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...

Descripción completa

Guardado en:
Detalles Bibliográficos
Publicado: 2008
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:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03060012_v37_n5_p937_Murgida
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 paper:paper_03060012_v37_n5_p937_Murgida
record_format dspace
spelling paper:paper_03060012_v37_n5_p937_Murgida2023-06-08T15:31:02Z Disentangling interfacial redox processes of proteins by SERR spectroscopy 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. 2008 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03060012_v37_n5_p937_Murgida 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
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.
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
publishDate 2008
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03060012_v37_n5_p937_Murgida
http://hdl.handle.net/20.500.12110/paper_03060012_v37_n5_p937_Murgida
_version_ 1768542597367726080

Ejemplares similares