EC Tree |
1. Oxidoreductases |
1.8 Acting on a sulfur group of donors |
1.8.2 With a cytochrome as acceptor |
ID: | 1.8.2.4 |
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Description: | Dimethyl sulfide:cytochrome c2 reductase. |
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BRENDA Enzyme Link: | BRENDA 1.8.2.4 |
KEGG Enzyme Link: | KEGG1.8.2.4 |
BioCyc Enzyme Link: | BioCyc 1.8.2.4 |
ExPASy Enzyme Link: | ExPASy1.8.2.4 |
EC2PDB Enzyme Link: | EC2PDB 1.8.2.4 |
ExplorEnz Enzyme Link: | ExplorEnz 1.8.2.4 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.8.2.4 |
IntEnz Enzyme Link: | IntEnz 1.8.2.4 |
MEDLINE Enzyme Link: | MEDLINE 1.8.2.4 |
RHEA:30227 | 2 [Fe(III)cytochrome c2] + dimethyl sulfide + H2O = 2 [Fe(II)cytochrome c2] + dimethyl sulfoxide + 2 H(+) |
RULE(radius=1) | [*:1]-[S;H0;+0:2]-[*:3].[Fe+3;H0:4].[Fe+3;H0:5].[OH2;+0:6]>>[*:1]-[S;H0;+0:2](-[*:3])=[O;H0;+0:6].[Fe+2;H0:4].[Fe+2;H0:5] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Dimethylsulfide:acceptor oxidoreductase from Rhodobacter sulfidophilus. The purified enzyme contains b-type haem and a pterin molybdenum cofactor. | Hanlon SP, Toh TH, Solomon PS, Holt RA, McEwan AG | 1996 Jul 15 | 8706745 |
Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes. | McDevitt CA, Hugenholtz P, Hanson GR, McEwan AG | 2002 Jun | 12067345 |