Oxygen Activation at the Active Site of a Fungal Lytic Polysaccharide Monooxygenase.

ABSTRACT: Lytic polysaccharide monooxygenases have attracted vast attention owing to their abilities to disrupt glycosidic bonds via oxidation instead of hydrolysis and to enhance enzymatic digestion of recalcitrant substrates including chitin and cellulose. We have determined high-resolution X-ray crystal structures of an enzyme from Neurospora crassa in the resting state and of a copper(II) dioxo intermediate complex formed in the absence of substrate. X-ray crystal structures also revealed "pre-bound" molecular oxygen adjacent to the active site. An examination of protonation states enabled by neutron crystallography and density functional theory calculations identified a role for a conserved histidine in promoting oxygen activation. These results provide a new structural description of oxygen ac

SUBMITTER: O'Dell WB 

PROVIDER: S-EPMC5340418 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature