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
06/03/2000Pubmed ID
10835270DOI
10.1006/jmbi.2000.3702Scopus ID
2-s2.0-0034625310 (requires institutional sign-in at Scopus site) 100 CitationsAbstract
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 ASAuthor
Brian Bennett D.Phil. Professor and Chair in the Physics department at Marquette UniversityMESH terms used to index this publication - Major topics in bold
Binding SitesCatalysis
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