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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.
Additional recommended knowledge
Active site and mechanism
The active site contains a molybdopterin-containing core that supports molybdenum in its highest oxidation state (MoVI). The proposed mechanism of DMSO reductase cycles molybdenum between the +4 and +6 oxidation states.
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.PubMed
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "DMSO_reductase". A list of authors is available in Wikipedia.|