INQUIMAE   12526
INSTITUTO DE QUIMICA, FISICA DE LOS MATERIALES, MEDIOAMBIENTE Y ENERGIA
Unidad Ejecutora - UE
artículos
Título:
Disentangling interfacial redox processes of proteins by SERR spectroscopy
Autor/es:
MURGIDA, D. H.; HILDEBRANDT, P.
Revista:
CHEMICAL SOCIETY REVIEWS (PRINT)
Referencias:
Año: 2008 vol. 37 p. 937 - 937
ISSN:
0306-0012
Resumen:
Surface-enhanced resonance-Raman spectroelectrochemistry represents a powerful approach forstudying the structure and reaction dynamics of redox proteins immobilized on biocompatibleelectrodes in fundamental and applied sciences. Using this approach it has been recently shownthat electric fields of biologically relevant magnitude are able to influence crucial parameters forthe functioning of a variety of soluble and membrane bound heme proteins. Electric field effectsdiscussed in this tutorial review include modulation of redox potentials, reorganization energies,protein dynamics and redox-linked structural changes.