Cytochrome c oxidase models. A novel dinuclear iron–copper complex derived from a covalently modified deuteroporphyrin–L-histidine–bis(benzimidazole) ligand

Abstract

The iron(III)–copper(II) complex derived from a covalently modified deuteroporphyrin at both carboxylate ends of the two propionic acid side chains is described as a model for the dioxygen reduction site of cytochrome c oxidase; it exhibits a weak coupling between the metal centres, and its fully reduced Fe^IICu^I form reacts smoothly and nondestructively with dioxygen at room temperature to produce the Fe^IIICu^II species.