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dc.provenanceCONICET-
dc.creatorKhoa Ly, Hong-
dc.creatorSezer, Murat-
dc.creatorWisitruangsakul, Nattawadee-
dc.creatorFeng, Jiu-Ju-
dc.creatorKranich, Anja-
dc.creatorMillo, Diego-
dc.creatorWeidinger, Inez M.-
dc.creatorZebger, Ingo-
dc.creatorMurgida, Daniel Horacio-
dc.creatorHildebrandt, Peter-
dc.date2019-03-19T16:06:40Z-
dc.date2019-03-19T16:06:40Z-
dc.date2011-05-
dc.date2019-03-08T20:16:43Z-
dc.date.accessioned2019-04-29T15:39:22Z-
dc.date.available2019-04-29T15:39:22Z-
dc.date.issued2011-05-
dc.identifierKhoa Ly, Hong; Sezer, Murat; Wisitruangsakul, Nattawadee; Feng, Jiu-Ju; Kranich, Anja; et al.; Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c; Wiley Blackwell Publishing, Inc; Febs Journal; 278; 9; 5-2011; 1382-1390-
dc.identifier1742-464X-
dc.identifierhttp://hdl.handle.net/11336/72003-
dc.identifierCONICET Digital-
dc.identifierCONICET-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/298694-
dc.descriptionMost of the biochemical and biophysical processes of proteins take place at membranes, and are thus under the influence of strong local electric fields, which are likely to affect the structure as well as the reaction mechanism and dynamics. To analyse such electric field effects, biomimetic interfaces may be employed that consist of membrane models deposited on nanostructured metal electrodes. For such devices, surface-enhanced resonance Raman and IR absorption spectroscopy are powerful techniques to disentangle the complex interfacial processes of proteins in terms of rotational diffusion, electron transfer, and protein and cofactor structural changes. The present article reviews the results obtained for the haem protein cytochrome c, which is widely used as a model protein for studying the various reaction steps of interfacial redox processes in general. In addition, it is shown that electric field effects may be functional for the natural redox processes of cytochrome c in the respiratory chain, as well as for the switch from the redox to the peroxidase function, one of the key events preceding apoptosis. The review focuses on the effects of local electric fields on cytochrome c bound to coated electrodes. For such devices that mimic the electrostatic properties of biological membranes surface-sensitive spectroelectrochemicals allow for an in-depth analysis of the molecular processes of the immobilised cytochrome c, contributing to a better understanding of the potential electric-field dependent control of the protein's function. © 2011 The Authors Journal compilation © 2011 FEBS.-
dc.descriptionFil: Khoa Ly, Hong. Technishe Universitat Berlin; Alemania-
dc.descriptionFil: Sezer, Murat. Technishe Universitat Berlin; Alemania-
dc.descriptionFil: Wisitruangsakul, Nattawadee. Technishe Universitat Berlin; Alemania. Iron and Steel Institute of Thailand; Tailandia-
dc.descriptionFil: Feng, Jiu-Ju. Technishe Universitat Berlin; Alemania. Henan Normal University; China-
dc.descriptionFil: Kranich, Anja. Technishe Universitat Berlin; Alemania-
dc.descriptionFil: Millo, Diego. Technishe Universitat Berlin; Alemania-
dc.descriptionFil: Weidinger, Inez M.. Technishe Universitat Berlin; Alemania-
dc.descriptionFil: Zebger, Ingo. Technishe Universitat Berlin; Alemania-
dc.descriptionFil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Inorgánica, Analítica y Química Física; Argentina-
dc.descriptionFil: Hildebrandt, Peter. Technishe Universitat Berlin; Alemania-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherWiley Blackwell Publishing, Inc-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1111/j.1742-4658.2011.08064.x-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://febs.onlinelibrary.wiley.com/doi/full/10.1111/j.1742-4658.2011.08064.x-
dc.rightsinfo:eu-repo/semantics/openAccess-
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.source.urihttp://hdl.handle.net/11336/72003-
dc.subjectAPOPTOSIS-
dc.subjectCYTOCHROME C-
dc.subjectELECTRIC FIELD-
dc.subjectELECTRON TRANSFER-
dc.subjectPROTEIN DYNAMICS-
dc.subjectSURFACE-ENHANCED INFRARED SPECTROSCOPY-
dc.subjectSURFACE-ENHANCED RESONANCE RAMAN SPECTROSCOPY-
dc.subjectOtras Ciencias Químicas-
dc.subjectCiencias Químicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleSurface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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