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Binding of ligands originates small perturbations on the microscopic thermodynamic properties of a multicentre redox protein

Binding of ligands originates small perturbations on the microscopic thermodynamic properties of a multicentre redox protein
Binding of ligands originates small perturbations on the microscopic thermodynamic properties of a multicentre redox protein
NMR and visible spectroscopy coupled to redox measurements were used to determine the equilibrium thermodynamic properties of the four haems in cytochrome c(3) under conditions in which the protein was bound to ligands, the small anion phosphate and the protein rubredoxin with the iron in the active site replaced by zinc. Comparison of these results with data for the isolated cytochrome shows that binding of ligands causes only small changes in the reduction potentials of the haems and their pairwise interactions, and also that the redox-sensitive acid-base centre responsible for the redox-Bohr effect is essentially unaffected. Although neither of the ligands tested is a physiological partner of cytochrome c(3), the small changes observed for the thermodynamic properties of cytochrome c(3) bound to these ligands vs. the unbound state, indicate that the thermodynamic properties measured for the isolated protein are relevant for a physiological interpretation of the role of this cytochrome in the bioenergetic metabolism of Desulfovibrio.
cytochrome c(3), electron transfer, nmr, protein docking, thermodynamic properties, sulfate-reducing bacteria, desulfovibrio-vulgaris hildenborough, tetrahaem cytochrome c(3), electron-transfer, multiheme cytochromes, diglycerol phosphate, energy transduction, miyazaki-f, complex
1742-464X
2251-2260
Salgueiro, Carlos A.
a9805ac9-e610-42ca-bb85-ef4e288eeffb
Morgado, Leonor
8b1e4378-117c-45bb-b3f5-6ac6490a7cf2
Fonseca, Bruno
34c9eab7-4446-4942-ab9a-c587f5eb8168
Lamosa, Pedro
9c2fdf0a-8bc3-4ed6-b295-f26bc448bfd7
Catarino, Teresa
608a4400-1611-4798-bf27-7472e7c6a476
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29
Louro, Ricardo O.
8014cf88-eb58-4ecd-8e04-8ce90a4e43f6
Salgueiro, Carlos A.
a9805ac9-e610-42ca-bb85-ef4e288eeffb
Morgado, Leonor
8b1e4378-117c-45bb-b3f5-6ac6490a7cf2
Fonseca, Bruno
34c9eab7-4446-4942-ab9a-c587f5eb8168
Lamosa, Pedro
9c2fdf0a-8bc3-4ed6-b295-f26bc448bfd7
Catarino, Teresa
608a4400-1611-4798-bf27-7472e7c6a476
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29
Louro, Ricardo O.
8014cf88-eb58-4ecd-8e04-8ce90a4e43f6

Salgueiro, Carlos A., Morgado, Leonor, Fonseca, Bruno, Lamosa, Pedro, Catarino, Teresa, Turner, David L. and Louro, Ricardo O. (2005) Binding of ligands originates small perturbations on the microscopic thermodynamic properties of a multicentre redox protein. Febs Journal, 272 (9), 2251-2260. (doi:10.1111/j.1742-4658.2005.04649.x).

Record type: Article

Abstract

NMR and visible spectroscopy coupled to redox measurements were used to determine the equilibrium thermodynamic properties of the four haems in cytochrome c(3) under conditions in which the protein was bound to ligands, the small anion phosphate and the protein rubredoxin with the iron in the active site replaced by zinc. Comparison of these results with data for the isolated cytochrome shows that binding of ligands causes only small changes in the reduction potentials of the haems and their pairwise interactions, and also that the redox-sensitive acid-base centre responsible for the redox-Bohr effect is essentially unaffected. Although neither of the ligands tested is a physiological partner of cytochrome c(3), the small changes observed for the thermodynamic properties of cytochrome c(3) bound to these ligands vs. the unbound state, indicate that the thermodynamic properties measured for the isolated protein are relevant for a physiological interpretation of the role of this cytochrome in the bioenergetic metabolism of Desulfovibrio.

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More information

Published date: 1 May 2005
Keywords: cytochrome c(3), electron transfer, nmr, protein docking, thermodynamic properties, sulfate-reducing bacteria, desulfovibrio-vulgaris hildenborough, tetrahaem cytochrome c(3), electron-transfer, multiheme cytochromes, diglycerol phosphate, energy transduction, miyazaki-f, complex

Identifiers

Local EPrints ID: 20903
URI: http://eprints.soton.ac.uk/id/eprint/20903
ISSN: 1742-464X
PURE UUID: 2ea24ca5-046a-481f-b7ee-7d88a2fba0e4

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Date deposited: 28 Feb 2006
Last modified: 06 Oct 2020 23:43

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Contributors

Author: Carlos A. Salgueiro
Author: Leonor Morgado
Author: Bruno Fonseca
Author: Pedro Lamosa
Author: Teresa Catarino
Author: David L. Turner
Author: Ricardo O. Louro

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