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Most of the biochemical and biophysical processes of proteins take place at membranes, and are thus under the influence of strong local electric fields, which are likely to affect the structure as well as the reaction mecha-nism and dynamics. | IFEBS Journal MINIREVIEW Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces electric field effects on structure dynamics and function of cytochrome c Hong Khoa Ly1 Murat Sezer1 Nattawadee Wisitruangsakul1 2 Jiu-Ju Feng1 3 Anja Kranich1 Diego Millo1 Inez M. Weidinger1 Ingo Zebger1 Daniel H. Murgida4 and Peter Hildebrandt1 1 Technische Universitat Berlin Institut fur Chemie Germany 2 Iron and Steel Institute of Thailand Bangkok Thailand 3 Schoolof Chemistry and EnvironmentalScience Henan NormalUniversity Xinxiang China 4 Departamento de Quimica Inorganica Analitica y Quimica Fisica INQUIMAE-CONICET Facultad de Ciencias Exactas y Naturales Universi-dad de Buenos Aires Argentina Keywords apoptosis cytochrome c electric field electron transfer protein dynamics surface-enhanced infrared spectroscopy surface-enhanced resonance Raman spectroscopy Correspondence P. Hildebrandt Technische Universitat Berlin Institut fur Chemie Sekr. PC 14 StraBe des 17 Juni 135 D-10623 Berlin Germany Fax 49 30 31421122 Tel 49 30 31421419 E-mail Hildebrandt@chem.tu-berlin.de Received 23 November 2010 revised 21 January 2011 accepted 22 February 2011 doi 10.1111 j.1742-4658.2011.08064.x Most of the biochemical and biophysical processes of proteins take place at membranes and are thus under the influence of strong local electric fields which are likely to affect the structure as well as the reaction mechanism and dynamics. To analyse such electric field effects biomimetic interfaces may be employed that consist of membrane models deposited on nanostructured metal electrodes. For such devices surface-enhanced resonance Raman and IR absorption spectroscopy are powerful techniques to disentangle the complex interfacial processes of proteins in terms of rotational diffusion electron transfer and protein and cofactor structural changes. The present article reviews the results obtained for the haem protein cytochrome c which is widely .
