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dc.contributor.authorGonzález Ayala, Julián 
dc.contributor.authorCalvo Hernández, Antonio 
dc.contributor.authorSantillán, Moisés
dc.date.accessioned2022-11-28T15:36:57Z
dc.date.available2022-11-28T15:36:57Z
dc.date.issued2023-02
dc.identifier.issn0301-4622
dc.identifier.urihttp://hdl.handle.net/10366/151206
dc.description.abstract[EN]Previous research has suggested that molecular energy converters such as ATP synthases, ion pumps, and cotransporters operate via spatially separate pathways for free energy donor and acceptor reactions linked by a protein molecule. We present a chemical kinetics model based on these works, with the basic assumption that all molecular energy converters can be thought of as linked enzymatic reactions, one running downhill the chemical potential gradient and driving the other uphill. To develop the model we first look at how an enzyme process can be forced to go backwards using a basic kinetic model. We then use these findings to suggest a thermodynamically consistent method of linking two enzymatic reactions. Finally, in the context of the aforementioned energy converters, the thermodynamic performance of the resulting model is thoroughly investigated and the obtained results are contrasted with experimental data.es_ES
dc.description.sponsorshipConacyt-M´exico, Grant No. CDF19-568462; University of Salamanca, Contract No. 0218 463AB01es_ES
dc.format.mimetypeapplication/pdf
dc.language.isoenges_ES
dc.subjectMolecular energy converters
dc.subjectCoupled enzymes
dc.subjectThermodynamic optimization
dc.subjectIrreversible thermodynamics
dc.subjectATP synthasees_ES
dc.titleThermodynamic performance of coupled enzymatic reactions: A chemical kinetics model for analyzing cotransporters, ion pumps, and ATP synthaseses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.relation.publishversionhttps://doi.org/10.1016/j.bpc.2022.106932
dc.subject.unesco2210.03 Cinética Química
dc.identifier.doi10.1016/j.bpc.2022.106932
dc.rights.accessRightsinfo:eu-repo/semantics/embargoedAccesses_ES
dc.journal.titleBiophysical Chemistryes_ES
dc.volume.number293es_ES
dc.page.initial106932es_ES
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersiones_ES


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