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@ARTICLE{Immeln:59358,
      author       = {Immeln, D. and Schlesinger, R. and Heberle, J. and Kottke,
                      T.},
      title        = {{B}lue {L}ight {I}nduces {R}adical {F}ormation and
                      {A}utophosphorylation in the {L}ight-sensitive {D}omain of
                      {C}hlamydomonas {C}ryptochrome},
      journal      = {The journal of biological chemistry},
      volume       = {282},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PreJuSER-59358},
      pages        = {21720 - 21728},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Cryptochromes are sensory blue light receptors mediating
                      various responses in plants and animals. Studies on the
                      mechanism of plant cryptochromes have been focused on the
                      flowering plant Arabidopsis. In the genome of the
                      unicellular green alga Chlamydomonas reinhardtii, a single
                      plant cryptochrome, Chlamydomonas photolyase homologue 1
                      (CPH1), has been identified. The N-terminal 500 amino acids
                      comprise the light-sensitive domain of CPH1 linked to a
                      C-terminal extension of similar size. We have expressed the
                      light-sensitive domain heterologously in Escherichia coli in
                      high yield and purity. The 59-kDa protein bears exclusively
                      flavin adenine dinucleotide in its oxidized state.
                      Illumination with blue light induces formation of a neutral
                      flavin radical with absorption maxima at 540 and 580 nm. The
                      reaction proceeds aerobically even in the absence of an
                      exogenous electron donor, which suggests that it reflects a
                      physiological response. The process is completely reversible
                      in the dark and exhibits a decay time constant of 200 s in
                      the presence of oxygen. Binding of ATP strongly stabilizes
                      the radical state after illumination and impedes the dark
                      recovery. Thus, ATP binding has functional significance for
                      plant cryptochromes and does not merely result from
                      structural homology to DNA photolyase. The light-sensitive
                      domain responds to illumination by an increase in
                      phosphorylation. The autophosphorylation takes place
                      although the protein is lacking its native C-terminal
                      extension. This finding indicates that the extension is
                      dispensable for autophosphorylation, despite the role it has
                      been assigned in mediating signal transduction in
                      Arabidopsis.},
      keywords     = {Animals / Chlamydomonas: physiology / Chlamydomonas:
                      radiation effects / Cryptochromes / DNA, Protozoan: genetics
                      / DNA, Protozoan: isolation $\&$ purification / Escherichia
                      coli: genetics / Flavoproteins: genetics / Flavoproteins:
                      metabolism / Flavoproteins: radiation effects / Free
                      Radicals / Kinetics / Light / Light Signal Transduction /
                      Phosphorylation / Protozoan Proteins: metabolism / Protozoan
                      Proteins: radiation effects / Recombinant Proteins:
                      metabolism / Recombinant Proteins: radiation effects /
                      Cryptochromes (NLM Chemicals) / DNA, Protozoan (NLM
                      Chemicals) / Flavoproteins (NLM Chemicals) / Free Radicals
                      (NLM Chemicals) / Protozoan Proteins (NLM Chemicals) /
                      Recombinant Proteins (NLM Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17548357},
      UT           = {WOS:000248196800019},
      doi          = {10.1074/jbc.M700849200},
      url          = {https://juser.fz-juelich.de/record/59358},
}