Biology:Dimethyl sulfide:cytochrome c2 reductase

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Dimethyl sulfide:cytochrome c2 reductase
Identifiers
EC number1.8.2.4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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 + 2 ferricytochrome c2 + H2O [math]\displaystyle{ \rightleftharpoons }[/math] 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

  1. "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. July 1996. doi:10.1111/j.1432-1033.1996.0391u.x. PMID 8706745. 
  2. "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. June 2002. doi:10.1046/j.1365-2958.2002.02978.x. PMID 12067345. 
  3. SWISS-MODEL. Matched templates Model report Other data

External links