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Literature summary for 1.8.2.6 extracted from

  • Zander, U.; Faust, A.; Klink, B.U.; de Sanctis, D.; Panjikar, S.; Quentmeier, A.; Bardischewsky, F.; Friedrich, C.G.; Scheidig, A.J.
    Structural basis for the oxidation of protein-bound sulfur by the sulfur cycle molybdohemo-enzyme sulfane dehydrogenase SoxCD (2011), J. Biol. Chem., 286, 8349-8360 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Paracoccus pantotrophus

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of SoxCD1, solved at 1.33 A . SoxCD1 misses the heme-2 domain D2 and is catalytically as active as SoxCD.The substrate of SoxCD is the outer (sulfane) sulfur of Cys-110-persulfide located at the C-terminal peptide swinging arm of SoxY of the SoxYZ carrier complex. The oxidation reactions of the sulfane-sulfur are initiated by the nucleophilic attack of the persulfide anion on the molybdenum atom that is, in turn, reduced. The close proximity of heme-1 to the molybdopterin allows easy acceptance of the electrons Paracoccus pantotrophus

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum sulfite oxidase-type molybdenum cofactor in subunit SoxC, residue Arg114 involved in the first oxidation step is in close proximity to the molybdenum atiom Paracoccus pantotrophus

Organism

Organism UniProt Comment Textmining
Paracoccus pantotrophus
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Subunits

Subunits Comment Organism
heterotetramer structure resembles a tight alpha2beta-complex with internal 2-fold symmetry, crystallization data Paracoccus pantotrophus

Synonyms

Synonyms Comment Organism
sulfite-dehydrogenase
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Paracoccus pantotrophus