Mimicking the Reactivity of LPMOs with a Mononuclear Cu Complex.

ABSTRACT: Lytic polysaccharide monooxygenases (LPMOs) are Cu-dependent metalloenzymes that catalyze the hydroxylation of strong C-H bonds in polysaccharides using O₂ or H₂O₂ as oxidants (monooxygenase/peroxygenase). In the absence of C-H substrate, LPMOs reduce O₂ to H₂O₂ (oxidase) and H₂O₂ to H₂O (peroxidase) using proton/electron donors. This rich oxidative reactivity is promoted by a mononuclear Cu center in which some of the amino acid residues surrounding the metal might can accept and donate protons and/or electrons during O₂ and H₂O₂ reduction. Herein, we utilize a podal ligand containing H-bond/proton donors (LH₂) to analyze the reactivity of mononucl

SUBMITTER: Sagar K 

PROVIDER: S-EPMC11719791 | biostudies-literature | 2024 May

REPOSITORIES: biostudies-literature