Abstract
Lytic polysaccharide monooxygenases (LPMOs) have an essential role in global carbon cycle, industrial biomass processing and microbial pathogenicity by catalysing the oxidative cleavage of recalcitrant polysaccharides. Despite initially being considered monooxygenases, experimental and theoretical studies show that LPMOs are essentially peroxygenases, using a single copper ion and H2O2 for C–H bond oxygenation. Here, we examine LPMO catalysis, emphasizing key studies that have shaped our comprehension of their function, and address side and competing reactions that have partially obscured our understanding. Then, we compare this novel copper–peroxygenase reaction with reactions catalysed by haem iron enzymes, highlighting the different chemistries at play. We conclude by addressing some open questions surrounding LPMO catalysis, including the importance of peroxygenase and monooxygenase reactions in biological contexts, how LPMOs modulate copper site reactivity and potential protective mechanisms against oxidative damage.
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Change history
22 January 2024
A Correction to this paper has been published: https://doi.org/10.1038/s41570-024-00580-8
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Acknowledgements
We thank the current and past members of our research groups that have contributed to LPMO research. We also thank our colleagues from the LPMO community. We apologize in advance to all investigators whose research cannot be appropriately discussed and cited owing to space limitations. A.M. and B.B. disclose support for the research of this work from INRAE (EvoFun project PAF_02). V.G.H.E. discloses support for the research of this work from the European Research Council (grant number 856446).
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Munzone, A., Eijsink, V.G.H., Berrin, JG. et al. Expanding the catalytic landscape of metalloenzymes with lytic polysaccharide monooxygenases. Nat Rev Chem 8, 106–119 (2024). https://doi.org/10.1038/s41570-023-00565-z
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DOI: https://doi.org/10.1038/s41570-023-00565-z
