DMSO reductase is a molybdenum-containing enzyme capable of reducing dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). This enzyme serves as the terminal reductase under anaerobic conditions in some bacteria, with DMSO being the terminal electron acceptor. During the course of the reaction, the oxygen atom in DMSO is transferred to molybdenum, and then is subsequently removed from molybdenum as water.

The reaction catalyzed by DMSO reductase.

[edit] Active site and mechanism

The active site contains a molybdopterin-containing core that supports molybdenum in its highest oxidation state (Mo^VI). The proposed mechanism of DMSO reductase cycles molybdenum between the +4 and +6 oxidation states.

The proposed mechanism of DMSO reductase.

[edit] References

Kisker, C.; Schindelin, H.; Baas, D.; Rétey, J.; Meckenstock, R.U.; Kroneck, P.M.H. (1999). "A structural comparison of molybdenum cofactor-containing enzymes". FEMS Microbiol. Rev. 22: 503–521. doi:10.1111/j.1574-6976.1998.tb00384.x. PubMed