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-Structure paper
タイトル | Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 1912, Year 2020 |
掲載日 | 2020年4月20日 |
著者 | Christin Radon / Gerd Mittelstädt / Benjamin R Duffus / Jörg Bürger / Tobias Hartmann / Thorsten Mielke / Christian Teutloff / Silke Leimkühler / Petra Wendler / |
PubMed 要旨 | Metal-containing formate dehydrogenases (FDH) catalyse the reversible oxidation of formate to carbon dioxide at their molybdenum or tungsten active site. They display a diverse subunit and cofactor ...Metal-containing formate dehydrogenases (FDH) catalyse the reversible oxidation of formate to carbon dioxide at their molybdenum or tungsten active site. They display a diverse subunit and cofactor composition, but structural information on these enzymes is limited. Here we report the cryo-electron microscopic structures of the soluble Rhodobacter capsulatus FDH (RcFDH) as isolated and in the presence of reduced nicotinamide adenine dinucleotide (NADH). RcFDH assembles into a 360 kDa dimer of heterotetramers revealing a putative interconnection of electron pathway chains. In the presence of NADH, the RcFDH structure shows charging of cofactors, indicative of an increased electron load. |
リンク | Nat Commun / PubMed:32313256 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.24 - 3.26 Å |
構造データ | EMDB-10495, PDB-6tg9: EMDB-10496, PDB-6tga: |
化合物 | ChemComp-MGD: ChemComp-6MO: ChemComp-FES: ChemComp-SF4: ChemComp-H2S: ChemComp-FMN: ChemComp-NAI: |
由来 |
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キーワード | OXIDOREDUCTASE / molybdoenzyme / formate oxidation / NAD+-dependent |