Structure-activity relationships for 1st-and 2nd-coordination sphere mutants of the Cu-dependent LPMO enzyme

Lytic Polysaccharide MonoOxygenases (LPMOs) are Cu-dependent enzymes that have attracted intensive research and industrial interest due to their unique capacity to catalyse the oxidative breakage of strong C-H bonds in lignocellulosic biomass and hence facilitate its valorisation. In this proposal, we aim to characterize, by means of X-ray absorption spectroscopy (XAS), the Cu-binding site in several 1st and 2nd coordination sphere LPMO mutants designed to boost the enzyme activity, broaden substrate scope and enhance its stability against self-inactivation. This study will deliver valuable structure-activity relationships useful to elucidate the enzyme mechanism, which is still debated, and develop further optimized LPMO variants.