The cytochrome P-450 alkane monooxygenase system of the yeast lodderomyces elongisporus: Purification and some properties of the NADPH-cytochrome P-450 reductase

• Published in: Biochemical and biophysical research communications Vol. 106; no. 4; pp. 1318 - 1324
• Main Authors: Honeck, H., Schunck, W.-H., Riege, P., Müller, H.-G.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 30.06.1982
• Subjects: Ascomycota - enzymology; Cytochrome P-450 CYP4A; Cytochrome P-450 Enzyme System - metabolism; Intracellular Membranes - enzymology; Kinetics; Microsomes - enzymology; Mixed Function Oxygenases - metabolism; NADPH-Ferrihemoprotein Reductase - isolation & purification; NADPH-Ferrihemoprotein Reductase - metabolism; Saccharomycetales - enzymology; Spectrophotometry; cyt
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/0006-291X(82)91257-8

NADPH-cytochrome P-450 reductase has been purified to homogeneity, as judged by SDS-polyacrylamide gel electrophoresis, from microsomal fraction of Lodderomyces elongisporus using an effective 2-step chromatography procedure. One mol enzyme contains 1 mol each of FAD and FMN and exhibits an apparent molecular weight of 79.000. Recombination of the NADPH-cytochrome P-450 reductase with highly purified cytochrome P-450 results in an active alkane monooxygenase system. The activity of the hexadecane hydroxylation was enhanced by the addition of non-ionic detergent.