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, D.A., Marmisollé, W.A., Williams, F.J., Murgida, D.H.
Formato: JOUR
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: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 todo:paper_14639076_v15_n15_p5386_Capdevila
record_format dspace
spelling todo:paper_14639076_v15_n15_p5386_Capdevila2023-10-03T16:16:48Z Phosphate mediated adsorption and electron transfer of cytochrome c. A time-resolved SERR spectroelectrochemical study Capdevila, D.A. Marmisollé, W.A. Williams, F.J. Murgida, D.H. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, D.A.
Marmisollé, W.A.
Williams, F.J.
Murgida, D.H.
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.
format JOUR
author Capdevila, D.A.
Marmisollé, W.A.
Williams, F.J.
Murgida, D.H.
author_facet Capdevila, D.A.
Marmisollé, W.A.
Williams, F.J.
Murgida, D.H.
author_sort Capdevila, D.A.
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
url http://hdl.handle.net/20.500.12110/paper_14639076_v15_n15_p5386_Capdevila
work_keys_str_mv AT capdevilada phosphatemediatedadsorptionandelectrontransferofcytochromecatimeresolvedserrspectroelectrochemicalstudy
AT marmisollewa phosphatemediatedadsorptionandelectrontransferofcytochromecatimeresolvedserrspectroelectrochemicalstudy
AT williamsfj phosphatemediatedadsorptionandelectrontransferofcytochromecatimeresolvedserrspectroelectrochemicalstudy
AT murgidadh phosphatemediatedadsorptionandelectrontransferofcytochromecatimeresolvedserrspectroelectrochemicalstudy
_version_ 1782029752200069120

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