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 no.1.8.2.4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

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


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