A functional model related to cytochrome c oxidase and its electrocatalytic four-electron reduction of O2

James P. Collman; Lei Fu; Paul C. Herrmann; Xumu Zhang

doi:10.1126/science.275.5302.949

A functional model related to cytochrome c oxidase and its electrocatalytic four-electron reduction of O₂

James P. Collman^*, Lei Fu, Paul C. Herrmann, Xumu Zhang

^*Corresponding author for this work

Stanford University

Research output: Contribution to journal › Article › peer-review

185 Citations (Scopus)

Abstract

A cytochrome c oxidase model that consists of a cobalt(II) porphyrin with a copper(I) triazacyclononane macrocycle fastened on the distal face and an imidazole covalently attached to the proximal face has been synthesized and characterized. Redox titrations with molecular oxygen (O₂) and cobaltocene were carried out, and O₂ was found to bind irreversibly in a 1:1 ratio to the model compound. This O₂ adduct (a bridged peroxide) can be fully reduced to the deoxygenated form with four equivalents of cobaltocene. The model compound was adsorbed on an edge-plane graphite electrode, and rotating ring-disk voltammetry was used to monitor the electrocatalytic reduction of O₂. Fourelectron reduction of O₂ was observed at physiological pH.

Original language	English
Pages (from-to)	949-951
Number of pages	3
Journal	Science
Volume	275
Issue number	5302
DOIs	https://doi.org/10.1126/science.275.5302.949
Publication status	Published - 14 Feb 1997
Externally published	Yes

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title = "A functional model related to cytochrome c oxidase and its electrocatalytic four-electron reduction of O2",

abstract = "A cytochrome c oxidase model that consists of a cobalt(II) porphyrin with a copper(I) triazacyclononane macrocycle fastened on the distal face and an imidazole covalently attached to the proximal face has been synthesized and characterized. Redox titrations with molecular oxygen (O2) and cobaltocene were carried out, and O2 was found to bind irreversibly in a 1:1 ratio to the model compound. This O2 adduct (a bridged peroxide) can be fully reduced to the deoxygenated form with four equivalents of cobaltocene. The model compound was adsorbed on an edge-plane graphite electrode, and rotating ring-disk voltammetry was used to monitor the electrocatalytic reduction of O2. Fourelectron reduction of O2 was observed at physiological pH.",

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AU - Collman, James P.

AU - Fu, Lei

AU - Herrmann, Paul C.

AU - Zhang, Xumu

PY - 1997/2/14

Y1 - 1997/2/14

N2 - A cytochrome c oxidase model that consists of a cobalt(II) porphyrin with a copper(I) triazacyclononane macrocycle fastened on the distal face and an imidazole covalently attached to the proximal face has been synthesized and characterized. Redox titrations with molecular oxygen (O2) and cobaltocene were carried out, and O2 was found to bind irreversibly in a 1:1 ratio to the model compound. This O2 adduct (a bridged peroxide) can be fully reduced to the deoxygenated form with four equivalents of cobaltocene. The model compound was adsorbed on an edge-plane graphite electrode, and rotating ring-disk voltammetry was used to monitor the electrocatalytic reduction of O2. Fourelectron reduction of O2 was observed at physiological pH.

AB - A cytochrome c oxidase model that consists of a cobalt(II) porphyrin with a copper(I) triazacyclononane macrocycle fastened on the distal face and an imidazole covalently attached to the proximal face has been synthesized and characterized. Redox titrations with molecular oxygen (O2) and cobaltocene were carried out, and O2 was found to bind irreversibly in a 1:1 ratio to the model compound. This O2 adduct (a bridged peroxide) can be fully reduced to the deoxygenated form with four equivalents of cobaltocene. The model compound was adsorbed on an edge-plane graphite electrode, and rotating ring-disk voltammetry was used to monitor the electrocatalytic reduction of O2. Fourelectron reduction of O2 was observed at physiological pH.

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A functional model related to cytochrome c oxidase and its electrocatalytic four-electron reduction of O2

Abstract

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A functional model related to cytochrome c oxidase and its electrocatalytic four-electron reduction of O₂