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@ARTICLE{Bednarz:38378,
      author       = {Bednarz, T. and Losi, A. and Gärtner, W. and Hegemann, P.
                      and Heberle, J.},
      title        = {{F}unctional variations among {LOV} domains as revealed by
                      {FTIR} difference spectroscopy},
      journal      = {Photochemical $\&$ photobiological sciences},
      volume       = {3},
      issn         = {1474-905X},
      address      = {Cambridge},
      publisher    = {Royal Society of Chemistry},
      reportid     = {PreJuSER-38378},
      pages        = {575 - 579},
      year         = {2004},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The two LOV domains, LOV1 and LOV2, from Chlamydomonas
                      reinhardtii were investigated by light-induced FT-IR
                      difference spectroscopy and compared to the LOV domain of
                      Bacillus subtilis (YtvA-LOV). It is shown that the two S-H
                      conformations of the reactive LOV1 cysteine C57(1) are
                      exposed to environments of different hydrogen bonding
                      strength. Thus, the two rotamer configurations of C57 might
                      be related to the fact that the triplet state decays
                      bi-exponentially into the LOV1-390 photoproduct. Exchange of
                      the two other cysteines of LOV1 (C32S and C83S) does not
                      alter the S-H stretching band providing evidence that this
                      band feature arises solely from C57. The reactive cysteine
                      of LOV2 from Chlamydomonas reinhardtii (C250) and of
                      YtvA-LOV (C62) exhibit both a homogenous S-H stretching
                      vibrational band which suggests a single conformer of the
                      amino acid side chain. Finally, the FT-IR difference
                      spectrum of YtvA from Bacillus subtilis comprising the light
                      absorbing LOV domain and the putative signaling STAS
                      (sulfate transporter/antisigma-factor antagonist) domain,
                      reveals conformational changes in the latter after
                      blue-light excitation.},
      keywords     = {Animals / Bacillus subtilis: physiology / Bacillus
                      subtilis: radiation effects / Bacterial Proteins: chemistry
                      / Bacterial Proteins: genetics / Bacterial Proteins:
                      physiology / Chlamydomonas reinhardtii: physiology /
                      Chlamydomonas reinhardtii: radiation effects /
                      Crystallography, X-Ray / Protein Conformation /
                      Spectrometry, Fluorescence / Spectroscopy, Fourier Transform
                      Infrared: methods / Bacterial Proteins (NLM Chemicals) / J
                      (WoSType)},
      cin          = {IBI-2},
      ddc          = {620},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics /
                      Chemistry, Physical},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:15170487},
      UT           = {WOS:000221746800012},
      doi          = {10.1039/b400976b},
      url          = {https://juser.fz-juelich.de/record/38378},
}