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...

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Detalles Bibliográficos
Autor principal: Murgida, Daniel Horacio
Publicado: 2008
Materias:
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
Kinetics
Protein Conformation
Silver
Spectrum Analysis, Raman
Sulfhydryl Compounds
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v130_n30_p9844_Kranich
http://hdl.handle.net/20.500.12110/paper_00027863_v130_n30_p9844_Kranich
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_00027863_v130_n30_p9844_Kranich
record_format dspace
spelling paper:paper_00027863_v130_n30_p9844_Kranich2023-06-08T14:22:44Z Direct observation of the gating step in protein electron transfer: Electric-field-controlled protein dynamics Murgida, Daniel Horacio 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. 2008 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v130_n30_p9844_Kranich 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
Murgida, Daniel Horacio
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.
author Murgida, Daniel Horacio
author_facet Murgida, Daniel Horacio
author_sort Murgida, Daniel Horacio
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
publishDate 2008
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v130_n30_p9844_Kranich
http://hdl.handle.net/20.500.12110/paper_00027863_v130_n30_p9844_Kranich
work_keys_str_mv AT murgidadanielhoracio directobservationofthegatingstepinproteinelectrontransferelectricfieldcontrolledproteindynamics
_version_ 1768541541534531584

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