Reactivity of a heterobinuclear heme-peroxo-Cu complex with <i>para</i>-substituted catechols shows a p<i>K</i> _a-dependent change in mechanism.

ABSTRACT: In biological systems, heme-copper oxidase (HCO) enzymes play a crucial role in the oxygen reduction reaction (ORR), where the pivotal O-O bond cleavage of the (heme)Fe^III-peroxo-Cu^II intermediate is facilitated by active-site (peroxo core) hydrogen bonding followed by proton-coupled electron transfer (PCET) from a nearby (phenolic) tyrosine residue. A useful approach to comprehend the fundamental relationships among H-bonding/proton/H-atom donors and their abilities to induce O-O bond homolysis involves the investigation of synthetic, bioinspired model systems where the exogenous substrate properties (such as pK _a and bond dissociation energy (BDE)) can be systematically altered. This report details the reactivity of a heme-peroxo-copper HCO model c

SUBMITTER: Panda S 

PROVIDER: S-EPMC11707526 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature