Capture of activated dioxygen intermediates at the copper-active site of a lytic polysaccharide monooxygenase.

ABSTRACT: Metalloproteins perform a diverse array of redox-related reactions facilitated by the increased chemical functionality afforded by their metallocofactors. Lytic polysaccharide monooxygenases (LPMOs) are a class of copper-dependent enzymes that are responsible for the breakdown of recalcitrant polysaccharides via oxidative cleavage at the glycosidic bond. The activated copper-oxygen intermediates and their mechanism of formation remains to be established. Neutron protein crystallography which permits direct visualization of protonation states was used to investigate the initial steps of oxygen activation directly following active site copper reduction in Neurospora crassa LPMO9D. Herein, we cryo-trap an activated dioxygen intermediate in a mixture of superoxo and hydroperoxo s

SUBMITTER: Schroder GC 

PROVIDER: S-EPMC9683017 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature