can realize "direct electron transfer (DET)-type bioelectrocatalysis." However, its 3-D structure, electrode-active sites, and electron transfer (ET) pathways remain unclear. The ET pathways were investigated using structural information, electrostatic interactions between the electrode and the enzyme, and the differences in the substrates. Two electrode-active sites and multiple ET pathways in FoDH1 were discovered. |
リンク | Chem Commun (Camb) / PubMed:35535582 |
手法 | EM (単粒子) |
解像度 | 2.19 Å |
構造データ | EMDB-32151, PDB-7vw6: |
化合物 | ChemComp-SF4: ChemComp-FES: ChemComp-MGD: ChemComp-W: ChemComp-UNX: ChemComp-FMN: |
由来 |
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キーワード | OXIDOREDUCTASE / Complex |