Expanding the Catalytic Landscape of Metalloenzymes with Lytic Polysaccharide Monooxygenases

Overview

Journal Nat Rev Chem

Publisher Springer Nature

Specialty Chemistry

Date 2024 Jan 10

PMID 38200220

Authors

Alessia Munzone

Vincent G H Eijsink

Jean-Guy Berrin

Bastien Bissaro

Affiliations

Soon will be listed here.

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 HO 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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