dc.creator | Márquez Escudero, Inmaculada | es |
dc.creator | Pérez Mejías, Gonzalo | es |
dc.creator | Guerra Castellano, Alejandra | es |
dc.creator | Olloqui Sariego, José Luis | es |
dc.creator | Andreu Fondacabe, Rafael Jesús | es |
dc.creator | Calvente Pacheco, Juan José | es |
dc.creator | Rosa Acosta, Miguel Ángel de la | es |
dc.creator | Díaz Moreno, Irene | es |
dc.date.accessioned | 2021-11-19T15:31:23Z | |
dc.date.available | 2021-11-19T15:31:23Z | |
dc.date.issued | 2021 | |
dc.identifier.citation | Márquez Escudero, I., Pérez Mejías, G., Guerra Castellano, A., Olloqui Sariego, J.L., Andreu Fondacabe, R.J., Calvente Pacheco, J.J.,...,Díaz Moreno, I. (2021). Structural and functional insights into lysine acetylation of cytochrome c using mimetic point mutants. FEBS Open Bio | |
dc.identifier.issn | 2211-5463 | es |
dc.identifier.uri | https://hdl.handle.net/11441/127575 | |
dc.description.abstract | Post-translational modifications frequently modulate protein functions. Lysine acetylation in particular plays a key role in interactions between respiratory cytochrome c and its metabolic partners. To date, in vivo acetylation of lysines at positions 8 and 53 has specifically been identified in mammalian cytochrome c, but little is known about the structural basis of acetylation-induced functional changes. Here, we independently replaced these two residues in recombinant human cytochrome c with glutamine to mimic lysine acetylation and then characterized the structure and function of the resulting K8Q and K53Q mutants. We found that the physicochemical features were mostly unchanged in the two acetyl-mimetic mutants, but their thermal stability was significantly altered. NMR chemical shift perturbations of the backbone amide resonances revealed local structural changes, and the thermodynamics and kinetics of electron transfer in mutants immobilized on gold electrodes showed an increase in both protein dynamics and solvent involvement in the redox process. We also observed that the K8Q (but not the K53Q) mutation slightly increased the binding affinity of cytochrome c to its physiological electron donor, cytochrome c1—which is a component of mitochondrial complex III, or cytochrome bc1—thus suggesting that Lys8 (but not Lys53) is located in the interaction area. Finally, the K8Q and K53Q mutants exhibited reduced efficiency as electron donors to complex IV, or cytochrome c oxidase. | es |
dc.description.sponsorship | Ministerio de Ciencia e Innovación PGC2018-096049-B-I00 | es |
dc.description.sponsorship | Junta de Andalucía BIO-198, US-1254317, US-1257019, P18-FR-3487, P18-HO-4091 | es |
dc.format | application/pdf | es |
dc.format.extent | 20 p. | es |
dc.language.iso | eng | es |
dc.publisher | Wiley-Blackwell | es |
dc.relation.ispartof | FEBS Open Bio | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Acetylation | es |
dc.subject | Bioenergetics | es |
dc.subject | Cytochrome c | es |
dc.subject | Electron transport chain | es |
dc.subject | Post-translational modifications | es |
dc.title | Structural and functional insights into lysine acetylation of cytochrome c using mimetic point mutants | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Química Física | es |
dc.relation.projectID | PGC2018-096049-B-I00 | es |
dc.relation.projectID | BIO-198 | es |
dc.relation.projectID | US-1254317 | es |
dc.relation.projectID | US-1257019 | es |
dc.relation.projectID | P18-FR-3487 | es |
dc.relation.projectID | P18-HO-4091 | es |
dc.relation.publisherversion | https://doi.org/10.1002/2211-5463.13284 | es |
dc.identifier.doi | 10.1002/2211-5463.13284 | es |
dc.journaltitle | FEBS Open Bio | es |