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Cooperativity between electrons and protons in a monomeric Cytochrome c3: the importance of mechano-chemical coupling for energy transduction

Cooperativity between electrons and protons in a monomeric Cytochrome c3: the importance of mechano-chemical coupling for energy transduction
Cooperativity between electrons and protons in a monomeric Cytochrome c3: the importance of mechano-chemical coupling for energy transduction
To fully understand the structural bases for the mechanisms of biological energy transduction, it is essential to determine the microscopic thermodynamic parameters which describe the properties of each centre involved in the reactions, as well as its interactions with the others. These interactions between centres can then be interpreted in the light of structural features of the proteins. Redox titrations of cytochrome c(3), from Desulfovibrio desulfuricans ATCC27774 followed by NMR and visible spectroscopy were analysed by using an equilibrium thermodynamic model. The network of homotropic and heterotropic cooperativities results in the coupled transfer of electrons and protons under physiological conditions. The microscopic characterisation allows the identification of several pairs of centres for which there are clear conformational (non-Coulombic) contributions to their coupling energies, thus establishing the existence of localised redox- and acid - base-linked structural modifications in the protein (mechano-chemical coupling). The modulation of interactions between centres observed for this cytochrome may be an important general phenomenon and is discussed in the framework of its physiological function and of the current focus of energy, transduction research.
cooperative phenomena, cytochromes, electrostatic interactions, heme proteins, nmr spectroscopydesulfovibrio-vulgaris hildenborough, desulfuricans atcc-27774, structural basis, miyazaki-f, c(3), redox, protein, reduction, gigas, nmr
1439-4227
831-837
Louro, Ricardo O.
8014cf88-eb58-4ecd-8e04-8ce90a4e43f6
Catarino, Teresa
608a4400-1611-4798-bf27-7472e7c6a476
LeGall, Jean
8b9fe4c9-d915-4c71-a05d-db0a771ed393
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29
Xavier, António V.
77269a6a-27cb-4c75-abf0-7d03ac64c228
Louro, Ricardo O.
8014cf88-eb58-4ecd-8e04-8ce90a4e43f6
Catarino, Teresa
608a4400-1611-4798-bf27-7472e7c6a476
LeGall, Jean
8b9fe4c9-d915-4c71-a05d-db0a771ed393
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29
Xavier, António V.
77269a6a-27cb-4c75-abf0-7d03ac64c228

Louro, Ricardo O., Catarino, Teresa, LeGall, Jean, Turner, David L. and Xavier, António V. (2001) Cooperativity between electrons and protons in a monomeric Cytochrome c3: the importance of mechano-chemical coupling for energy transduction. ChemBioChem, 2 (11), 831-837. (doi:10.1002/1439-7633(20011105)2:11<831::AID-CBIC831>3.0.CO;2-W).

Record type: Article

Abstract

To fully understand the structural bases for the mechanisms of biological energy transduction, it is essential to determine the microscopic thermodynamic parameters which describe the properties of each centre involved in the reactions, as well as its interactions with the others. These interactions between centres can then be interpreted in the light of structural features of the proteins. Redox titrations of cytochrome c(3), from Desulfovibrio desulfuricans ATCC27774 followed by NMR and visible spectroscopy were analysed by using an equilibrium thermodynamic model. The network of homotropic and heterotropic cooperativities results in the coupled transfer of electrons and protons under physiological conditions. The microscopic characterisation allows the identification of several pairs of centres for which there are clear conformational (non-Coulombic) contributions to their coupling energies, thus establishing the existence of localised redox- and acid - base-linked structural modifications in the protein (mechano-chemical coupling). The modulation of interactions between centres observed for this cytochrome may be an important general phenomenon and is discussed in the framework of its physiological function and of the current focus of energy, transduction research.

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More information

Published date: 5 November 2001
Keywords: cooperative phenomena, cytochromes, electrostatic interactions, heme proteins, nmr spectroscopydesulfovibrio-vulgaris hildenborough, desulfuricans atcc-27774, structural basis, miyazaki-f, c(3), redox, protein, reduction, gigas, nmr

Identifiers

Local EPrints ID: 19561
URI: http://eprints.soton.ac.uk/id/eprint/19561
ISSN: 1439-4227
PURE UUID: 863a1a4a-2326-437b-81d8-1c4a3aa5e69c

Catalogue record

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

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