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

Benjamin Melling, Tamara Mielke, Adrian C. Whitwood, Timothy J.C. O'Riordan, Nicholas Mulholland, Jared Cartwright, William P. Unsworth*, Gideon Grogan*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Article number100889
Number of pages14
JournalCHEM: Catalysis
Issue number2
Early online date18 Jan 2024
Publication statusPublished - 15 Feb 2024

Bibliographical note

Funding Information:
We thank the UK Engineering and Physical Sciences Research Council ( EPSRC ) and Syngenta for the award of a studentship to B.M. (project 2602946 ) and the Industrial Affiliates of the Center of Excellence for Biotransformations, Bioprocessing, and Biomanufacturing ( CoEBio3 ) for the award of a studentship to T.M.

Publisher Copyright:
© 2023 The Authors


  • cytochromes P450
  • C–H activation
  • oxygenation
  • SDG9: Industry, innovation, and infrastructure
  • terpenes
  • unspecific peroxygenases
  • UPOs

Cite this