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TitleCryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 1912, Year 2020
Publish dateApr 20, 2020
AuthorsChristin Radon / Gerd Mittelstädt / Benjamin R Duffus / Jörg Bürger / Tobias Hartmann / Thorsten Mielke / Christian Teutloff / Silke Leimkühler / Petra Wendler /
PubMed AbstractMetal-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 linksNat Commun / PubMed:32313256 / PubMed Central
MethodsEM (single particle)
Resolution3.24 - 3.26 Å
Structure data

10495

6tg9

EMDB-10495, PDB-6tg9:
Cryo-EM Structure of NADH reduced form of NAD+-dependent Formate Dehydrogenase from Rhodobacter capsulatus
Method: EM (single particle) / Resolution: 3.24 Å

10496

6tga

EMDB-10496, PDB-6tga:
Cryo-EM Structure of as isolated form of NAD+-dependent Formate Dehydrogenase from Rhodobacter capsulatus
Method: EM (single particle) / Resolution: 3.26 Å

Chemicals

ChemComp-MGD:
2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE

ChemComp-6MO:
Unknown entry

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster

ChemComp-SF4:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

ChemComp-H2S:
HYDROSULFURIC ACID / Hydrogen sulfide

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE / Flavin mononucleotide

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE / Nicotinamide adenine dinucleotide

Source
  • rhodobacter capsulatus (bacteria)
KeywordsOXIDOREDUCTASE / molybdoenzyme / formate oxidation / NAD+-dependent

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