Enzyme

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EC Tree
     1. Oxidoreductases
        1.8 Acting on a sulfur group of donors
            1.8.2 With a cytochrome as acceptor
ID:1.8.2.3
Description:Sulfide-cytochrome-c reductase (flavocytochrome c).
Cath: 3.50.50.60; 3.90.760.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.8.2.3
BRENDA Enzyme Link: BRENDA 1.8.2.3
KEGG Enzyme Link: KEGG1.8.2.3
BioCyc Enzyme Link: BioCyc 1.8.2.3
ExPASy Enzyme Link: ExPASy1.8.2.3
EC2PDB Enzyme Link: EC2PDB 1.8.2.3
ExplorEnz Enzyme Link: ExplorEnz 1.8.2.3
PRIAM enzyme-specific profiles Link: PRIAM 1.8.2.3
IntEnz Enzyme Link: IntEnz 1.8.2.3
MEDLINE Enzyme Link: MEDLINE 1.8.2.3
MSA:

1.8.2.3;

Phylogenetic Tree:

1.8.2.3;

Uniprot:
M-CSA:
RHEA:30223 2 [Fe(III)cytochrome c] + hydrogen sulfide = 2 [Fe(II)cytochrome c] + H(+) + sulfur
RULE(radius=1) [Fe+3;H0:1].[Fe+3;H0:2]>>[Fe+2;H0:1].[Fe+2;H0:2]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Partial purification and characterization of two soluble c-type cytochromes from Chromatium vinosum.Gray GO, Gaul DF, Knaff DB1983 Apr 16301383
The oxidation mechanisms of thiosulphate and sulphide in Chlorobium thiosulphatophilum: roles of cytochrome c-551 and cytochrome c-553.Kusai K, Yamanaka T1973 Nov 224357558
Flavocytochrome c of Chromatium vinosum. Some enzymatic properties and subunit structure.Fukumori Y, Yamanaka T1979 Jun222744