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Literature summary for 1.8.2.3 extracted from

  • Chen, Z.; Koh, M.; Van Driessche, G.; Van Beeumen, J.; Bartsch, R.; Meyer, T.; Cusanovich, M.; Mathews, F.
    The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium (1994), Science, 266, 430-432.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Allochromatium vinosum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
21000
-
1 * 46000 + 1 * 21000, the enzyme contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit Allochromatium vinosum
46000
-
1 * 46000 + 1 * 21000, the enzyme contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit Allochromatium vinosum
67000
-
-
Allochromatium vinosum

Organism

Organism UniProt Comment Textmining
Allochromatium vinosum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sulfide + oxidized flavocytochrome c
-
Allochromatium vinosum sulfur + reduced flavocytochrome c + H+
-
r

Subunits

Subunits Comment Organism
heterodimer 1 * 46000 + 1 * 21000, the enzyme contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit Allochromatium vinosum

Synonyms

Synonyms Comment Organism
FCSD
-
Allochromatium vinosum
flavocytochrome c sulfide dehydrogenase
-
Allochromatium vinosum

Cofactor

Cofactor Comment Organism Structure
FAD the enzyme contains a glutathione reductase-like flavin-binding subunit. FAD is bound covalently to the flavoprotein subunit by an 8-alpha-methyl(S-cysteinyl) thioether linkage Allochromatium vinosum
heme the enzyme contains a diheme cytochrome subunit Allochromatium vinosum