Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced infrared absorption spectroscopy

Time-resolved surface enhanced infrared absorption (SEIRA) spectroscopy is employed to analyse the dynamics of the protein structural changes coupled to the electron transfer process of immobilised cytochrome c (Cyt-c). Upon electrostatic binding of Cyt-c to Au electrodes coated with self-assembled...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Wisitruangsakul, N., Zebger, I., Ly, K.H., Murgida, D.H., Ekgasit, S., Hildebrandt, P.
Formato: JOUR
Materias:
cytochrome c
cytochrome c''
animal
article
chemistry
horse
infrared spectrophotometry
metabolism
methodology
oxidation reduction reaction
Animals
Cytochrome c Group
Horses
Oxidation-Reduction
Spectrophotometry, Infrared
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_14639076_v10_n34_p5276_Wisitruangsakul
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_14639076_v10_n34_p5276_Wisitruangsakul
record_format dspace
spelling todo:paper_14639076_v10_n34_p5276_Wisitruangsakul2023-10-03T16:16:42Z Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced infrared absorption spectroscopy Wisitruangsakul, N. Zebger, I. Ly, K.H. Murgida, D.H. Ekgasit, S. Hildebrandt, P. cytochrome c cytochrome c'' animal article chemistry horse infrared spectrophotometry metabolism methodology oxidation reduction reaction Animals Cytochrome c Group Horses Oxidation-Reduction Spectrophotometry, Infrared Time-resolved surface enhanced infrared absorption (SEIRA) spectroscopy is employed to analyse the dynamics of the protein structural changes coupled to the electron transfer process of immobilised cytochrome c (Cyt-c). Upon electrostatic binding of Cyt-c to Au electrodes coated with self-assembled monolayers (SAMs) of carboxyl-terminated thiols, cyclic voltammetric measurements demonstrate a reversible redox process with a redox potential that is similar to that of Cyt-c in solution, and a non-exponential distance-dependence of the electron transfer rate as observed previously (D. H. Murgida and P. Hildebrandt, Chem. Soc. Rev. 2008, 37, 937). On the basis of characteristic redox-state-sensitive amide I bands, the protein structural changes triggered by the electron transfer are monitored by rapid scan and step scan SEIRA spectroscopy in combination with the potential jump technique. Whereas the temporal evolution of the conjugate bands at 1693 and 1673 cm -1 displays the same rate constants as electron transfer, the time-dependent changes of the 1660-cm-1 band are slower by about a factor of 2. The study demonstrates that time-resolved SEIRA spectroscopy provides further information about the dynamics and mechanism of interfacial processes of redox proteins, thereby complementing the results obtained from other surface-sensitive techniques. In comparison with previous surface enhanced resonance Raman spectroscopic findings, the present results are discussed in terms of the local electric field strengths at the Au/SAM/Cyt-c interface. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_14639076_v10_n34_p5276_Wisitruangsakul
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic cytochrome c
cytochrome c''
animal
article
chemistry
horse
infrared spectrophotometry
metabolism
methodology
oxidation reduction reaction
Animals
Cytochrome c Group
Horses
Oxidation-Reduction
Spectrophotometry, Infrared
spellingShingle cytochrome c
cytochrome c''
animal
article
chemistry
horse
infrared spectrophotometry
metabolism
methodology
oxidation reduction reaction
Animals
Cytochrome c Group
Horses
Oxidation-Reduction
Spectrophotometry, Infrared
Wisitruangsakul, N.
Zebger, I.
Ly, K.H.
Murgida, D.H.
Ekgasit, S.
Hildebrandt, P.
Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced infrared absorption spectroscopy
topic_facet cytochrome c
cytochrome c''
animal
article
chemistry
horse
infrared spectrophotometry
metabolism
methodology
oxidation reduction reaction
Animals
Cytochrome c Group
Horses
Oxidation-Reduction
Spectrophotometry, Infrared
description Time-resolved surface enhanced infrared absorption (SEIRA) spectroscopy is employed to analyse the dynamics of the protein structural changes coupled to the electron transfer process of immobilised cytochrome c (Cyt-c). Upon electrostatic binding of Cyt-c to Au electrodes coated with self-assembled monolayers (SAMs) of carboxyl-terminated thiols, cyclic voltammetric measurements demonstrate a reversible redox process with a redox potential that is similar to that of Cyt-c in solution, and a non-exponential distance-dependence of the electron transfer rate as observed previously (D. H. Murgida and P. Hildebrandt, Chem. Soc. Rev. 2008, 37, 937). On the basis of characteristic redox-state-sensitive amide I bands, the protein structural changes triggered by the electron transfer are monitored by rapid scan and step scan SEIRA spectroscopy in combination with the potential jump technique. Whereas the temporal evolution of the conjugate bands at 1693 and 1673 cm -1 displays the same rate constants as electron transfer, the time-dependent changes of the 1660-cm-1 band are slower by about a factor of 2. The study demonstrates that time-resolved SEIRA spectroscopy provides further information about the dynamics and mechanism of interfacial processes of redox proteins, thereby complementing the results obtained from other surface-sensitive techniques. In comparison with previous surface enhanced resonance Raman spectroscopic findings, the present results are discussed in terms of the local electric field strengths at the Au/SAM/Cyt-c interface.
format JOUR
author Wisitruangsakul, N.
Zebger, I.
Ly, K.H.
Murgida, D.H.
Ekgasit, S.
Hildebrandt, P.
author_facet Wisitruangsakul, N.
Zebger, I.
Ly, K.H.
Murgida, D.H.
Ekgasit, S.
Hildebrandt, P.
author_sort Wisitruangsakul, N.
title Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced infrared absorption spectroscopy
title_short Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced infrared absorption spectroscopy
title_full Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced infrared absorption spectroscopy
title_fullStr Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced infrared absorption spectroscopy
title_full_unstemmed Redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced infrared absorption spectroscopy
title_sort redox-linked protein dynamics of cytochrome c probed by time-resolved surface enhanced infrared absorption spectroscopy
url http://hdl.handle.net/20.500.12110/paper_14639076_v10_n34_p5276_Wisitruangsakul
work_keys_str_mv AT wisitruangsakuln redoxlinkedproteindynamicsofcytochromecprobedbytimeresolvedsurfaceenhancedinfraredabsorptionspectroscopy
AT zebgeri redoxlinkedproteindynamicsofcytochromecprobedbytimeresolvedsurfaceenhancedinfraredabsorptionspectroscopy
AT lykh redoxlinkedproteindynamicsofcytochromecprobedbytimeresolvedsurfaceenhancedinfraredabsorptionspectroscopy
AT murgidadh redoxlinkedproteindynamicsofcytochromecprobedbytimeresolvedsurfaceenhancedinfraredabsorptionspectroscopy
AT ekgasits redoxlinkedproteindynamicsofcytochromecprobedbytimeresolvedsurfaceenhancedinfraredabsorptionspectroscopy
AT hildebrandtp redoxlinkedproteindynamicsofcytochromecprobedbytimeresolvedsurfaceenhancedinfraredabsorptionspectroscopy
_version_ 1807316294387630080

Ejemplares similares