Phosphate mediated adsorption and electron transfer of cytochrome c. A time-resolved SERR spectroelectrochemical study

The study of proteins immobilized on biomimetic or biocompatible electrodes represents an active field of research as it pursues both fundamental and technological interests. In this context, adsorption and redox properties of cytochrome c (Cyt) on different electrode surfaces have been extensively...

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Autores principales:	Capdevila, Daiana Andrea, Marmisolle, Waldemar Alejandro, Williams, Federico Jose, Murgida, Daniel Horacio
Publicado:	2013
Materias:	adenosine triphosphate cytochrome c phosphate adsorption article chemistry electrochemical analysis electrode electron electron transport kinetics metabolism oxidation reduction reaction protein tertiary structure Raman spectrometry time Adenosine Triphosphate Adsorption Cytochromes c Electrochemical Techniques Electrodes Electron Transport Electrons Kinetics Oxidation-Reduction Phosphates Protein Structure, Tertiary Spectrum Analysis, Raman Time Factors
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v15_n15_p5386_Capdevila http://hdl.handle.net/20.500.12110/paper_14639076_v15_n15_p5386_Capdevila
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_14639076_v15_n15_p5386_Capdevila
record_format	dspace
spelling	paper:paper_14639076_v15_n15_p5386_Capdevila2023-06-08T16:16:26Z Phosphate mediated adsorption and electron transfer of cytochrome c. A time-resolved SERR spectroelectrochemical study Capdevila, Daiana Andrea Marmisolle, Waldemar Alejandro Williams, Federico Jose Murgida, Daniel Horacio adenosine triphosphate cytochrome c phosphate adsorption article chemistry electrochemical analysis electrode electron electron transport kinetics metabolism oxidation reduction reaction protein tertiary structure Raman spectrometry time Adenosine Triphosphate Adsorption Cytochromes c Electrochemical Techniques Electrodes Electron Transport Electrons Kinetics Oxidation-Reduction Phosphates Protein Structure, Tertiary Spectrum Analysis, Raman Time Factors The study of proteins immobilized on biomimetic or biocompatible electrodes represents an active field of research as it pursues both fundamental and technological interests. In this context, adsorption and redox properties of cytochrome c (Cyt) on different electrode surfaces have been extensively reported, although in some cases with contradictory results. Here we report a SERR spectroelectrochemical study of the adsorption and electron transfer behaviour of the basic protein Cyt on electrodes coated with amino-terminated monolayers. The obtained results show that inorganic phosphate (Pi) and ATP anions are able to mediate high affinity binding of the protein with preservation of the native structure and rendering an average orientation that guarantees efficient pathways for direct electron transfer. These findings aid the design of Cyt-based bioelectronic devices and understanding the modulation by Pi and ATP of physiological functions of Cyt. © 2013 the Owner Societies. Fil:Capdevila, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Marmisollé, W.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Williams, F.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Murgida, D.H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2013 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v15_n15_p5386_Capdevila http://hdl.handle.net/20.500.12110/paper_14639076_v15_n15_p5386_Capdevila
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	adenosine triphosphate cytochrome c phosphate adsorption article chemistry electrochemical analysis electrode electron electron transport kinetics metabolism oxidation reduction reaction protein tertiary structure Raman spectrometry time Adenosine Triphosphate Adsorption Cytochromes c Electrochemical Techniques Electrodes Electron Transport Electrons Kinetics Oxidation-Reduction Phosphates Protein Structure, Tertiary Spectrum Analysis, Raman Time Factors
spellingShingle	adenosine triphosphate cytochrome c phosphate adsorption article chemistry electrochemical analysis electrode electron electron transport kinetics metabolism oxidation reduction reaction protein tertiary structure Raman spectrometry time Adenosine Triphosphate Adsorption Cytochromes c Electrochemical Techniques Electrodes Electron Transport Electrons Kinetics Oxidation-Reduction Phosphates Protein Structure, Tertiary Spectrum Analysis, Raman Time Factors Capdevila, Daiana Andrea Marmisolle, Waldemar Alejandro Williams, Federico Jose Murgida, Daniel Horacio Phosphate mediated adsorption and electron transfer of cytochrome c. A time-resolved SERR spectroelectrochemical study
topic_facet	adenosine triphosphate cytochrome c phosphate adsorption article chemistry electrochemical analysis electrode electron electron transport kinetics metabolism oxidation reduction reaction protein tertiary structure Raman spectrometry time Adenosine Triphosphate Adsorption Cytochromes c Electrochemical Techniques Electrodes Electron Transport Electrons Kinetics Oxidation-Reduction Phosphates Protein Structure, Tertiary Spectrum Analysis, Raman Time Factors
description	The study of proteins immobilized on biomimetic or biocompatible electrodes represents an active field of research as it pursues both fundamental and technological interests. In this context, adsorption and redox properties of cytochrome c (Cyt) on different electrode surfaces have been extensively reported, although in some cases with contradictory results. Here we report a SERR spectroelectrochemical study of the adsorption and electron transfer behaviour of the basic protein Cyt on electrodes coated with amino-terminated monolayers. The obtained results show that inorganic phosphate (Pi) and ATP anions are able to mediate high affinity binding of the protein with preservation of the native structure and rendering an average orientation that guarantees efficient pathways for direct electron transfer. These findings aid the design of Cyt-based bioelectronic devices and understanding the modulation by Pi and ATP of physiological functions of Cyt. © 2013 the Owner Societies.
author	Capdevila, Daiana Andrea Marmisolle, Waldemar Alejandro Williams, Federico Jose Murgida, Daniel Horacio
author_facet	Capdevila, Daiana Andrea Marmisolle, Waldemar Alejandro Williams, Federico Jose Murgida, Daniel Horacio
author_sort	Capdevila, Daiana Andrea
title	Phosphate mediated adsorption and electron transfer of cytochrome c. A time-resolved SERR spectroelectrochemical study
title_short	Phosphate mediated adsorption and electron transfer of cytochrome c. A time-resolved SERR spectroelectrochemical study
title_full	Phosphate mediated adsorption and electron transfer of cytochrome c. A time-resolved SERR spectroelectrochemical study
title_fullStr	Phosphate mediated adsorption and electron transfer of cytochrome c. A time-resolved SERR spectroelectrochemical study
title_full_unstemmed	Phosphate mediated adsorption and electron transfer of cytochrome c. A time-resolved SERR spectroelectrochemical study
title_sort	phosphate mediated adsorption and electron transfer of cytochrome c. a time-resolved serr spectroelectrochemical study
publishDate	2013
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v15_n15_p5386_Capdevila http://hdl.handle.net/20.500.12110/paper_14639076_v15_n15_p5386_Capdevila
work_keys_str_mv	AT capdeviladaianaandrea phosphatemediatedadsorptionandelectrontransferofcytochromecatimeresolvedserrspectroelectrochemicalstudy AT marmisollewaldemaralejandro phosphatemediatedadsorptionandelectrontransferofcytochromecatimeresolvedserrspectroelectrochemicalstudy AT williamsfedericojose phosphatemediatedadsorptionandelectrontransferofcytochromecatimeresolvedserrspectroelectrochemicalstudy AT murgidadanielhoracio phosphatemediatedadsorptionandelectrontransferofcytochromecatimeresolvedserrspectroelectrochemicalstudy
_version_	1768544927400067072

Phosphate mediated adsorption and electron transfer of cytochrome c. A time-resolved SERR spectroelectrochemical study

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