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000041691 084__ $$2WoS$$aChemistry, Multidisciplinary
000041691 1001_ $$0P:(DE-Juel1)VDB5396$$aAtaka, K.$$b0$$uFZJ
000041691 245__ $$aFunctional vibrational spectroscopy of a cytochrome c monolayer: SEIDAS probes the interaction with different surface modified electrodes
000041691 260__ $$aWashington, DC$$bAmerican Chemical Society$$c2004
000041691 300__ $$a9445 - 9457
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000041691 440_0 $$08502$$aJournal of the American Chemical Society$$v126$$x0002-7863
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000041691 520__ $$aElectrochemically induced infrared difference spectra of cytochrome c on various chemically modified electrodes (CMEs) are recorded by exploiting the surface-enhancement exerted by a granular gold film. We have recently developed surface-enhanced infrared difference absorption spectroscopy (SEIDAS), which provides acute sensitivity to observe the minute enzymatic change of a protein on the level of a monolayer. By these means, we demonstrate that the relative band intensities in the potential-induced difference spectra of adsorbed cytochrome c are significantly dependent on the type of CME used (mercaptopropionic acid, mercaptoethanol, 4,4'-dithiodipyridine, or L-cysteine). These differences are attributed to the altered interaction of cytochrome c with the headgroup of the various CMEs leading to variations in surface orientation and relative distance from the surface. Nevertheless, the peak positions of the observed bands are identical among the CMEs employed. This implies that the internal conformational changes induced by the redox reaction of the adsorbed cytochrome c are not disturbed by the interaction with the CME and that full functionality of the protein is retained. Finally, we critically discuss our results within the framework of the different models for cytochrome c adsorption on CMEs.
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000041691 650_2 $$2MeSH$$aCrystallography, X-Ray
000041691 650_2 $$2MeSH$$aCytochromes c: chemistry
000041691 650_2 $$2MeSH$$aElectrochemistry: instrumentation
000041691 650_2 $$2MeSH$$aElectrochemistry: methods
000041691 650_2 $$2MeSH$$aElectrodes
000041691 650_2 $$2MeSH$$aGold: chemistry
000041691 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular
000041691 650_2 $$2MeSH$$aOxidation-Reduction
000041691 650_2 $$2MeSH$$aSpectroscopy, Fourier Transform Infrared: instrumentation
000041691 650_2 $$2MeSH$$aSpectroscopy, Fourier Transform Infrared: methods
000041691 650_7 $$07440-57-5$$2NLM Chemicals$$aGold
000041691 650_7 $$09007-43-6$$2NLM Chemicals$$aCytochromes c
000041691 650_7 $$2WoSType$$aJ
000041691 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b1$$uFZJ
000041691 773__ $$0PERI:(DE-600)1472210-0$$a10.1021/ja048346n$$gVol. 126, p. 9445 - 9457$$p9445 - 9457$$q126<9445 - 9457$$tJournal of the American Chemical Society$$v126$$x0002-7863$$y2004
000041691 8567_ $$uhttp://hdl.handle.net/2128/698$$uhttp://dx.doi.org/10.1021/ja048346n
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