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Published on: March 18, 2012
Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site
L J Stewart1, S Bailey, B Bennett
1CLRC Daresbury Laboratory, Daresbury, Warrington, Cheshire, WA4 4AD, UK.
Abstract:
DMSO reductase (DMSOR) from Rhodobacter capsulatus, well-characterised as a molybdoenzyme, will bind tungsten. Protein crystallography has shown that tungsten in W-DMSOR is ligated by the dithiolene group of the two pyranopterins, the oxygen atom of Ser147 plus another oxygen atom, and is located in a very similar site to that of molybdenum in Mo-DMSOR. These conclusions are consistent with W L(III)-edge X-ray absorption, EPR and UV/visible spectroscopic data. W-DMSOR is significantly more active than Mo-DMSOR in catalysing the reduction of DMSO but, in contrast to the latter, shows no significant ability to catalyse the oxidation of DMS.
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