Molecular mechanism of the chitinolytic peroxygenase reaction.

ABSTRACT: Lytic polysaccharide monooxygenases (LPMOs) are a recently discovered class of monocopper enzymes broadly distributed across the tree of life. Recent reports indicate that LPMOs can use H₂O₂ as an oxidant and thus carry out a novel type of peroxygenase reaction involving unprecedented copper chemistry. Here, we present a combined computational and experimental analysis of the H₂O₂-mediated reaction mechanism. In silico studies, based on a model of the enzyme in complex with a crystalline substrate, suggest that a network of hydrogen bonds, involving both the enzyme and the substrate, brings H₂O₂ into a strained reactive conformation and guides a derived hydroxyl radical toward formation of a copper-oxyl intermediate. The ini

SUBMITTER: Bissaro B 

PROVIDER: S-EPMC6983374 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature