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

Christin Radon, Gerd Mittelstädt, Benjamin R. Duffus, Jörg Bürger, Tobias Hartmann, Thorsten Mielke, Christian Teutloff, Silke Leimkühler and Petra Wendler ()
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Christin Radon: University of Potsdam
Gerd Mittelstädt: University of Potsdam
Benjamin R. Duffus: University of Potsdam
Jörg Bürger: Max-Planck Institute of Molecular Genetics
Tobias Hartmann: University of Potsdam
Thorsten Mielke: Max-Planck Institute of Molecular Genetics
Christian Teutloff: Freie Universität Berlin
Silke Leimkühler: University of Potsdam
Petra Wendler: University of Potsdam

Nature Communications, 2020, vol. 11, issue 1, 1-9

Abstract: 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 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.

Date: 2020
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DOI: 10.1038/s41467-020-15614-0

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