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 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.
Murgida
Daniel H
DH
Departamento de Química Inorgánica, Analítica y Química Física/INQUIMAE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria Pab. 2, piso 1, C1428EHA-Buenos Aires, Argentina. dhmurgida@qi.fcen.uba.ar
Hildebrandt
Peter
P
D004563:Electrochemistry; D004566:Electrodes; D004800:Enzymes, Immobilized / Q000737:chemistry; D006420:Hemeproteins / Q000737:chemistry*; D010084:Oxidation-Reduction; D012834:Silver / Q000737:chemistry; D013059:Spectrum Analysis, Raman
D004800:Enzymes, Immobilized; D006420:Hemeproteins; D012834:Silver