Phenol-Induced O-O Bond Cleavage in a Low-Spin Heme-Peroxo-Copper Complex: Implications for O₂ Reduction in Heme-Copper Oxidases.

ABSTRACT: This study evaluates the reaction of a biomimetic heme-peroxo-copper complex, {[(DCHIm)(F₈)Fe^III]-(O₂^2-)-[Cu^II(AN)]}⁺ (1), with a phenolic substrate, involving a net H-atom abstraction to cleave the bridging peroxo O-O bond that produces Fe^IV═O, Cu^II-OH, and phenoxyl radical moieties, analogous to the chemistry carried out in heme-copper oxidases (HCOs). A 3D potential energy surface generated for this reaction reveals two possible reaction pathways: one involves nearly complete proton transfer (PT) from the phenol to the peroxo ligand before the barrier; the other involves O-O homolysis, where the phenol remains H-bonding to the peroxo O_Cu in the transition state (TS) and transfers the H

SUBMITTER: Schaefer AW 

PROVIDER: S-EPMC5605297 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature