Peroxide-Mediated Oxygenation of Organic Compounds by Fungal Peroxygenases

Research output: Contribution to journalReview articleContributedpeer-review



Unspecific peroxygenases (UPOs), whose sequences can be found in the genomes of thousands of filamentous fungi, many yeasts and certain fungus-like protists, are fascinating biocatalysts that transfer peroxide-borne oxygen (from H2 O2 or R-OOH) with high efficiency to a wide range of organic substrates, including less or unactivated carbons and heteroatoms. A twice-proline-flanked cysteine (PCP motif) typically ligates the heme that forms the heart of the active site of UPOs and enables various types of relevant oxygenation reactions (hydroxylation, epoxidation, subsequent dealkylations, deacylation, or aromatization) together with less specific one-electron oxidations (e.g., phenoxy radical formation). In consequence, the substrate portfolio of a UPO enzyme always combines prototypical monooxygenase and peroxidase activities. Here, we briefly review nearly 20 years of peroxygenase research, considering basic mechanistic, molecular, phylogenetic, and biotechnological aspects.


Original languageEnglish
Article number163
Issue number1
Publication statusPublished - 14 Jan 2022

External IDs

PubMed 35052667
unpaywall 10.3390/antiox11010163
Mendeley c68055c4-1441-3dcb-997e-4c7eb5b441ac



  • Dealkylation, EC, Epoxidation, Hydroxylation, Monooxygenases, Peroxidases, Unspecific peroxygenases, UPO

Library keywords