Protected cyclohexanol and cyclohex-2-enol substrates, containing benzyl ether and benzoate ester moieties, were designed to fit into the active site of the Tyr96Ala mutant of cytochrome P450cam. The protected cyclohexanol substrates were efficiently and selectively hydroxylated by the mutant enzyme at the trans C–H bond of C-4 on the cyclohexyl ring. The selectivity of oxidation of the benzoate ester protected cyclohexanol ...
[Ross, Angela M.; Pohl, Terese M.; Piazza, Kathryn; Thomas, Michael; Fox, Bonnie; Whalen, Dale L. Journal of the American Chemical Society, 1982 , vol. 104, # 6 p. 1658 - 1665]