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Structure paper

TitleKinetic, structural, and EPR studies reveal that aldehyde oxidoreductase from Desulfovibrio gigas does not need a sulfido ligand for catalysis and give evidence for a direct Mo-C interaction in a biological system.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 131, Page 7990-7998, Year 2009
Publish dateNov 17, 2008 (structure data deposition date)
AuthorsSantos-Silva, T. / Ferroni, F. / Thapper, A. / Marangon, J. / Gonzalez, P.J. / Rizzi, A.C. / Moura, I. / Moura, J.J. / Romao, M.J. / Brondino, C.D.
External linksJ. Am. Chem. Soc. / PubMed:19459677
MethodsX-ray diffraction
Resolution1.72 - 1.79 Å
Structure data

PDB-3fah:
Glycerol inhibited form of Aldehyde oxidoreductase from Desulfovibrio gigas
Method: X-RAY DIFFRACTION / Resolution: 1.72 Å

PDB-3fc4:
Ethylene glycol inhibited form of Aldehyde oxidoreductase from Desulfovibrio gigas
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-PCD:
(MOLYBDOPTERIN-CYTOSINE DINUCLEOTIDE-S,S)-DIOXO-AQUA-MOLYBDENUM(V)

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-EDO:
1,2-ETHANEDIOL

Source
  • desulfovibrio gigas (bacteria)
KeywordsOXIDOREDUCTASE / MO-glycerol adduct / FAD / Flavoprotein / Iron / Iron-sulfur / Metal-binding / Molybdenum / NAD / Mo-ethylene glycol adduct / 2Fe-2S

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