Direct observation of the gating step in protein electron transfer: Electric-field-controlled protein dynamics
Heterogeneous electron transfer of proteins at biomimetic interfaces is characterized by unusual distance dependences of the electron-transfer rates, whose origin has been elusive and controversial. Using a two-color, time-resolved, surface-enhanced resonance Raman spectroelectrochemical approach, w...
Guardado en:
Autores principales: | , , , |
---|---|
Formato: | JOUR |
Materias: | |
Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00027863_v130_n30_p9844_Kranich |
Aporte de: |
id |
todo:paper_00027863_v130_n30_p9844_Kranich |
---|---|
record_format |
dspace |
spelling |
todo:paper_00027863_v130_n30_p9844_Kranich2023-10-03T13:53:58Z Direct observation of the gating step in protein electron transfer: Electric-field-controlled protein dynamics Kranich, A. Ly, H.K. Hildebrandt, P. Murgida, D.H. American Chemical Society (ACS) Biomimetic interfaces Cytochrome c (Cyt c) Direct observation Electron transfer (ET) Electron transfer kinetics Electron transfer rates Heterogeneous electron transfer (HET) Monitor (CO) Protein dynamics Real time Self assembled monolayers (SAMs) Spectroelectrochemical Surface-Enhanced Resonance Time-resolved Two-color Biological membranes Biomimetics Dynamics Electric fields Electromagnetic field theory Electromagnetic fields Electron transitions Metallizing Self assembled monolayers Electrons cytochrome c article electric field electricity electrochemical analysis electrode electron transport protein analysis protein assembly Raman spectrometry Cytochromes c Electrochemistry Electrodes Electrons Kinetics Protein Conformation Silver Spectrum Analysis, Raman Sulfhydryl Compounds Heterogeneous electron transfer of proteins at biomimetic interfaces is characterized by unusual distance dependences of the electron-transfer rates, whose origin has been elusive and controversial. Using a two-color, time-resolved, surface-enhanced resonance Raman spectroelectrochemical approach, we have been able to monitor simultaneously and in real time the structure, electron-transfer kinetics, and configurational fluctuations of cytochrome c electrostatically adsorbed to electrodes coated with self-assembled monolayers. Our results show that the overall electron-transfer kinetics is determined by protein dynamics rather than by tunnelling probabilities and that the protein dynamics in turn is controlled by the interfacial electric field. Implications for interprotein electron transfer at biological membranes are discussed. © 2008 American Chemical Society. 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_00027863_v130_n30_p9844_Kranich |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
American Chemical Society (ACS) Biomimetic interfaces Cytochrome c (Cyt c) Direct observation Electron transfer (ET) Electron transfer kinetics Electron transfer rates Heterogeneous electron transfer (HET) Monitor (CO) Protein dynamics Real time Self assembled monolayers (SAMs) Spectroelectrochemical Surface-Enhanced Resonance Time-resolved Two-color Biological membranes Biomimetics Dynamics Electric fields Electromagnetic field theory Electromagnetic fields Electron transitions Metallizing Self assembled monolayers Electrons cytochrome c article electric field electricity electrochemical analysis electrode electron transport protein analysis protein assembly Raman spectrometry Cytochromes c Electrochemistry Electrodes Electrons Kinetics Protein Conformation Silver Spectrum Analysis, Raman Sulfhydryl Compounds |
spellingShingle |
American Chemical Society (ACS) Biomimetic interfaces Cytochrome c (Cyt c) Direct observation Electron transfer (ET) Electron transfer kinetics Electron transfer rates Heterogeneous electron transfer (HET) Monitor (CO) Protein dynamics Real time Self assembled monolayers (SAMs) Spectroelectrochemical Surface-Enhanced Resonance Time-resolved Two-color Biological membranes Biomimetics Dynamics Electric fields Electromagnetic field theory Electromagnetic fields Electron transitions Metallizing Self assembled monolayers Electrons cytochrome c article electric field electricity electrochemical analysis electrode electron transport protein analysis protein assembly Raman spectrometry Cytochromes c Electrochemistry Electrodes Electrons Kinetics Protein Conformation Silver Spectrum Analysis, Raman Sulfhydryl Compounds Kranich, A. Ly, H.K. Hildebrandt, P. Murgida, D.H. Direct observation of the gating step in protein electron transfer: Electric-field-controlled protein dynamics |
topic_facet |
American Chemical Society (ACS) Biomimetic interfaces Cytochrome c (Cyt c) Direct observation Electron transfer (ET) Electron transfer kinetics Electron transfer rates Heterogeneous electron transfer (HET) Monitor (CO) Protein dynamics Real time Self assembled monolayers (SAMs) Spectroelectrochemical Surface-Enhanced Resonance Time-resolved Two-color Biological membranes Biomimetics Dynamics Electric fields Electromagnetic field theory Electromagnetic fields Electron transitions Metallizing Self assembled monolayers Electrons cytochrome c article electric field electricity electrochemical analysis electrode electron transport protein analysis protein assembly Raman spectrometry Cytochromes c Electrochemistry Electrodes Electrons Kinetics Protein Conformation Silver Spectrum Analysis, Raman Sulfhydryl Compounds |
description |
Heterogeneous electron transfer of proteins at biomimetic interfaces is characterized by unusual distance dependences of the electron-transfer rates, whose origin has been elusive and controversial. Using a two-color, time-resolved, surface-enhanced resonance Raman spectroelectrochemical approach, we have been able to monitor simultaneously and in real time the structure, electron-transfer kinetics, and configurational fluctuations of cytochrome c electrostatically adsorbed to electrodes coated with self-assembled monolayers. Our results show that the overall electron-transfer kinetics is determined by protein dynamics rather than by tunnelling probabilities and that the protein dynamics in turn is controlled by the interfacial electric field. Implications for interprotein electron transfer at biological membranes are discussed. © 2008 American Chemical Society. |
format |
JOUR |
author |
Kranich, A. Ly, H.K. Hildebrandt, P. Murgida, D.H. |
author_facet |
Kranich, A. Ly, H.K. Hildebrandt, P. Murgida, D.H. |
author_sort |
Kranich, A. |
title |
Direct observation of the gating step in protein electron transfer: Electric-field-controlled protein dynamics |
title_short |
Direct observation of the gating step in protein electron transfer: Electric-field-controlled protein dynamics |
title_full |
Direct observation of the gating step in protein electron transfer: Electric-field-controlled protein dynamics |
title_fullStr |
Direct observation of the gating step in protein electron transfer: Electric-field-controlled protein dynamics |
title_full_unstemmed |
Direct observation of the gating step in protein electron transfer: Electric-field-controlled protein dynamics |
title_sort |
direct observation of the gating step in protein electron transfer: electric-field-controlled protein dynamics |
url |
http://hdl.handle.net/20.500.12110/paper_00027863_v130_n30_p9844_Kranich |
work_keys_str_mv |
AT kranicha directobservationofthegatingstepinproteinelectrontransferelectricfieldcontrolledproteindynamics AT lyhk directobservationofthegatingstepinproteinelectrontransferelectricfieldcontrolledproteindynamics AT hildebrandtp directobservationofthegatingstepinproteinelectrontransferelectricfieldcontrolledproteindynamics AT murgidadh directobservationofthegatingstepinproteinelectrontransferelectricfieldcontrolledproteindynamics |
_version_ |
1782029268041072640 |