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Full-Text Articles in Physics
Dimethylsulfoxide Reductase: An Enzyme Capable Of Catalysis With Either Molybdenum Or Tungsten At The Active Site, Lisa J. Stewart, Susan Bailey, Brian Bennett, John M. Charnock, C. David Garner, Alan S. Mcalpine
Dimethylsulfoxide Reductase: An Enzyme Capable Of Catalysis With Either Molybdenum Or Tungsten At The Active Site, Lisa J. Stewart, Susan Bailey, Brian Bennett, John M. Charnock, C. David Garner, Alan S. Mcalpine
Physics Faculty Research and Publications
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 LIII-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.