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TitleKinetic and Structural Studies of Aldehyde Oxidoreductase from Desulfovibrio Gigas Reveal a Dithiolene-Based Chemistry for Enzyme Activation and Inhibition by H2O2.
Journal, issue, pagesPlos One, Vol. 8, Page 83234-, Year 2013
Publish dateSep 27, 2013 (structure data deposition date)
AuthorsMarangon, J. / Correia, H.D. / Brondino, C.D. / Moura, J.J.G. / Romao, M.J. / Gonzalez, P.J. / Santos-Silva, T.
External linksPlos One / PubMed:24391748
MethodsX-ray diffraction
Resolution1.5 - 1.57 Å
Structure data

PDB-4c7y:
Aldehyde Oxidoreductase from Desulfovibrio gigas (MOP), soaked with sodium dithionite and sodium sulfide
Method: X-RAY DIFFRACTION / Resolution: 1.57 Å

PDB-4c7z:
Aldehyde Oxidoreductase from Desulfovibrio gigas (MOP), activated with sodium dithionite and sodium sulfide
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-4c80:
Aldehyde Oxidoreductase from Desulfovibrio gigas (MOP), soaked with hydrogen peroxide
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-IPA:
ISOPROPYL ALCOHOL / alkaloid*YM

ChemComp-BCT:
BICARBONATE ION / pH buffer*YM

ChemComp-MG:
Unknown entry

ChemComp-CL:
Unknown entry

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

ChemComp-PEO:
HYDROGEN PEROXIDE

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

Source
  • desulfovibrio gigas (bacteria)
KeywordsOXIDOREDUCTASE / MOLYBDENUM ENZYME / MOP / ACTIVATION / INACTIVATION

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