Complementary specificity of unspecific peroxygenases enables access to diverse products from terpene oxygenation

Unspecific peroxygenases (UPOs) have emerged as attractive biocatalysts for selective oxygenations because, unlike cytochromes P450, they can be employed as easy-to-use lyophilized powders and depend only upon hydrogen peroxide as the external oxidant. The application of UPOs to a range of synthetic challenges relies on the characterization of activity and specificity of complementary enzymes. Here, we show that two UPOs, artUPO and rAaeUPO-PaDa-I-H, which are representative members of the "short" family I and "long" family II UPOs, display complementary activity in a series of scalable, preparative biotransformations of a diverse array of terpenes. The UPOs were also applied to the biotransformation of chrysanthemic-acid-derived fragments relevant in the agrichemical industry, culminating in the highly diastereoselective and enantioselective oxidation of a racemic synthetic pyrethroid derivative via kinetic resolution.