The copper-containing enzymes Lytic Polysaccharide MonoOxygenases (LPMOs) are known as activity boosters for biomass conversion, in which recalcitrant polysaccharides such as cellulose and chitin undergo oxidative breakdown. Since their discovery, much attention has been paid to LPMOs structure, physical-spectroscopic properties, substrate scope, and mechanism of action occurring at the single copper active site which possesses nitrogen containing ligands. In fact, mechanistic-kinetic studies strongly suggest that LPMOs operate as efficient peroxygenases. In this report, we describe new work where we have adopted various Cu(ligand) systems which possess tripodal tetradentate N-coordination to probe the possibility of biomimetic reactivity. The results observed point to the development of ligand-copper ion bound O or O<sub>2</sub> derived species which exhibit enhanced O-H and C-H substrate bond activation chemistry.

Oxidative reactivity of copper complexes as bioinspired models of LPMOs

ACS Spring 2022

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