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Title: Redox-linked conformational changes of a multiheme cytochrome from Geobacter sulfurreducens

Abstract

Multiheme c-type cytochromes from members of the Desulfovibrionacea and Geobactereacea families play crucial roles in the bioenergetics of these microorganisms. Thermodynamic studies using NMR and visible spectroscopic techniques on tetraheme cytochromes c {sub 3} isolated from Desulfovibrio spp. and more recently on a triheme cytochrome from Geobacter sulfurreducens showed that the properties of each redox centre are modulated by the neighbouring redox centres enabling these proteins to perform energy transduction and thus contributing to cellular energy conservation. Electron/proton transfer coupling relies on redox-linked conformational changes that were addressed for some multiheme cytochromes from the comparison of protein structure of fully reduced and fully oxidised forms. In this work, we identify for the first time in a multiheme cytochrome the simultaneous presence of two different conformations in solution. This was achieved by probing the different oxidation stages of a triheme cytochrome isolated from G. sulfurreducens using 2D-NMR techniques. The results presented here will be the foundations to evaluate the modulation of the redox centres properties by conformational changes that occur during the reoxidation of a multiheme protein.

Authors:
 [1];  [2];  [3];  [3];  [3];  [4]
  1. Requimte - CQFB, Departamento de Quimica, Faculdade de Ciencias e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica (Portugal)
  2. Departamento de Espectroscopia y Estructura Molecular, Instituto de Quimica-Fisica 'Rocasolano', CSIC, Serrano 119, 28006 Madrid (Spain)
  3. Biosciences Division, Argonne National Laboratory, Argonne, IL 60439 (United States)
  4. Requimte - CQFB, Departamento de Quimica, Faculdade de Ciencias e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica (Portugal). E-mail: csalgueiro@dq.fct.unl.pt
Publication Date:
OSTI Identifier:
20991497
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 360; Journal Issue: 1; Other Information: DOI: 10.1016/j.bbrc.2007.06.026; PII: S0006-291X(07)01253-3; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CONFORMATIONAL CHANGES; COUPLING; CYTOCHROMES; DESULFOVIBRIO; ENERGY CONSERVATION; MODULATION; NUCLEAR MAGNETIC RESONANCE; OXIDATION; PROTEIN STRUCTURE

Citation Formats

Morgado, Leonor, Bruix, Marta, Londer, Yuri Y., Pokkuluri, P. Raj, Schiffer, Marianne, and Salgueiro, Carlos A. Redox-linked conformational changes of a multiheme cytochrome from Geobacter sulfurreducens. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2007.06.026.
Morgado, Leonor, Bruix, Marta, Londer, Yuri Y., Pokkuluri, P. Raj, Schiffer, Marianne, & Salgueiro, Carlos A. Redox-linked conformational changes of a multiheme cytochrome from Geobacter sulfurreducens. United States. doi:10.1016/j.bbrc.2007.06.026.
Morgado, Leonor, Bruix, Marta, Londer, Yuri Y., Pokkuluri, P. Raj, Schiffer, Marianne, and Salgueiro, Carlos A. Fri . "Redox-linked conformational changes of a multiheme cytochrome from Geobacter sulfurreducens". United States. doi:10.1016/j.bbrc.2007.06.026.
@article{osti_20991497,
title = {Redox-linked conformational changes of a multiheme cytochrome from Geobacter sulfurreducens},
author = {Morgado, Leonor and Bruix, Marta and Londer, Yuri Y. and Pokkuluri, P. Raj and Schiffer, Marianne and Salgueiro, Carlos A.},
abstractNote = {Multiheme c-type cytochromes from members of the Desulfovibrionacea and Geobactereacea families play crucial roles in the bioenergetics of these microorganisms. Thermodynamic studies using NMR and visible spectroscopic techniques on tetraheme cytochromes c {sub 3} isolated from Desulfovibrio spp. and more recently on a triheme cytochrome from Geobacter sulfurreducens showed that the properties of each redox centre are modulated by the neighbouring redox centres enabling these proteins to perform energy transduction and thus contributing to cellular energy conservation. Electron/proton transfer coupling relies on redox-linked conformational changes that were addressed for some multiheme cytochromes from the comparison of protein structure of fully reduced and fully oxidised forms. In this work, we identify for the first time in a multiheme cytochrome the simultaneous presence of two different conformations in solution. This was achieved by probing the different oxidation stages of a triheme cytochrome isolated from G. sulfurreducens using 2D-NMR techniques. The results presented here will be the foundations to evaluate the modulation of the redox centres properties by conformational changes that occur during the reoxidation of a multiheme protein.},
doi = {10.1016/j.bbrc.2007.06.026},
journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 1,
volume = 360,
place = {United States},
year = {2007},
month = {8}
}