+Search query
-Structure paper
Title | Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase. |
---|---|
Journal, issue, pages | Nat Commun, Vol. 11, Issue 1, Page 1912, Year 2020 |
Publish date | Apr 20, 2020 |
Authors | Christin Radon / Gerd Mittelstädt / Benjamin R Duffus / Jörg Bürger / Tobias Hartmann / Thorsten Mielke / Christian Teutloff / Silke Leimkühler / Petra Wendler / |
PubMed Abstract | 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. |
External links | Nat Commun / PubMed:32313256 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.24 - 3.26 Å |
Structure data | EMDB-10495, PDB-6tg9: EMDB-10496, PDB-6tga: |
Chemicals | ChemComp-MGD: ChemComp-6MO: ChemComp-FES: ChemComp-SF4: ChemComp-H2S: ChemComp-FMN: ChemComp-NAI: |
Source |
|
Keywords | OXIDOREDUCTASE / molybdoenzyme / formate oxidation / NAD+-dependent |