The iron(m)-copper(Ir) 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 FeIICuI form reacts smoothly and nondestructively with dioxygen at room temperature to produce the FeIIICuII species
Cytochrome c Oxidase Models. A Novel Dinuclear Iron/Copper Complex Derived from a Covalently Modified Deuteroporphyrin-L-Histidine-Bis(benzimidazole) Ligand
MONZANI, ENRICO;CASELLA, LUIGI;
1996-01-01
Abstract
The iron(m)-copper(Ir) 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 FeIICuI form reacts smoothly and nondestructively with dioxygen at room temperature to produce the FeIIICuII speciesFile in questo prodotto:
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