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.