Cytochrome c Oxidase Models. A Novel Dinuclear Iron/Copper Complex Derived from a Covalently Modified Deuteroporphyrin-L-Histidine-Bis(benzimidazole) Ligand
Articolo
Data di Pubblicazione:
1996
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 species
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
Tipologia CRIS:
1.1 Articolo in rivista
Elenco autori:
Franceschi, F.; Gullotti, M.; Monzani, Enrico; Casella, Luigi; Papaefthymiou, V.
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