Title

Dimethylsulfoxide Reductase: An Enzyme Capable of Catalysis with Either Molybdenum or Tungsten at the Active Site

Document Type

Article

Language

eng

Format of Original

8 p.

Publication Date

6-9-2000

Publisher

Elsevier

Source Publication

Journal of Molecular Biology

Source ISSN

0022-2836

Original Item ID

doi: 10.1006/jmbi.2000.3702

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 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.

Comments

Journal of Molecular Biology, Vol. 299, No. 3 (June 9, 2000): 593-600. DOI.

Brian Bennett was affiliated with the CLRC Daresbury Laboratory Daresbury at the time of publication.