Flavin supported fatty acid oxidation by the heme domain of Bacillus megaterium cytochrome P450BM-3.
Cytochrome P450BM-3 is a fatty acid hydroxylase that consists of a heme domain covalently attached to a diflavin (FMN+FAD) cytochrome P450 reductase domain. The heme and flavin domains can be separately expressed and purified from E. coli recombinant expression systems. Normally P450s require a protein redox partner as a source of electrons. We now have found that the P450BM-3 heme domain can be reduced by NADPH+FMN and that reduced FMN can support the P450 catalyzed hydroxylation of a fatty acid substrate, myristic acid. HPLC profiles show that the "artificial" FMN supported hydroxylation gives the same products as does holo-P450BM-3.
Gonvindaraj
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Department of Molecular Biology & Biochemistry, University of California, Irvine 92717-3900.
Li
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Poulos
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D001410:Bacillus megaterium / Q000201:enzymology*; D001426:Bacterial Proteins; D002250:Carbon Radioisotopes; D002851:Chromatography, High Pressure Liquid; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D005486:Flavin Mononucleotide / Q000378:metabolism* / Q000494:pharmacology; D006418:Heme / Q000378:metabolism; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D019814:Myristic Acid; D009227:Myristic Acids / Q000378:metabolism*; D009249:NADP / Q000378:metabolism; D009251:NADPH-Ferrihemoprotein Reductase; D010084:Oxidation-Reduction; D011865:Radioisotope Dilution Technique; D013053:Spectrophotometry
D001426:Bacterial Proteins; D002250:Carbon Radioisotopes; D009227:Myristic Acids; D019814:Myristic Acid; D006418:Heme; D009249:NADP; D005486:Flavin Mononucleotide; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases