Artículo
Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength
Autor/es | 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 de publicación | 2015 |
Fecha de depósito | 2018-01-19 |
Publicado en |
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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 ... 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. |
Identificador del proyecto | Grant PAI, BIO198
BFU2010-19451/BMC BFU2012-31670/BMC AP2009-4092 |
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. |
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