Purification and properties of an FAD-containing NADH oxidase from Mycoplasma capricolum.
From the prokaryotic microorganism Mycoplasma capricolum an FAD-containing NADH oxidase has been purified by preparative FPLC to homogeneity, as judged by polyacrylamide gel electrophoresis. The apparent molecular mass of the enzyme was found to be 72.5 kDa, with an isoelectric point of 5.2, and no detectable subunits. No iron, copper, manganese or molybdenium could be detected. On the basis of a minimum molecular mass of 72.5 kDa a ratio of FAD/protein of 1:1 could be derived. Its amino-acid composition, the light absorption and the fluorescence spectra are presented.
D000596:Amino Acids / Q000032:analysis; D002384:Catalysis; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003579:Cytochrome Reductases / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism*; D007700:Kinetics; D009174:Mycoplasma / Q000201:enzymology*; D009245:NADH Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism; D013050:Spectrometry, Fluorescence
D000596:Amino Acids; D005182:Flavin-Adenine Dinucleotide; D003579:Cytochrome Reductases; D009245:NADH Dehydrogenase