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@ARTICLE{Ataka:41691,
      author       = {Ataka, K. and Heberle, J.},
      title        = {{F}unctional vibrational spectroscopy of a cytochrome c
                      monolayer: {SEIDAS} probes the interaction with different
                      surface modified electrodes},
      journal      = {Journal of the American Chemical Society},
      volume       = {126},
      issn         = {0002-7863},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-41691},
      pages        = {9445 - 9457},
      year         = {2004},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Electrochemically 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.},
      keywords     = {Crystallography, X-Ray / Cytochromes c: chemistry /
                      Electrochemistry: instrumentation / Electrochemistry:
                      methods / Electrodes / Gold: chemistry / Nuclear Magnetic
                      Resonance, Biomolecular / Oxidation-Reduction /
                      Spectroscopy, Fourier Transform Infrared: instrumentation /
                      Spectroscopy, Fourier Transform Infrared: methods / Gold
                      (NLM Chemicals) / Cytochromes c (NLM Chemicals) / J
                      (WoSType)},
      cin          = {IBI-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Chemistry, Multidisciplinary},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:15281838},
      UT           = {WOS:000222950900057},
      doi          = {10.1021/ja048346n},
      url          = {https://juser.fz-juelich.de/record/41691},
}