Purification and properties of dimethyl sulphoxide reductase from Rhodobacter capsulatus. A periplasmic molybdoenzyme.
Dimethyl sulphoxide reductase was purified from the photosynthetic bacterium Rhodobacter capsulatus. The enzyme is composed of a single polypeptide of Mr 82,000 and contains a pterin-type molybdenum cofactor as the only detectable prosthetic group. The oxidized molybdenum cofactor of dimethyl sulphoxide reductase is a weak chromophore and exhibits broad absorption bands in the u.v.-visible-absorption spectral region. A distinct spectrum was generated upon addition of dithionite.
McEwan
A G
AG
School of Biochemistry, University of Birmingham, U.K.
Ferguson
S J
SJ
Jackson
J B
JB
D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003067:Coenzymes; D004591:Electrophoresis, Polyacrylamide Gel; D007506:Iron-Sulfur Proteins; D007700:Kinetics; D008667:Metalloproteins / Q000032:analysis; D008970:Molecular Weight; D008982:Molybdenum / Q000032:analysis*; D000090006:Molybdenum Cofactors; D010088:Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D011621:Pteridines / Q000032:analysis; D016354:Rhodobacter capsulatus / Q000201:enzymology*; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry
D003067:Coenzymes; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D008982:Molybdenum; D000090006:Molybdenum Cofactors; D010088:Oxidoreductases; D011621:Pteridines; C022261:molybdopterin; C045664:dimethyl sulfoxide reductase