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

 

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Opened Access Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength
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Author: Moreno Beltrán, José Blas
Díaz Moreno, Irene
González Arzola, Katiuska
Guerra Castellano, Alejandra
Velázquez Campoy, Adrián
Rosa Acosta, Miguel Ángel de la
Díaz Quintana, Antonio Jesús
Department: Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular
Date: 2015
Published in: FEBS Letters, 598 (4), 476-483.
Document type: Article
Abstract: 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 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.
Cite: Moreno Beltrán, B., Díaz Moreno, I., González Arzola, K., Guerra Castellano, A., Velázquez Campoy, A., Rosa Acosta, M.Á.d.l. y Díaz Quintana, A. (2015). Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength. FEBS Letters, 598 (4), 476-483.
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URI: https://hdl.handle.net/11441/69243

DOI: 10.1016/j.febslet.2015.01.004

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