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Disentangling interfacial redox processes of proteins by SERR spectroscopy
Citation key ISI:000255444700007
Author Murgida, D H and Hildebrandt, P
Pages 937-945
Year 2008
ISSN 0306-0012
DOI 10.1039/b705976k
Address THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND
Journal Chem. Soc. Rev.
Volume 37
Number 5
Publisher ROYAL SOC CHEMISTRY
Abstract 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.
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