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@ARTICLE{Kottke:51338,
      author       = {Kottke, T. and Ahmad, M. and Batschauer, A. and Heberle,
                      J.},
      title        = {{B}lue-{L}ight-{I}nduced {C}hanges in {A}rabidopsis
                      {C}ryptochrome 1 {P}robed by {FTIR} {D}ifference
                      {S}pectroscopy},
      journal      = {Biochemistry},
      volume       = {45},
      issn         = {0006-2960},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-51338},
      pages        = {2472 - 2479},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Cryptochromes are blue-light photoreceptors that regulate a
                      variety of responses in animals and plants, including
                      circadian entrainment in Drosophila and photomorphogenesis
                      in Arabidopsis. They comprise a photolyase homology region
                      (PHR) of about 500 amino acids and a C-terminal extension of
                      varying length. In the PHR domain, flavin adenine
                      dinucleotide (FAD) is noncovalently bound. The presence of a
                      second chromophore, such as methenyltetrahydrofolate, in
                      animal and plant cryptochromes is still under debate.
                      Arabidopsis cryptochrome 1 (CRY1) has been intensively
                      studied with regard to function and interaction of the
                      protein in vivo and in vitro. However, little is known about
                      the pathway from light absorption to signal transduction on
                      the molecular level. We investigated the full-length CRY1
                      protein by Fourier transform infrared (FTIR) and UV/vis
                      difference spectroscopy. Starting from the fully oxidized
                      state of the chromophore FAD, a neutral flavoprotein radical
                      is formed upon illumination in the absence of any exogenous
                      electron donor. A preliminary assignment of the chromophore
                      bands is presented. The FTIR difference spectrum reveals
                      only moderate changes in secondary structure of the
                      apoprotein in response to the photoreduction of the
                      chromophore. Deprotonation of an aspartic or glutamic acid,
                      probably D396, accompanies radical formation, as is deduced
                      from the negative band at 1734 cm(-)(1) in D(2)O. The main
                      positive band at 1524 cm(-)(1) in the FTIR spectrum shows a
                      strong shift to lower frequencies as compared to other
                      flavoproteins. Together with the unusual blue-shift of the
                      absorption in the visible range to 595 nm, this clearly
                      distinguishes the radical form of CRY1 from those of
                      structurally highly homologous DNA photolyases. As a
                      consequence, the direct comparison of cryptochrome to
                      photolyase in terms of photoreactivity and mechanism has to
                      be made with caution.},
      keywords     = {Arabidopsis Proteins: chemistry / Cryptochromes /
                      Crystallography, X-Ray / Deoxyribodipyrimidine Photo-Lyase:
                      chemistry / Deoxyribodipyrimidine Photo-Lyase: metabolism /
                      Escherichia coli: metabolism / Flavins: metabolism /
                      Flavoproteins: chemistry / Flavoproteins: metabolism / Light
                      / Models, Molecular / Signal Transduction: physiology /
                      Spectrophotometry, Ultraviolet / Spectroscopy, Fourier
                      Transform Infrared: methods / Structural Homology, Protein /
                      Arabidopsis Proteins (NLM Chemicals) / Cryptochromes (NLM
                      Chemicals) / Flavins (NLM Chemicals) / Flavoproteins (NLM
                      Chemicals) / Deoxyribodipyrimidine Photo-Lyase (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    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16489739},
      UT           = {WOS:000235792300002},
      doi          = {10.1021/bi051964b},
      url          = {https://juser.fz-juelich.de/record/51338},
}