A Copper Cage-Complex as Mimic of the pMMO Cu_C Site.

ABSTRACT: The active site of particulate methane monooxygenase (pMMO) and its mechanism of action are not known. Recently, the Cu_C site emerged as a potential active site, but to date it lacks any study on biomimetic resemblance of the coordination environment provided by the enzyme. Here, the synthesis of a cage ligand providing such an environment is reported. Copper is incorporated, and coordination occurs by the two imidazole and one carboxylate group offered by the ligand. Depending on the oxidation state, it can adopt different coordination modes, as evidenced by the solid-state structures and computational investigation. The copper(I) state readily reacts with dioxygen and thereby undergoes CH activation. Moreover, the catalytic aerobic oxidation of hydroquinones as ubiquinol mimic

SUBMITTER: Bete SC 

PROVIDER: S-EPMC9544873 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature