Purification and properties of dimethylsulfoxide reductase containing a molybdenum cofactor from a photodenitrifier, Rhodopseudomonas sphaeroides f.s. denitrificans.
Dimethylsulfoxide (DMSO) reductase was purified to electrophoretic homogeneity from the periplasmic fraction of a photodenitrifier, Rhodopseudomonas sphaeroides f.s. denitrificans. The enzyme had a molecular weight of 82,000 and had no subunit. It contained 1 mol of molybdenum per mol of enzyme, but iron and acid-labile sulfur were not present. The UV-visible spectrum showed only one absorption maximum at 280 nm. Denaturation of the enzyme released a molybdopterin cofactor, the fluorescence spectra of which were almost the same as those of a form B derivative of molybdopterin found in formate dehydrogenase. The Km value for DMSO was 15 microM, which was much lower than that for trimethylamin-N-oxide (TMAO), whereas Vmax with TMAO was larger than that with DMSO.
Satoh
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Department of Biology, Tokyo Metropolitan University.
Kurihara
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FN
D000596:Amino Acids / Q000032:analysis; D002845:Chromatography; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003067:Coenzymes; D017886:Durapatite; D006882:Hydroxyapatites; D007506:Iron-Sulfur Proteins; D007700:Kinetics; D008667:Metalloproteins / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D000090006:Molybdenum Cofactors; D010088:Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D011621:Pteridines / Q000302:isolation & purification* / Q000378:metabolism; D012242:Rhodobacter sphaeroides / Q000201:enzymology*; D013056:Spectrophotometry, Ultraviolet; D013379:Substrate Specificity
D000596:Amino Acids; D003067:Coenzymes; D017886:Durapatite; D006882:Hydroxyapatites; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D000090006:Molybdenum Cofactors; D010088:Oxidoreductases; D011621:Pteridines; C022261:molybdopterin; C045664:dimethyl sulfoxide reductase