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Copper-Dependent Polysaccharide Monooxygenases: Mechanism and Function
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DOI：10.1021/acs.chemrev.6c00006.png)
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Abstract
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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.
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55.8
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557
Citations:
24.7W
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