Dimethyl sulfide:cytochrome c2 reductase

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 dimethyl sulfoxide + 2 ferrocytochrome c2 + 2 H+
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

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. 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.
  2. 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.
  3. SWISS-MODEL. Matched templates Model report Other data


This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.