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dc.creatorÁlvarez Paggi, Damián Jorge-
dc.creatorCastro, Maria Ana-
dc.creatorTortora, Verónica-
dc.creatorCastro, Laura-
dc.creatorRadi, Rafael-
dc.creatorMurgida, Daniel Horacio-
dc.date2015-06-16T18:59:04Z-
dc.date2015-06-16T18:59:04Z-
dc.date2013-03-
dc.date2016-03-30 10:35:44.97925-03-
dc.date.accessioned2019-04-29T15:54:49Z-
dc.date.available2019-04-29T15:54:49Z-
dc.identifierÁlvarez Paggi, Damián Jorge; Castro, Maria Ana; Tortora, Verónica; Castro, Laura; Radi, Rafael; et al.; Electrostatically Driven Second-Sphere Ligand Switch between High and Low Reorganization Energy Forms of Native Cytochrome c; Amer Chemical Soc; Journal of the American Chemical Society; 135; 3-2013; 4389-4397-
dc.identifier0002-7863-
dc.identifierhttp://hdl.handle.net/11336/757-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/305204-
dc.descriptionWe have employed a combination of protein film voltammetry, time-resolved vibrational spectroelectrochemistry and molecular dynamics simulations to evaluate the electron-transfer reorganization free energy (λ) of cytochrome c (Cyt) in electrostatic complexes that mimic some basic features of protein–protein and protein–lipid interactions. The results reveal the existence of two native-like conformations of Cyt that present significantly different λ values. Conversion from the high to the low λ forms is triggered by electrostatic interactions, and involves the rupture of a weak H-bond between first- (M80) and second-sphere (Y67) ligands of the heme iron, as a distinctive feature of the conformational switch. The two flexible Ω loops operate as transducers of the electrostatic signal. This fine-tuning effect is abolished in the Y67F Cyt mutant, which presents a λ value similar to the WT protein in electrostatic complexes. We propose that interactions of Cyt with the natural redox partner proteins activate a similar mechanism to minimize the reorganization energy of interprotein electron transfer.-
dc.descriptionFil: Álvarez Paggi, Damián Jorge. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina;-
dc.descriptionFil: Castro, Maria Ana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina;-
dc.descriptionFil: Tortora, Verónica. Universidad de la República. Departamento de Bioquímica and Center for Free Radical and Biomedical Research; Uruguay;-
dc.descriptionFil: Castro, Laura. Universidad de la República. Departamento de Bioquímica and Center for Free Radical and Biomedical Research; Uruguay;-
dc.descriptionFil: Radi, Rafael. Universidad de la República. Departamento de Bioquímica and Center for Free Radical and Biomedical Research; Uruguay;-
dc.descriptionFil: Murgida, Daniel Horacio. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina;-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherAmer Chemical Soc-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/dx.doi.org/10.1021/ja311786b-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/ja311786b-
dc.rightsinfo:eu-repo/semantics/restrictedAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.subjectcytochrome c-
dc.subjectelectron transfer-
dc.subjectreorganization energy-
dc.subjectelectrostatic switch-
dc.subjectCiencias Naturales y Exactas-
dc.subjectCiencias Químicas-
dc.subjectFísico-química, Ciencia de Los Polímeros, Electroquímica-
dc.titleElectrostatically Driven Second-Sphere Ligand Switch between High and Low Reorganization Energy Forms of Native Cytochrome c-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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