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Conformational component in the coupled transfer of multiple electrons and protons in a monomeric tetraheme cytochrome

Conformational component in the coupled transfer of multiple electrons and protons in a monomeric tetraheme cytochrome
Conformational component in the coupled transfer of multiple electrons and protons in a monomeric tetraheme cytochrome
Cell metabolism relies on energy transduction usually performed by complex membrane-spanning proteins that couple different chemical processes, e.g. electron and proton transfer in proton-pumps. There is great interest in determining at the molecular level the structural details that control these energy transduction events, particularly those involving multiple electrons and protons, because tight control is required to avoid the production of dangerous reactive intermediates. Tetraheme cytochrome c(3) is a small soluble and monomeric protein that performs a central step in the bioenergetic, metabolism of sulfate reducing bacteria, termed "proton-thrusting," linking the oxidation of molecular hydrogen with the reduction of sulfate. The mechanochemical coupling involved in the transfer of multiple electrons and protons in cytochrome c. from Desulfovibrio desulfuricans ATCC 27774 is described using results derived from the microscopic thermodynamic characterization of the redox and acid-base centers involved, crystallographic studies in the oxidized and reduced states of the cytochrome, and theoretical studies of the redox and acid-base transitions. This proton-assisted two-electron step involves very small, localized structural changes that are sufficient to generate the complex network of functional cooperativities leading to energy transduction, while using molecular mechanisms distinct from those established for other Desulfovibrio sp. cytochromes from the same structural family.
desulfovibrio-vulgaris hildenborough, x-ray-diffraction, desulfuricans atcc-27774, energy transduction, angstrom resolution, structural basis, c-oxidase, c(3), redox, ranslocation
0021-9258
44044-44051
Louro, Ricardo O.
8014cf88-eb58-4ecd-8e04-8ce90a4e43f6
Bento, Isabel
a3d32ac0-a472-49b6-903b-f2d3cafe0323
Matias, Pedro M.
2635a4c4-da64-4694-aaa5-800f5b4fb5e9
Catarino, Teresa
608a4400-1611-4798-bf27-7472e7c6a476
Baptista, António M.
e8b5a4a2-7ca2-42fb-a2ae-3f7e7af63c07
Soares, Cláudio M.
eced7465-ffc0-4730-9996-57797e55ec53
Carrondo, Maria Arménia
26a04601-ce94-4cc9-a2f4-0d6a3c2ba544
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29
Xavier, António V.
77269a6a-27cb-4c75-abf0-7d03ac64c228
Louro, Ricardo O.
8014cf88-eb58-4ecd-8e04-8ce90a4e43f6
Bento, Isabel
a3d32ac0-a472-49b6-903b-f2d3cafe0323
Matias, Pedro M.
2635a4c4-da64-4694-aaa5-800f5b4fb5e9
Catarino, Teresa
608a4400-1611-4798-bf27-7472e7c6a476
Baptista, António M.
e8b5a4a2-7ca2-42fb-a2ae-3f7e7af63c07
Soares, Cláudio M.
eced7465-ffc0-4730-9996-57797e55ec53
Carrondo, Maria Arménia
26a04601-ce94-4cc9-a2f4-0d6a3c2ba544
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29
Xavier, António V.
77269a6a-27cb-4c75-abf0-7d03ac64c228

Louro, Ricardo O., Bento, Isabel, Matias, Pedro M., Catarino, Teresa, Baptista, António M., Soares, Cláudio M., Carrondo, Maria Arménia, Turner, David L. and Xavier, António V. (2001) Conformational component in the coupled transfer of multiple electrons and protons in a monomeric tetraheme cytochrome. The Journal of Biological Chemistry, 276 (47), 44044-44051. (doi:10.1074/jbc.M107136200).

Record type: Article

Abstract

Cell metabolism relies on energy transduction usually performed by complex membrane-spanning proteins that couple different chemical processes, e.g. electron and proton transfer in proton-pumps. There is great interest in determining at the molecular level the structural details that control these energy transduction events, particularly those involving multiple electrons and protons, because tight control is required to avoid the production of dangerous reactive intermediates. Tetraheme cytochrome c(3) is a small soluble and monomeric protein that performs a central step in the bioenergetic, metabolism of sulfate reducing bacteria, termed "proton-thrusting," linking the oxidation of molecular hydrogen with the reduction of sulfate. The mechanochemical coupling involved in the transfer of multiple electrons and protons in cytochrome c. from Desulfovibrio desulfuricans ATCC 27774 is described using results derived from the microscopic thermodynamic characterization of the redox and acid-base centers involved, crystallographic studies in the oxidized and reduced states of the cytochrome, and theoretical studies of the redox and acid-base transitions. This proton-assisted two-electron step involves very small, localized structural changes that are sufficient to generate the complex network of functional cooperativities leading to energy transduction, while using molecular mechanisms distinct from those established for other Desulfovibrio sp. cytochromes from the same structural family.

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More information

Published date: 23 November 2001
Keywords: desulfovibrio-vulgaris hildenborough, x-ray-diffraction, desulfuricans atcc-27774, energy transduction, angstrom resolution, structural basis, c-oxidase, c(3), redox, ranslocation

Identifiers

Local EPrints ID: 19560
URI: http://eprints.soton.ac.uk/id/eprint/19560
ISSN: 0021-9258
PURE UUID: 96505689-1ac1-497b-94ae-ee9eaaea8935

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

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Contributors

Author: Ricardo O. Louro
Author: Isabel Bento
Author: Pedro M. Matias
Author: Teresa Catarino
Author: António M. Baptista
Author: Cláudio M. Soares
Author: Maria Arménia Carrondo
Author: David L. Turner
Author: António V. Xavier

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