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@ARTICLE{Efremov:52270,
      author       = {Efremov, R. and Gordeliy, V. I. and Heberle, J. and Büldt,
                      G.},
      title        = {{T}ime-resolved microscopy on a single crystal of
                      bacteriorhodopsin reveals lattice induced differences in the
                      photocycle kinetics},
      journal      = {Biophysical journal},
      volume       = {91},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PreJuSER-52270},
      pages        = {1441 - 1451},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The determination of the intermediate state structures of
                      the bacteriorhodopsin photocycle has lead to an
                      unprecedented level of understanding of the catalytic
                      process exerted by a membrane protein. However, the
                      crystallographic structures of the intermediate states are
                      only relevant if the working cycle is not impaired by the
                      crystal lattice. Therefore, we applied visible and Fourier
                      transform infrared spectroscopy (FTIR) microspectroscopy
                      with microsecond time resolution to compare the
                      photoreaction of a single bacteriorhodopsin crystal to that
                      of bacteriorhodopsin residing in the native purple membrane.
                      The analysis of the FTIR difference spectra of the resolved
                      intermediate states reveals great similarity in structural
                      changes taking place in the crystal and in PM. However, the
                      kinetics of the photocycle are significantly altered in the
                      three-dimensional crystal as compared to PM. Strikingly, the
                      L state decay is accelerated in the crystal, whereas the M
                      decay is delayed. The physical origin of this deviation and
                      the implications for trapping of intermediate states are
                      discussed. As a methodological advance, time-resolved
                      step-scan FTIR spectroscopy on a single protein crystal is
                      demonstrated for the first time which may be used in the
                      future to gauge the functionality of other crystallized
                      proteins with the molecular resolution of vibrational
                      spectroscopy.},
      keywords     = {Bacteriorhodopsins: chemistry / Bacteriorhodopsins:
                      radiation effects / Bacteriorhodopsins: ultrastructure /
                      Crystallography: methods / Dose-Response Relationship,
                      Radiation / Kinetics / Light / Photobiology: methods /
                      Photochemistry: methods / Radiation Dosage / Spectroscopy,
                      Fourier Transform Infrared: methods / Time Factors /
                      Bacteriorhodopsins (NLM Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16731567},
      pmc          = {pmc:PMC1518640},
      UT           = {WOS:000239242000029},
      doi          = {10.1529/biophysj.106.083345},
      url          = {https://juser.fz-juelich.de/record/52270},
}