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Peroxide-Mediated Oxygenation of Organic Compounds by Fungal Peroxygenases

  • 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.

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Author: Martin HofrichterORCiD, Harald Kellner, Robert Herzog, Alexander Karich, Jan Kiebist, Katrin Scheibner, René UllrichORCiD
URL:https://www.mdpi.com/2076-3921/11/1/163
DOI:https://doi.org/10.3390/antiox11010163
ISSN:2076-3921
Title of the source (English):Antioxidants
Document Type:Scientific journal article peer-reviewed
Language:English
Year of publication:2022
Contributing Corporation:TU Dresden
Tag:dealkylation; epoxidation; hydroxylation; monooxygenase; peroxidases; unspecific peroxygenase
Volume/Year:11
Issue number:1
First Page:1
Last Page:21
Article number:163
Faculty/Chair:Fakultät 2 Umwelt und Naturwissenschaften / FG Enzymtechnologie
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