Medical College of Wisconsin
CTSICores SearchResearch InformaticsREDCap

Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site. J Mol Biol 2000 Jun 09;299(3):593-600

Date

06/03/2000

Pubmed ID

10835270

DOI

10.1006/jmbi.2000.3702

Scopus ID

2-s2.0-0034625310 (requires institutional sign-in at Scopus site)   100 Citations

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.

Author List

Stewart LJ, Bailey S, Bennett B, Charnock JM, Garner CD, McAlpine AS

Author

Brian Bennett D.Phil. Professor and Chair in the Physics department at Marquette University




MESH terms used to index this publication - Major topics in bold

Binding Sites
Catalysis
Crystallography, X-Ray
Dimethyl Sulfoxide
Electron Spin Resonance Spectroscopy
Fourier Analysis
Iron-Sulfur Proteins
Kinetics
Models, Molecular
Molecular Sequence Data
Molecular Weight
Molybdenum
Oxidation-Reduction
Oxidoreductases
Oxygen
Protein Conformation
Pterins
Rhodobacter capsulatus
Spectrophotometry
Tungsten