2024-03-28T14:49:21Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/1102792018-08-07T07:31:44Zcom_10261_80com_10261_1com_10261_34com_10261_5col_10261_333col_10261_287
Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength
Moreno-Beltrán, Blas
Díaz-Moreno, Irene
González-Arzola, Katiuska
Guerra-Castellano, Alejandra
Velázquez-Campoy, Adrián
Rosa, Miguel A. de la
Díaz-Quintana, Antonio
Cytochrome c
Cytochrome bc1
Cytochrome c oxidase
Isothermal Titration Calorimetry
Nuclear magnetic resonance
Supercomplex
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.
2015-02-05T10:10:23Z
2015-02-05T10:10:23Z
2015
artículo
FEBS Letters, 598(4): 476-483 (2015)
http://hdl.handle.net/10261/110279
10.1016/j.febslet.2015.01.004
25595453
eng
Postprint
http://dx.doi.org/10.1016/j.febslet.2015.01.004
Sí
http://creativecommons.org/licenses/by-nc-nd/4.0/
openAccess
Elsevier