Abstract

Lytic polysaccharide monooxygenase (LPMO) metalloenzymes activate strong C─H bonds (~100 kcal/mol) of polysaccharides such as cellulose. Nature has evolved the ability to perform these thermodynamically difficult processes within LPMO using an active site composed of a single copper ion coordinated to the protein in a T-shaped geometry referred to as the histidine brace. Inspiration from LPMOs has led to the development of synthetic systems to perform multi-electron chemistry using copper complexes.