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Abstract:

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.

Registro:

Documento: Artículo
Título:Phosphate mediated adsorption and electron transfer of cytochrome c. A time-resolved SERR spectroelectrochemical study
Autor:Capdevila, D.A.; Marmisollé, W.A.; Williams, F.J.; Murgida, D.H.
Filiación:Departamento de Química Inorgánica, Analítica y Química Física, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, piso 3, C1428EHA-Buenos Aires, Argentina
Palabras clave: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
Año:2013
Volumen:15
Número:15
Página de inicio:5386
Página de fin:5394
DOI: http://dx.doi.org/10.1039/c2cp42044a
Título revista:Physical Chemistry Chemical Physics
Título revista abreviado:Phys. Chem. Chem. Phys.
ISSN:14639076
CODEN:PPCPF
CAS:adenosine triphosphate, 15237-44-2, 56-65-5, 987-65-5; cytochrome c, 9007-43-6, 9064-84-0; phosphate, 14066-19-4, 14265-44-2; Adenosine Triphosphate, 56-65-5; Cytochromes c, 9007-43-6; Phosphates
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14639076_v15_n15_p5386_Capdevila

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Citas:

---------- APA ----------
Capdevila, D.A., Marmisollé, W.A., Williams, F.J. & Murgida, D.H. (2013) . Phosphate mediated adsorption and electron transfer of cytochrome c. A time-resolved SERR spectroelectrochemical study. Physical Chemistry Chemical Physics, 15(15), 5386-5394.
http://dx.doi.org/10.1039/c2cp42044a
---------- CHICAGO ----------
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" . Physical Chemistry Chemical Physics 15, no. 15 (2013) : 5386-5394.
http://dx.doi.org/10.1039/c2cp42044a
---------- MLA ----------
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" . Physical Chemistry Chemical Physics, vol. 15, no. 15, 2013, pp. 5386-5394.
http://dx.doi.org/10.1039/c2cp42044a
---------- VANCOUVER ----------
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. Phys. Chem. Chem. Phys. 2013;15(15):5386-5394.
http://dx.doi.org/10.1039/c2cp42044a