Format of Original
Journal of Molecular Biology
Original Item ID
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.
Stewart, Lisa J.; Bailey, Susan; Bennett, Brian; Charnock, John M.; Garner, C. David; and McAlpine, Alan S., "Dimethylsulfoxide Reductase: An Enzyme Capable of Catalysis with Either Molybdenum or Tungsten at the Active Site" (2000). Physics Faculty Research and Publications. 84.
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