Engineering the haem monooxygenase cytochrome P450cam for monoterpene oxidation

Abstract

Monooxygenated terpenes are fine fragrance and flavouring chemicals, and active site mutants of the haem monooxygenase cytochrome P450_cam which were designed to have improved complementarity between the substrate binding pocket and the monoterpenes (+)-α-pinene (1) and S-limonene (2) have been shown to have greatly enhanced activity for the oxidation of these two substrates, and the major products, verbenol and isopiperitenol from (1) and (2) respectively, were formed with high regioselectivity and near-total stereoselectivity.