Dimethyl sulfoxide reductase (DMSO reductase)

Dimethyl sulfoxide reductase (DMSO reductase, DMSOR) is a molybdenum-containing enzyme found predominantly in bacteria and archaea[1][3][7]. It catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS) during anaerobic respiration, where DMSO is used as a terminal electron acceptor[1][6][8]. DMSO reductase has a highly conserved active site with molybdenum coordinated by two molybdopterin guanine dinucleotide cofactors and, depending on its subclass, an additional amino acid ligand (serine, cysteine, or aspartate)[1][3][7]. It plays a significant ecological role in the global sulfur cycle and can influence atmospheric processes by contributing to DMS release, which affects cloud formation and climate regulation[3][7]. While not a therapeutic target for drugs in human medicine, its metabolic activity is essential in microbial biochemistry and has potential utility in bioremediation and synthetic biocatalysis[2][7]. DMSO reductase enzymes are phylogenetically widespread in prokaryotes and represent one of the largest families of prokaryotic molybdoenzymes[7].

Other names

Dimethylsulfoxide reductaseDMSO reductaseDMSOR

Catalyzes the two-electron reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS) at a molybdenum active center; Acts as a terminal electron acceptor in bacterial anaerobic metabolism