Mechanistic basis of substrate-O₂ coupling within a chitin-active lytic polysaccharide monooxygenase: An integrated NMR/EPR study.

ABSTRACT: Lytic polysaccharide monooxygenases (LPMOs) have a unique ability to activate molecular oxygen for subsequent oxidative cleavage of glycosidic bonds. To provide insight into the mode of action of these industrially important enzymes, we have performed an integrated NMR/electron paramagnetic resonance (EPR) study into the detailed aspects of an AA10 LPMO-substrate interaction. Using NMR spectroscopy, we have elucidated the solution-phase structure of apo-BlLPMO10A from Bacillus licheniformis, along with solution-phase structural characterization of the Cu(I)-LPMO, showing that the presence of the metal has minimal effects on the overall protein structure. We have, moreover, used paramagnetic relaxation enhancement (PRE) to characterize Cu(II)-LPMO by NMR spectroscopy. I

SUBMITTER: Courtade G 

PROVIDER: S-EPMC7431007 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature