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@ARTICLE{Jiang:588,
      author       = {Jiang, X. and Zaitseva, E. and Schmidt, M. and Siebert, F.
                      and Engelhard, M. and Schlesinger, R. and Ataka, K. and
                      Vogel, R. and Heberle, J.},
      title        = {{R}esolving voltage-dependent structural changes of a
                      membrane photoreceptor by surface-enhanced {IR} difference
                      spectroscopy},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {105},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {Academy},
      reportid     = {PreJuSER-588},
      pages        = {12113 - 12117},
      year         = {2008},
      note         = {We thank Rebecca M. Nyquist for reading the manuscript;
                      R.S. thanks Georg Buldt for generous support; and J.H.
                      acknowledges helpful discussions with Eberhard Neumann and
                      Benjamin Kaupp. This work was supported by grants from the
                      German Ministry for Science and Education (to J.H.) and
                      Deutsche Forschungsgemeinschaft Grant Vo 811/3,4 (to R.V.)
                      and Za 566/1-1 (to E.Z.). X.J. thanks the
                      Alexander-von-Humboldt foundation for a fellowship.},
      abstract     = {Membrane proteins are molecular machines that transport
                      ions, solutes, or information across the cell membrane.
                      Electrophysiological techniques have unraveled many
                      functional aspects of ion channels but suffer from the lack
                      of structural sensitivity. Here, we present
                      spectroelectrochemical data on vibrational changes of
                      membrane proteins derived from a single monolayer. For the
                      seven-helical transmembrane protein sensory rhodopsin II,
                      structural changes of the protein backbone and the retinal
                      cofactor as well as single ion transfer events are resolved
                      by surface-enhanced IR difference absorption spectroscopy
                      (SEIDAS). Angular changes of bonds versus the membrane
                      normal have been determined because SEIDAS monitors only
                      those vibrations whose dipole moment are oriented
                      perpendicular to the solid surface. The application of
                      negative membrane potentials (DeltaV = -0.3 V) leads to the
                      selective halt of the light-induced proton transfer at the
                      stage of D75, the counter ion of the retinal Schiff base. It
                      is inferred that the voltage raises the energy barrier of
                      this particular proton-transfer reaction, rendering the
                      energy deposited in the retinal by light excitation
                      insufficient for charge transfer to occur. The other
                      structural rearrangements that accompany light-induced
                      activity of the membrane protein, are essentially unaffected
                      by the transmembrane electric field. Our results demonstrate
                      that SEIDAS is a generic approach to study processes that
                      depend on the membrane potential, like those in
                      voltage-gated ion channels and transporters, to elucidate
                      the mechanism of ion transfer with unprecedented spatial
                      sensitivity and temporal resolution.},
      keywords     = {Ion Channel Gating / Light / Membrane Potentials / Membrane
                      Proteins: chemistry / Photoreceptor Cells: chemistry /
                      Protein Conformation / Rhodopsin: chemistry /
                      Spectrophotometry, Infrared: methods / Membrane Proteins
                      (NLM Chemicals) / Rhodopsin (NLM Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {000},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Multidisciplinary Sciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18719097},
      pmc          = {pmc:PMC2527874},
      UT           = {WOS:000258905700005},
      doi          = {10.1073/pnas.0802289105},
      url          = {https://juser.fz-juelich.de/record/588},
}