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Copper-Dependent Polysaccharide Monooxygenases: Mechanism and Function.

Created on 29 Jun 2026

Authors

Allison E Batka, Michael A Marletta

Published in

Chemical reviews. Jun 29, 2026. Epub Jun 29, 2026.

Abstract

Polysaccharide monooxygenases (PMOs) constitute a superfamily of enzymes that hydroxylate carbon atoms in glycosidic bonds, ultimately leading to the degradation of carbohydrate polymers. PMOs catalyze this challenging transformation at a mononuclear copper site and utilize either O2 or H2O2 as a cosubstrate. In this review, the mechanisms of three types of catalytic chemistry are discussed: monooxygenase (O2 as a cosubstrate), oxidase (O2 reduction to H2O2), and peroxygenase (H2O2 as a cosubstrate). Key discoveries in the understanding of PMO mechanism and function are described. Several important questions remain unanswered about the utilization of O2 and H2O2 as cosubstrates for polysaccharide hydroxylation. This review will summarize the progress toward understanding the mechanism of O2 activation by this unique class of monooxygenases.

PMID:
42371685
Bibliographic data and abstract were imported from PubMed on 29 Jun 2026.

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