Abstract
Cytochrome P450BM-3 is a fatty acid hydoxylase 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 P450(BM-3)heme domain can be reduced by NADPH+FMN and that reduced FMN can support the P450 catalyzed hydroxylation of a fatty acid substrate, myrtistic acid. HPLC profiles show that that the "artificial" FMN supported hydroxylation gives the same products as does holo-P450BM-3.
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