Thermal fluctuations determine the electron-transfer rates of cytochrome c in electrostatic and covalent complexes
The heterogeneous electron-transfer (ET) reaction of cytochrome c (Cyt-c) electrostatically or covalently immobilized on electrodes coated with self-assembled monolayers (SAMs) of ω-functionalized alkanethiols is analyzed by surface-enhanced resonance Raman (SERR) spectroscopy and molecular dynamics...
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_14394235_v11_n6_p1225_Ly |
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todo:paper_14394235_v11_n6_p1225_Ly2023-10-03T16:16:16Z Thermal fluctuations determine the electron-transfer rates of cytochrome c in electrostatic and covalent complexes Ly, H.K. Marti, M.A. Martin, D.F. Alvarez-Paggi, D. Meister, W. Kranich, A. Weidinger, I.M. Hildebrandt, P. Murgida, D.H. Electron transfer Molecular dynamics Monolayers Proteins Time-resolved spectroscopy cytochrome c immobilized protein article chemistry electrode electron transport kinetics molecular dynamics oxidation reduction reaction Raman spectrometry static electricity thermodynamics Cytochromes c Electrodes Electron Transport Immobilized Proteins Kinetics Molecular Dynamics Simulation Oxidation-Reduction Spectrum Analysis, Raman Static Electricity Thermodynamics The heterogeneous electron-transfer (ET) reaction of cytochrome c (Cyt-c) electrostatically or covalently immobilized on electrodes coated with self-assembled monolayers (SAMs) of ω-functionalized alkanethiols is analyzed by surface-enhanced resonance Raman (SERR) spectroscopy and molecular dynamics (MD) simulations. Electrostatically bound Cyt-c on pure carboxyl-terminated and mixed carboxyl/hydroxyl-terminated SAMs reveals the same distance dependence of the rate constants, that is, electron tunneling at long distances and a regime controlled by the protein orientational distribution and dynamics that leads to a nearly distance-independent rate constant at short distances. Qualitatively, the same behavior is found for covalently bound Cyt-c, although the apparent ET rates in the plateau region are lower since protein mobility is restricted due to formation of amide bonds between the protein and the SAM. The experimental findings are consistent with the results of MD simulations indicating that thermal fluctuations of the protein and interfacial solvent molecules can effectively modulate the electron tunneling probability. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. Fil:Marti, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Alvarez-Paggi, D. 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_14394235_v11_n6_p1225_Ly |
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Universidad de Buenos Aires |
| institution_str |
I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Electron transfer Molecular dynamics Monolayers Proteins Time-resolved spectroscopy cytochrome c immobilized protein article chemistry electrode electron transport kinetics molecular dynamics oxidation reduction reaction Raman spectrometry static electricity thermodynamics Cytochromes c Electrodes Electron Transport Immobilized Proteins Kinetics Molecular Dynamics Simulation Oxidation-Reduction Spectrum Analysis, Raman Static Electricity Thermodynamics |
| spellingShingle |
Electron transfer Molecular dynamics Monolayers Proteins Time-resolved spectroscopy cytochrome c immobilized protein article chemistry electrode electron transport kinetics molecular dynamics oxidation reduction reaction Raman spectrometry static electricity thermodynamics Cytochromes c Electrodes Electron Transport Immobilized Proteins Kinetics Molecular Dynamics Simulation Oxidation-Reduction Spectrum Analysis, Raman Static Electricity Thermodynamics Ly, H.K. Marti, M.A. Martin, D.F. Alvarez-Paggi, D. Meister, W. Kranich, A. Weidinger, I.M. Hildebrandt, P. Murgida, D.H. Thermal fluctuations determine the electron-transfer rates of cytochrome c in electrostatic and covalent complexes |
| topic_facet |
Electron transfer Molecular dynamics Monolayers Proteins Time-resolved spectroscopy cytochrome c immobilized protein article chemistry electrode electron transport kinetics molecular dynamics oxidation reduction reaction Raman spectrometry static electricity thermodynamics Cytochromes c Electrodes Electron Transport Immobilized Proteins Kinetics Molecular Dynamics Simulation Oxidation-Reduction Spectrum Analysis, Raman Static Electricity Thermodynamics |
| description |
The heterogeneous electron-transfer (ET) reaction of cytochrome c (Cyt-c) electrostatically or covalently immobilized on electrodes coated with self-assembled monolayers (SAMs) of ω-functionalized alkanethiols is analyzed by surface-enhanced resonance Raman (SERR) spectroscopy and molecular dynamics (MD) simulations. Electrostatically bound Cyt-c on pure carboxyl-terminated and mixed carboxyl/hydroxyl-terminated SAMs reveals the same distance dependence of the rate constants, that is, electron tunneling at long distances and a regime controlled by the protein orientational distribution and dynamics that leads to a nearly distance-independent rate constant at short distances. Qualitatively, the same behavior is found for covalently bound Cyt-c, although the apparent ET rates in the plateau region are lower since protein mobility is restricted due to formation of amide bonds between the protein and the SAM. The experimental findings are consistent with the results of MD simulations indicating that thermal fluctuations of the protein and interfacial solvent molecules can effectively modulate the electron tunneling probability. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. |
| format |
JOUR |
| author |
Ly, H.K. Marti, M.A. Martin, D.F. Alvarez-Paggi, D. Meister, W. Kranich, A. Weidinger, I.M. Hildebrandt, P. Murgida, D.H. |
| author_facet |
Ly, H.K. Marti, M.A. Martin, D.F. Alvarez-Paggi, D. Meister, W. Kranich, A. Weidinger, I.M. Hildebrandt, P. Murgida, D.H. |
| author_sort |
Ly, H.K. |
| title |
Thermal fluctuations determine the electron-transfer rates of cytochrome c in electrostatic and covalent complexes |
| title_short |
Thermal fluctuations determine the electron-transfer rates of cytochrome c in electrostatic and covalent complexes |
| title_full |
Thermal fluctuations determine the electron-transfer rates of cytochrome c in electrostatic and covalent complexes |
| title_fullStr |
Thermal fluctuations determine the electron-transfer rates of cytochrome c in electrostatic and covalent complexes |
| title_full_unstemmed |
Thermal fluctuations determine the electron-transfer rates of cytochrome c in electrostatic and covalent complexes |
| title_sort |
thermal fluctuations determine the electron-transfer rates of cytochrome c in electrostatic and covalent complexes |
| url |
http://hdl.handle.net/20.500.12110/paper_14394235_v11_n6_p1225_Ly |
| work_keys_str_mv |
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1807315889115103232 |