Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site.
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.
Stewart
L J
LJ
CLRC Daresbury Laboratory, Daresbury, Warrington, Cheshire, WA4 4AD, UK.
Bailey
S
S
Bennett
B
B
Charnock
J M
JM
Garner
C D
CD
McAlpine
A S
AS
D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray; D004121:Dimethyl Sulfoxide / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D005583:Fourier Analysis; D007506:Iron-Sulfur Proteins; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008970:Molecular Weight; D008982:Molybdenum / Q000378:metabolism*; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism*; D010100:Oxygen / Q000378:metabolism; D011487:Protein Conformation; D011622:Pterins / Q000737:chemistry / Q000378:metabolism; D016354:Rhodobacter capsulatus / Q000201:enzymology* / Q000254:growth & development; D013053:Spectrophotometry; D014414:Tungsten / Q000378:metabolism*
D007506:Iron-Sulfur Proteins; D011622:Pterins; D008982:Molybdenum; D010088:Oxidoreductases; C045664:dimethyl sulfoxide reductase; D010100:Oxygen; D014414:Tungsten; D004121:Dimethyl Sulfoxide