Polyphenol Oxidase Products Are Priming Agents For LPMO Peroxygenase Activity

Caio de Oliveira Gorgulho Silva, Marlene Vuillemin, Mirjam A. Kabel, Willem J. H. van Berkel, Anne S. Meyer, Jane Wittrup Agger*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

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Polyphenol oxidases catalyze the hydroxylation of monophenols to diphenols, which are reducing agents for lytic polysaccharide monooxygenases (LPMOs) in their degradation of cellulose. In particular, the polyphenol oxidase MtPPO7 from Myceliophthora thermophila convert lignocellulose-derived monophenols, and under the new perspective of the peroxygenase reaction catalyzed by LPMOs, we aim to differentiate the role of the catalytic products of MtPPO7 in priming and fueling of LPMO activity. Exemplified by the activity of MtPPO7 towards guaiacol and by using the benchmark LPMO NcAA9C from Neurospora crassa we show that MtPPO7 catalytic products provide the initial electron for the reduction of Cu(II) to Cu(I) but cannot provide the required reducing power for continuous fueling of the LPMO. We show that the priming reaction occurs with catalytic amounts of MtPPO7 products and that those compounds do not generate substantial amounts of H2O2in situ to fuel the LPMO peroxygenase activity. Reducing agents with a low propensity to generate H2O2 can provide the means for controlling the LPMO catalysis through exogenous H2O2 and thereby minimize any enzyme inactivation.
Original languageEnglish
Article numbere202300559
Issue number18
Number of pages9
Publication statusPublished - 2023


  • Lytic polysaccharide monooxygenase
  • Monophenol
  • Peroxygenase
  • Polyphenol oxidase
  • Priming reduction


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