dc.creator | Moreno Beltrán, José Blas | es |
dc.creator | Díaz Moreno, Irene | es |
dc.creator | González Arzola, Katiuska | es |
dc.creator | Guerra Castellano, Alejandra | es |
dc.creator | Velázquez Campoy, Adrián | es |
dc.creator | Rosa Acosta, Miguel Ángel de la | es |
dc.creator | Díaz Quintana, Antonio Jesús | es |
dc.date.accessioned | 2018-01-19T12:59:15Z | |
dc.date.available | 2018-01-19T12:59:15Z | |
dc.date.issued | 2015 | |
dc.identifier.citation | 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. | |
dc.identifier.issn | 0014-5793 | es |
dc.identifier.uri | https://hdl.handle.net/11441/69243 | |
dc.description.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. | es |
dc.description.sponsorship | España, MINECO Grant Nos. BFU2010-19451/BMC and BFU2012-31670/BMC | es |
dc.description.sponsorship | Junta de Andalucía Grant PAI, BIO198 | es |
dc.description.sponsorship | España Ministerio de Educación, y European Social Fund-ERDF AP2009-4092 | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Elsevier | es |
dc.relation.ispartof | FEBS Letters, 598 (4), 476-483. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Cytochrome c | es |
dc.subject | Cytochrome bc1 | es |
dc.subject | Cytochrome c oxidase | es |
dc.subject | Isothermal Titration Calorimetry | es |
dc.subject | Nuclear magnetic resonance | es |
dc.title | Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/submittedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular | es |
dc.relation.projectID | Grant PAI, BIO198 | es |
dc.relation.projectID | BFU2010-19451/BMC | es |
dc.relation.projectID | BFU2012-31670/BMC | es |
dc.relation.projectID | AP2009-4092 | es |
dc.relation.publisherversion | http://dx.doi.org/10.1016/j.febslet.2015.01.004 | es |
dc.identifier.doi | 10.1016/j.febslet.2015.01.004 | es |
idus.format.extent | 7 p. | es |
dc.journaltitle | FEBS Letters | es |
dc.publication.volumen | 598 | es |
dc.publication.issue | 4 | es |
dc.publication.initialPage | 476 | es |
dc.publication.endPage | 483 | es |