Journal
FEBS LETTERS
Volume 589, Issue 4, Pages 476-483Publisher
WILEY
DOI: 10.1016/j.febslet.2015.01.004
Keywords
Cytochrome c; Cytochrome bc(1); Cytochrome c oxidase; Isothermal Titration Calorimetry; Nuclear Magnetic Resonance; Supercomplex
Funding
- Spanish Ministry of Economy and Competitiveness [BFU2010-19451/BMC, BFU2012-31670/BMC]
- Andalusian Government [PAI, BIO198]
- Spanish Ministry of Education [AP2009-4092]
- European Social Fund-ERDF
- CSIC [JaePre-2011-01248]
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The transient interactions of respiratory cytochrome c with complexes III and IV is herein investigated by using heterologous proteins, namely human cytochrome c, the soluble domain of plant cytochrome c(1) and bovine cytochrome c oxidase. The binding molecular mechanisms of the resulting cross-complexes have been analyzed by Nuclear Magnetic Resonance and Isothermal Titration Calorimetry. Our data reveal that the two cytochrome c-involving adducts possess a 2:1 stoichiometry - that is, two cytochrome c molecules per adduct - at low ionic strength. We conclude that such extra binding sites at the surfaces of complexes III and IV can facilitate the turnover and sliding of cytochrome c molecules and, therefore, the electron transfer within respiratory supercomplexes. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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