EC 1.8.2.3 - Sulfide-cytochrome-c reductase (flavocytochrome c)

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IntEnz Enzyme Nomenclature
EC 1.8.2.3

Names

Accepted name:
sulfide-cytochrome-c reductase (flavocytochrome c)
Systematic name:
hydrogen-sulfide:flavocytochrome c oxidoreductase

Reaction

Cofactors

Comments:

The enzyme from Allochromatium vinosum contains covalently bound FAD and covalently-bound c-type hemes.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Kusai, K., Yamanaka, T.
    The oxidation mechanisms of thiosulphate and sulphide in Chlorobium thiosulphatophilum: roles of cytochrome c-551 and cytochrome c-553.
    Biochim. Biophys. Acta 325: 304-314 (1973). [PMID: 4357558]
  2. Fukumori, Y., Yamanaka, T.
    Flavocytochrome c of Chromatium vinosum. Some enzymatic properties and subunit structure.
    J. Biochem. 85: 1405-1414 (1979). [PMID: 222744]
  3. Gray, G. O., Gaul, D. F., Knaff, D. B.
    Partial purification and characterization of two soluble c-type cytochromes from Chromatium vinosum.
    Arch. Biochem. Biophys. 222: 78-86 (1983). [PMID: 6301383]
  4. Chen, Z. W., Koh, M., Van Driessche, G., Van Beeumen, J. J., Bartsch, R. G., Meyer, T. E., Cusanovich, M. A., Mathews, F. S.
    The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium.
    Science 266: 430-432 (1994). [PMID: 7939681]
  5. Sorokin, D.Yu, de Jong, G.A., Robertson, L.A. and Kuenen, G.J.
    Purification and characterization of sulfide dehydrogenase from alkaliphilic chemolithoautotrophic sulfur-oxidizing bacteria.
    FEBS Lett. 427: 11-14 (1998). [PMID: 9613590]
  6. Kostanjevecki, V., Brige, A., Meyer, T. E., Cusanovich, M. A., Guisez, Y., van Beeumen, J.
    A membrane-bound flavocytochrome c-sulfide dehydrogenase from the purple phototrophic sulfur bacterium Ectothiorhodospira vacuolata.
    J. Bacteriol. 182: 3097-3103 (2000). [PMID: 10809687]

[EC 1.8.2.3 created 2011]