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@ARTICLE{Ataka:26839,
      author       = {Ataka, K. and Hegemann, P. and Heberle, J.},
      title        = {{V}ibrational spectroscopy of an {A}lgal {P}hot-{LOV}1
                      domain probes the molecular changes associated with
                      blue-light reception},
      journal      = {Biophysical journal},
      volume       = {84},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PreJuSER-26839},
      pages        = {466 - 474},
      year         = {2003},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The LOV1 domain of the blue light Phot1-receptor
                      (phototropin homolog) from Chlamydomonas reinhardtii has
                      been studied by vibrational spectroscopy. The FMN modes of
                      the dark state of LOV1 were identified by preresonance Raman
                      spectroscopy and assigned to molecular vibrations. By
                      comparing the blue-light-induced FTIR difference spectrum,
                      with the preresonance Raman spectrum, most of the
                      differences are due to FMN modes. Thus, we exclude large
                      backbone changes, of the protein that might occur during the
                      phototransformation of the dark state LOV1-447 into the
                      putative signaling state LOV1-390. Still, the presence of
                      smaller amide difference bands cannot be excluded but may be
                      masked by overlapping FMN modes. The band at 2567 cm(-1) is
                      assigned to the S-H stretching vibration of C57, the residue
                      that forms the transient thio-adduct with, the chromophore
                      FMN. The occurrence of this band is evidence that C57 is
                      protonated in the dark state of LOV1. This result challenges
                      conclusions from the homologous LOV2 domain from oat that
                      the thiolate of the corresponding cysteine is the, reactive
                      species.},
      keywords     = {J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000183067300040},
      doi          = {10.1016/S0006-3495(03)74866-8},
      url          = {https://juser.fz-juelich.de/record/26839},
}