Peroxide-Mediated Oxygenation of Organic Compounds by Fungal Peroxygenases

• Published in: Antioxidants Vol. 11; no. 1; p. 163
• Main Authors: Hofrichter, Martin, Kellner, Harald, Herzog, Robert, Karich, Alexander, Kiebist, Jan, Scheibner, Katrin, Ullrich, René
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 14.01.2022; MDPI
• Subjects: active sites; aromatization; Biocatalysts; cysteine; Deacylation; E coli; EC 1.11.2.1; Enzymes; Epoxidation; epoxidation reactions; Fungi; genome; Genomes; Heme; Hydrogen peroxide; Hydroxylation; Mold; Monooxygenase; monooxygenases; Organic compounds; oxygen; Oxygenation; Peroxidase; peroxidases; Phylogeny; Proline; Proteins; protists; Review; Soybeans; unspecific peroxygenases; UPO; Yeast; epoxidation; UPO; hydroxylation; unspecific peroxygenases; dealkylation; peroxidases; monooxygenases; EC 1.11.2.1
• ISSN: 2076-3921; 2076-3921
• DOI: 10.3390/antiox11010163

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 H2O2 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.