Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c
Most of the biochemical and biophysical processes of proteins take place at membranes, and are thus under the influence of strong local electric fields, which are likely to affect the structure as well as the reaction mechanism and dynamics. To analyse such electric field effects, biomimetic interfa...
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paper:paper_1742464X_v278_n9_p1382_KhoaLy2023-06-08T16:27:03Z Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c Murgida, Daniel Horacio apoptosis cytochrome c electric field electron transfer protein dynamics surface-enhanced infrared spectroscopy surface-enhanced resonance Raman spectroscopy cytochrome c hemoprotein nanomaterial absorption spectroscopy apoptosis artificial membrane biomimetic interface controlled study device diffusion electric field electrode electron transport enzyme immobilization membrane model oxidation reduction reaction priority journal protein function protein interaction protein structure respiratory chain review spectroscopy surface enhanced infrared absorption surface enhanced resonance Raman surface enhanced vibrational spectroscopy transient interaction Biomimetics Cytochromes c Electrons Molecular Probes Molecular Structure Oxidation-Reduction Protein Binding Proteins Spectrum Analysis Vibration Most of the biochemical and biophysical processes of proteins take place at membranes, and are thus under the influence of strong local electric fields, which are likely to affect the structure as well as the reaction mechanism and dynamics. To analyse such electric field effects, biomimetic interfaces may be employed that consist of membrane models deposited on nanostructured metal electrodes. For such devices, surface-enhanced resonance Raman and IR absorption spectroscopy are powerful techniques to disentangle the complex interfacial processes of proteins in terms of rotational diffusion, electron transfer, and protein and cofactor structural changes. The present article reviews the results obtained for the haem protein cytochrome c, which is widely used as a model protein for studying the various reaction steps of interfacial redox processes in general. In addition, it is shown that electric field effects may be functional for the natural redox processes of cytochrome c in the respiratory chain, as well as for the switch from the redox to the peroxidase function, one of the key events preceding apoptosis. The review focuses on the effects of local electric fields on cytochrome c bound to coated electrodes. For such devices that mimic the electrostatic properties of biological membranes surface-sensitive spectroelectrochemicals allow for an in-depth analysis of the molecular processes of the immobilised cytochrome c, contributing to a better understanding of the potential electric-field dependent control of the protein's function. © 2011 The Authors Journal compilation © 2011 FEBS. Fil:Murgida, D.H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2011 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1742464X_v278_n9_p1382_KhoaLy http://hdl.handle.net/20.500.12110/paper_1742464X_v278_n9_p1382_KhoaLy |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
apoptosis cytochrome c electric field electron transfer protein dynamics surface-enhanced infrared spectroscopy surface-enhanced resonance Raman spectroscopy cytochrome c hemoprotein nanomaterial absorption spectroscopy apoptosis artificial membrane biomimetic interface controlled study device diffusion electric field electrode electron transport enzyme immobilization membrane model oxidation reduction reaction priority journal protein function protein interaction protein structure respiratory chain review spectroscopy surface enhanced infrared absorption surface enhanced resonance Raman surface enhanced vibrational spectroscopy transient interaction Biomimetics Cytochromes c Electrons Molecular Probes Molecular Structure Oxidation-Reduction Protein Binding Proteins Spectrum Analysis Vibration |
| spellingShingle |
apoptosis cytochrome c electric field electron transfer protein dynamics surface-enhanced infrared spectroscopy surface-enhanced resonance Raman spectroscopy cytochrome c hemoprotein nanomaterial absorption spectroscopy apoptosis artificial membrane biomimetic interface controlled study device diffusion electric field electrode electron transport enzyme immobilization membrane model oxidation reduction reaction priority journal protein function protein interaction protein structure respiratory chain review spectroscopy surface enhanced infrared absorption surface enhanced resonance Raman surface enhanced vibrational spectroscopy transient interaction Biomimetics Cytochromes c Electrons Molecular Probes Molecular Structure Oxidation-Reduction Protein Binding Proteins Spectrum Analysis Vibration Murgida, Daniel Horacio Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c |
| topic_facet |
apoptosis cytochrome c electric field electron transfer protein dynamics surface-enhanced infrared spectroscopy surface-enhanced resonance Raman spectroscopy cytochrome c hemoprotein nanomaterial absorption spectroscopy apoptosis artificial membrane biomimetic interface controlled study device diffusion electric field electrode electron transport enzyme immobilization membrane model oxidation reduction reaction priority journal protein function protein interaction protein structure respiratory chain review spectroscopy surface enhanced infrared absorption surface enhanced resonance Raman surface enhanced vibrational spectroscopy transient interaction Biomimetics Cytochromes c Electrons Molecular Probes Molecular Structure Oxidation-Reduction Protein Binding Proteins Spectrum Analysis Vibration |
| description |
Most of the biochemical and biophysical processes of proteins take place at membranes, and are thus under the influence of strong local electric fields, which are likely to affect the structure as well as the reaction mechanism and dynamics. To analyse such electric field effects, biomimetic interfaces may be employed that consist of membrane models deposited on nanostructured metal electrodes. For such devices, surface-enhanced resonance Raman and IR absorption spectroscopy are powerful techniques to disentangle the complex interfacial processes of proteins in terms of rotational diffusion, electron transfer, and protein and cofactor structural changes. The present article reviews the results obtained for the haem protein cytochrome c, which is widely used as a model protein for studying the various reaction steps of interfacial redox processes in general. In addition, it is shown that electric field effects may be functional for the natural redox processes of cytochrome c in the respiratory chain, as well as for the switch from the redox to the peroxidase function, one of the key events preceding apoptosis. The review focuses on the effects of local electric fields on cytochrome c bound to coated electrodes. For such devices that mimic the electrostatic properties of biological membranes surface-sensitive spectroelectrochemicals allow for an in-depth analysis of the molecular processes of the immobilised cytochrome c, contributing to a better understanding of the potential electric-field dependent control of the protein's function. © 2011 The Authors Journal compilation © 2011 FEBS. |
| author |
Murgida, Daniel Horacio |
| author_facet |
Murgida, Daniel Horacio |
| author_sort |
Murgida, Daniel Horacio |
| title |
Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c |
| title_short |
Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c |
| title_full |
Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c |
| title_fullStr |
Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c |
| title_full_unstemmed |
Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: Electric field effects on structure, dynamics and function of cytochrome c |
| title_sort |
surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: electric field effects on structure, dynamics and function of cytochrome c |
| publishDate |
2011 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1742464X_v278_n9_p1382_KhoaLy http://hdl.handle.net/20.500.12110/paper_1742464X_v278_n9_p1382_KhoaLy |
| work_keys_str_mv |
AT murgidadanielhoracio surfaceenhancedvibrationalspectroscopyforprobingtransientinteractionsofproteinswithbiomimeticinterfaceselectricfieldeffectsonstructuredynamicsandfunctionofcytochromec |
| _version_ |
1768544704506363904 |