Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function.

ABSTRACT: Heme-copper oxidases (HCOs) are terminal enzymes on the mitochondrial or bacterial respiratory electron transport chain, which utilize a unique heterobinuclear active site to catalyze the 4H⁺/4e^- reduction of dioxygen to water. This process involves a proton-coupled electron transfer (PCET) from a tyrosine (phenolic) residue and additional redox events coupled to transmembrane proton pumping and ATP synthesis. Given that HCOs are large, complex, membrane-bound enzymes, bioinspired synthetic model chemistry is a promising approach to better understand heme-Cu-mediated dioxygen reduction, including the details of proton and electron movements. This review encompasses important aspects of heme-O₂ and copper-O₂ (bio)chemistries as they relate to the

SUBMITTER: Adam SM 

PROVIDER: S-EPMC6360144 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature