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Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength

AuthorsMoreno-Beltrán, Blas ; Díaz-Moreno, Irene ; González-Arzola, Katiuska ; Guerra-Castellano, Alejandra ; Velázquez-Campoy, Adrián; Rosa, Miguel A. de la ; Díaz-Quintana, Antonio
KeywordsCytochrome c
Cytochrome bc1
Cytochrome c oxidase
Isothermal Titration Calorimetry
Nuclear magnetic resonance
Issue Date2015
CitationFEBS Letters, 598(4): 476-483 (2015)
AbstractThe 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 c1 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.
Publisher version (URL)http://dx.doi.org/10.1016/j.febslet.2015.01.004
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