Dimethyl sulfide:cytochrome c2 reductase (EC 1.8.2.4) is an enzyme with systematic name dimethyl sulfide:cytochrome-c2 oxidoreductase. It is also known by the name dimethylsulfide dehydrogenase (Ddh).[1][2] This enzyme catalyses the following chemical reaction
Dimethyl sulfide:cytochrome c2 reductase | |||||||||
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Identifiers | |||||||||
EC no. | 1.8.2.4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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- dimethyl sulfide + 2 ferricytochrome c2 + H2O dimethyl sulfoxide + 2 ferrocytochrome c2 + 2 H+
The enzyme from the bacterium Rhodovulum sulfidophilum binds molybdopterin guanine dinucleotide, heme b and [4Fe-4S] clusters. It is a heterotrimeric protein with three subunits, the Molybdopterin DdhA (Q8GPG4), the [4Fe-4S] DdhB (Q8GPG3), and the heme-binding DdhC (Q8GPG1). The subunits share homology with other DMSO reductase family enzymes; one example with all three subunits mapped is ethylbenzene hydroxylase from Aromatoleum aromaticum (PDB: 2ivf).[3]
References
edit- ^ Hanlon SP, Toh TH, Solomon PS, Holt RA, McEwan AG (July 1996). "Dimethylsulfide:acceptor oxidoreductase from Rhodobacter sulfidophilus. The purified enzyme contains b-type haem and a pterin molybdenum cofactor". European Journal of Biochemistry. 239 (2): 391–6. doi:10.1111/j.1432-1033.1996.0391u.x. PMID 8706745.
- ^ McDevitt CA, Hugenholtz P, Hanson GR, McEwan AG (June 2002). "Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes". Molecular Microbiology. 44 (6): 1575–87. doi:10.1046/j.1365-2958.2002.02978.x. PMID 12067345. S2CID 42229269.
- ^ SWISS-MODEL. Matched templates Model report Other data
External links
edit- Dimethyl+sulfide:cytochrome+c2+reductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)