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Cryo-EM Structure of as isolated form of NAD+-dependent Formate Dehydrogenase from Rhodobacter capsulatusCryo-EM Structure of as isolated form of NAD+-dependent Formate Dehydrogenase from Rhodobacter capsulatus
Structural highlights
Publication Abstract from PubMedMetal-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. Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase.,Radon C, Mittelstadt G, Duffus BR, Burger J, Hartmann T, Mielke T, Teutloff C, Leimkuhler S, Wendler P Nat Commun. 2020 Apr 20;11(1):1912. doi: 10.1038/s41467-020-15614-0. PMID:32313256[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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