Cytochrome P450 is a superfamily of heme thiolate enzymes which perform a variety of selective oxidation reactions on a wide range of substrates with two reducing equivalents, provided by the reductase, and molecular dioxygen as the source of oxygen atom. To circumvent the use of the reductase domain and expensive co-factor NADPH, our laboratory has developed a series of light-activated hybrid P450 enzymes. A Ru(II) di-imine photosensitizer is covalently attached to single, non-native cysteine residues on the P450 BM3 heme domain mutants. We recently reported an optimized hybrid P450 BM3 heme domain displaying the highest catalytic activity among the current alternative approaches in the hydroxylation of its model substrate, lauric acid. We will present our current efforts to optimize the hybrid P450 enzymes for the oxidation of polycyclic aromatic hydrocarbons.

Using light activated hybrid P450 BM3 enzymes for the aerobic oxidation of polycyclic aromatic hydrocarbons

248th National Meeting (2014)

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