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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 ( Rc FDH) as isolated and in the presence of reduced nicotinamide adenine dinucleotide (NADH).  Rc FDH assembles into a 360 kDa dimer of heterotetramers revealing a putative interconnection of electron pathway chains. In the presence of NADH, the  Rc FDH structure shows charging of cofactors, indicative of an increased electron load.

Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase