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@PHDTHESIS{Bolwien:35970,
      author       = {Bolwien, Carsten},
      title        = {{Z}eitauflösende {S}chwingungsspektroskopie an
                      {B}acteriorhodopsin und {H}alorhodopsin},
      volume       = {3945},
      issn         = {0944-2952},
      school       = {Univ. Düsseldorf},
      type         = {Dr. (Univ.)},
      address      = {Jülich},
      publisher    = {Forschungszentrum Jülch GmbH Zentralbibliothek, Verlag},
      reportid     = {PreJuSER-35970, Juel-3945},
      series       = {Berichte des Forschungszentrums Jülich},
      pages        = {II, 125 p.},
      year         = {2002},
      note         = {Record converted from VDB: 12.11.2012; Düsseldorf, Univ.,
                      Diss., 2001},
      abstract     = {The Proteins Bacteriorhodopsin (BR) and Halorhodopsin (HR)
                      can be found in the cell membrane of the halophilic
                      archaebacterium Halobacterium salinarum. Under extreme
                      circumstances, BR as a light-driven proton pump provides an
                      alternative to the respiratory chain in order to establish a
                      proton gradient. HR as a light-driven chloride pump is used
                      to maintain the Chloride concentration in the cytoplasm
                      under varying conditions. The previously published ground
                      state x-ray structures of both Proteins-in the case of BR
                      additional structures of photocycle intermediates are
                      known-form an important basis for the understanding of the
                      functional mechanism, although they fail to provide a
                      dynamic picture of the process. However, this picture is
                      provided by time-resolving vibrational spectroscopy, which
                      is able to detect transient changes in the structure of the
                      Proteins. Fourier-Transform Infrared (FTIR)-spectroscopy on
                      BR with polarized measuring light presents an additional
                      parameter, the linear dichroism, to tracé the structural
                      changes during the photocycle. These measurements are used
                      not only for improved separation of the photocycle
                      intermediates, but also to calculate orientations of
                      transition dipole moments and thereby of structural elements
                      . In addition, it is possible to resolve transient
                      protonations of amino acid side chains, an important part of
                      the mechanism of a proton pump and also invisible with the
                      x-ray technique . In contrast to BR not much is known about
                      the photocycle of the Chloride pump HR. In this work, the
                      influence of the Chloride concentration on the kinetics is
                      investigated with time-resolving FTIR-spectroscopy. The use
                      of the attenuated total reflection ATR-technique, here with
                      a new diamond ATR cell, allows reproducible adjustment of
                      the sait concentration in infrared experiments in the range
                      between 0 to 5 mol/L. An alternative photocycle model has
                      been formulated based on the respective influence on the
                      formation and decay of the intermediates . Resonance Raman
                      measurements on both proteins give additional information on
                      the assignment of vibrational modes and demonstrate the
                      potential of the spectroscopic setup as a
                      micro-Raman-spectrometer for the investigation of protein
                      crystals .},
      cin          = {IBI-2},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Biologische Strukturforschung},
      pid          = {G:(DE-Juel1)FUEK96},
      typ          = {PUB:(DE-HGF)11 / PUB:(DE-HGF)3},
      url          = {https://juser.fz-juelich.de/record/35970},
}