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Thermodynamic control of electron transfer rates in multicentre redox proteins

Thermodynamic control of electron transfer rates in multicentre redox proteins
Thermodynamic control of electron transfer rates in multicentre redox proteins
In the analysis of kinetic data from multicentre redox proteins, it is essential to distinguish between the observable macroscopic rate I constants and the structurally relevant microscopic properties. This distinction is complicated by the existence of interactions between centres. The problem is illustrated by the case of two interacting I redox centres and generalised for the analysis of stopped-flow kinetic data for the reduction of cytochrome c(3), in which four redox centres and at least one proteolytic centre are mutually interacting. It is shown that fast intramolecular electron transfer, which is typical of many multicentre redox proteins, and, where present, fast proton exchange, ensure that only N rate constants can be measured for a protein with N redox centres. The equations that relate the observable macroscopic rate constants to the microscopic rate constants of individual centres depend on a set of parameters that can be approximated by using the Marcus theory of electron transfer together with a set of reasonable assumptions. The results are tested by fitting experimental data for the reduction of cytochrome c(3) by sodium dithionite, including its pH dependence.
cytochromes, electron transfer, heme proteins, kinetics, marcus theory, desulfovibrio-gigas, cytochrome c(3), reduction, dithionite, mechanisms, couple
1439-4227
416-424
Catarino, Teresa
608a4400-1611-4798-bf27-7472e7c6a476
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29
Catarino, Teresa
608a4400-1611-4798-bf27-7472e7c6a476
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29

Catarino, Teresa and Turner, David L. (2001) Thermodynamic control of electron transfer rates in multicentre redox proteins. ChemBioChem, 2 (6), 416-424. (doi:10.1002/1439-7633(20010601)2:6<416::AID-CBIC416>3.0.CO;2-Z).

Record type: Article

Abstract

In the analysis of kinetic data from multicentre redox proteins, it is essential to distinguish between the observable macroscopic rate I constants and the structurally relevant microscopic properties. This distinction is complicated by the existence of interactions between centres. The problem is illustrated by the case of two interacting I redox centres and generalised for the analysis of stopped-flow kinetic data for the reduction of cytochrome c(3), in which four redox centres and at least one proteolytic centre are mutually interacting. It is shown that fast intramolecular electron transfer, which is typical of many multicentre redox proteins, and, where present, fast proton exchange, ensure that only N rate constants can be measured for a protein with N redox centres. The equations that relate the observable macroscopic rate constants to the microscopic rate constants of individual centres depend on a set of parameters that can be approximated by using the Marcus theory of electron transfer together with a set of reasonable assumptions. The results are tested by fitting experimental data for the reduction of cytochrome c(3) by sodium dithionite, including its pH dependence.

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More information

Published date: 2001
Keywords: cytochromes, electron transfer, heme proteins, kinetics, marcus theory, desulfovibrio-gigas, cytochrome c(3), reduction, dithionite, mechanisms, couple

Identifiers

Local EPrints ID: 19444
URI: http://eprints.soton.ac.uk/id/eprint/19444
ISSN: 1439-4227
PURE UUID: 6a39c642-11b7-4d48-9ec0-bb7daf4417fc

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Date deposited: 15 Feb 2006
Last modified: 15 Jul 2019 19:27

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