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Significance Degradation of polysaccharides such as cellulose is biologically important for fungi and bacteria and industrially relevant for production of second-generation biofuels. Enzymes called lytic polysaccharide monooxygenases (LPMOs) catalyze the degradation of crystalline polysaccharide substrates. These enzymes have mononuclear copper active sites that use reductant and an oxygen source to oxidatively cleave polysaccharide bonds. An important controversy remains regarding the role ofH 2 O 2 as the reactant in oxygenation. Here, we present data consistent with the involvement ofH 2 O 2 in the catalytic cycle. Our spectroscopic data define the identities of intermediates formed duringH 2 O 2 reaction with an LPMO and we develop a kinetic model that provides mechanistic insight into peroxidase reactivity that involves homolytic activity of theH 2 O 2 .

proceedings of the national academy of sciences of the united states of america

Kinetic analysis of amino acid radicals formed in H 2 O 2 -driven Cu I LPMO reoxidation implicates dominant homolytic reactivity