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

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

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Autor: 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
Departamento: Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular
Fecha: 2015
Publicado en: FEBS Letters, 598 (4), 476-483.
Tipo de documento: Artículo
Resumen: 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.
Cita: 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.
Tamaño: 9.538Mb
Formato: PDF

URI: https://hdl.handle.net/11441/69243

DOI: 10.1016/j.febslet.2015.01.004

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