Efficient hydroxylation of cycloalkanes by co-addition of decoy molecules to variants of the cytochrome P450 CYP102A1

Cycloalkanes were hydroxylated by cytochrome P450Bm3 variants (CYP102A1) with decoy molecules up to 8000-fold more efficiently than the wild-type enzyme alone. Different perfluorocarboxylic acids (PFCs) optimised the product formation rate (PFR) of select variant/cycloalkane combinations but did not enhance a variant (A74G/F87V/L188Q; GVQ) containing mutations in the substrate binding pocket.192