Disentangling interfacial redox processes of proteins by SERR spectroscopy

Surface-enhanced resonance-Raman spectroelectrochemistry represents a powerful approach for studying the structure and reaction dynamics of redox proteins immobilized on biocompatible electrodes in fundamental and applied sciences. Using this approach it has been recently shown that electric fields...

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Detalles Bibliográficos
Autores principales:	Murgida, D.H., Hildebrandt, P.
Formato:	JOUR
Materias:	hemoprotein immobilized enzyme silver article chemistry electrochemistry electrode oxidation reduction reaction Raman spectrometry Electrochemistry Electrodes Enzymes, Immobilized Hemeproteins Oxidation-Reduction Silver Spectrum Analysis, Raman
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_03060012_v37_n5_p937_Murgida
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_03060012_v37_n5_p937_Murgida
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spelling	todo:paper_03060012_v37_n5_p937_Murgida2023-10-03T15:22:08Z Disentangling interfacial redox processes of proteins by SERR spectroscopy Murgida, D.H. Hildebrandt, P. hemoprotein immobilized enzyme silver article chemistry electrochemistry electrode oxidation reduction reaction Raman spectrometry Electrochemistry Electrodes Enzymes, Immobilized Hemeproteins Oxidation-Reduction Silver Spectrum Analysis, Raman Surface-enhanced resonance-Raman spectroelectrochemistry represents a powerful approach for studying the structure and reaction dynamics of redox proteins immobilized on biocompatible electrodes in fundamental and applied sciences. Using this approach it has been recently shown that electric fields of biologically relevant magnitude are able to influence crucial parameters for the functioning of a variety of soluble and membrane bound heme proteins. Electric field effects discussed in this tutorial review include modulation of redox potentials, reorganization energies, protein dynamics and redox-linked structural changes. © The Royal Society of Chemistry. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03060012_v37_n5_p937_Murgida
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	hemoprotein immobilized enzyme silver article chemistry electrochemistry electrode oxidation reduction reaction Raman spectrometry Electrochemistry Electrodes Enzymes, Immobilized Hemeproteins Oxidation-Reduction Silver Spectrum Analysis, Raman
spellingShingle	hemoprotein immobilized enzyme silver article chemistry electrochemistry electrode oxidation reduction reaction Raman spectrometry Electrochemistry Electrodes Enzymes, Immobilized Hemeproteins Oxidation-Reduction Silver Spectrum Analysis, Raman Murgida, D.H. Hildebrandt, P. Disentangling interfacial redox processes of proteins by SERR spectroscopy
topic_facet	hemoprotein immobilized enzyme silver article chemistry electrochemistry electrode oxidation reduction reaction Raman spectrometry Electrochemistry Electrodes Enzymes, Immobilized Hemeproteins Oxidation-Reduction Silver Spectrum Analysis, Raman
description	Surface-enhanced resonance-Raman spectroelectrochemistry represents a powerful approach for studying the structure and reaction dynamics of redox proteins immobilized on biocompatible electrodes in fundamental and applied sciences. Using this approach it has been recently shown that electric fields of biologically relevant magnitude are able to influence crucial parameters for the functioning of a variety of soluble and membrane bound heme proteins. Electric field effects discussed in this tutorial review include modulation of redox potentials, reorganization energies, protein dynamics and redox-linked structural changes. © The Royal Society of Chemistry.
format	JOUR
author	Murgida, D.H. Hildebrandt, P.
author_facet	Murgida, D.H. Hildebrandt, P.
author_sort	Murgida, D.H.
title	Disentangling interfacial redox processes of proteins by SERR spectroscopy
title_short	Disentangling interfacial redox processes of proteins by SERR spectroscopy
title_full	Disentangling interfacial redox processes of proteins by SERR spectroscopy
title_fullStr	Disentangling interfacial redox processes of proteins by SERR spectroscopy
title_full_unstemmed	Disentangling interfacial redox processes of proteins by SERR spectroscopy
title_sort	disentangling interfacial redox processes of proteins by serr spectroscopy
url	http://hdl.handle.net/20.500.12110/paper_03060012_v37_n5_p937_Murgida
work_keys_str_mv	AT murgidadh disentanglinginterfacialredoxprocessesofproteinsbyserrspectroscopy AT hildebrandtp disentanglinginterfacialredoxprocessesofproteinsbyserrspectroscopy
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Disentangling interfacial redox processes of proteins by SERR spectroscopy

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