Dimethylsulfoxide DMSO Reductase

Members of the dimethylsulfoxide (DMSO) reductase family have the molybdenum ligated by two MPTs, one 0x0 group, and the donor atom from the side chain of an amino acid residue—O7 of a serinyl residue (DMSO reductase or trimethylamineoxide (TMAO) reductase), S7 of a cysteinyl residue (dissimilatory nitrate reductase), or Sc7 of selenocys-teinyl residue (formate dehydrogenase). 

In the case of the DMSO reductase family, as pointed out above, the metal centre is bound to two molecules of the cofactor. DMSO reductase itself catalyses the reduction of dimethylsulfoxide to dimethylsulfide with incorporation of the oxygen atom of DMSO into water. The active site of the oxidized enzyme is an L2MoVI0(0-Ser) centre, which, upon reduction, loses the M=0 ligand to give a L2MoIV(0-Ser) centre. In the catalytic... 

DMSO reductase reduces dimethylsulfoxide to dimethylsulfide (Eq. 16-62) as part of the biological sulfur cycle.647 648d... 

Dimethylsulfoxide reductase is a molybdenum-containing enzyme that catalyzes the conversion of dimethyl sulfoniopropionate (DMSP), produced by marine algae as an osmotic stabilizer and methylating agent, to dimethyl sulfide (DMS) (Figure 20.6). DMS is subsequently oxidized to dimethylsulfoxide (DMSO). Dimethylsulfoxide reductase contains two molecules of bound molybdopterin covalently linked to a serine residue in the enzyme. 

The periplasmic dimethylsulfoxide reductases (DMSORs) of the photosynthetic bacteria R. capsulatus and R. sphaeroides function in a respiratory chain with DMSO as the terminal electron acceptor and catalyse the environmentally important Reaction (2). " ... 

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