% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Berndt:59166,
      author       = {Berndt, A. and Kottke, T. and Breitkreuz, H. and Dvorsky,
                      R. and Hennig, S. and Alexander, M. and Wolf, E.},
      title        = {{A} {N}ovel {P}hotoreaction {M}echanism for the {C}ircadian
                      {B}lue {L}ight {P}hotoreceptor {D}rosophila {C}ryptochrome},
      journal      = {The journal of biological chemistry},
      volume       = {282},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PreJuSER-59166},
      pages        = {13011 - 13021},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Cryptochromes are flavoproteins that are evolutionary
                      related to the DNA photolyases but lack DNA repair activity.
                      Drosophila cryptochrome (dCRY) is a blue light photoreceptor
                      that is involved in the synchronization of the circadian
                      clock with the environmental light-dark cycle. Until now,
                      spectroscopic and structural studies on this and other
                      animal cryptochromes have largely been hampered by
                      difficulties in their recombinant expression. We have
                      therefore established an expression and purification scheme
                      that enables us to purify mg amounts of monomeric dCRY from
                      Sf21 insect cell cultures. Using UV-visible spectroscopy,
                      mass spectrometry, and reversed phase high pressure liquid
                      chromatography, we show that insect cell-purified dCRY
                      contains flavin adenine dinucleotide in its oxidized state
                      (FAD(ox)) and residual amounts of methenyltetrahydrofolate.
                      Upon blue light irradiation, dCRY undergoes a reversible
                      absorption change, which is assigned to the conversion of
                      FAD(ox) to the red anionic FAD(.) radical. Our findings lead
                      us to propose a novel photoreaction mechanism for dCRY, in
                      which FAD(ox) corresponds to the ground state, whereas the
                      FAD(.) radical represents the light-activated state that
                      mediates resetting of the Drosophila circadian clock.},
      keywords     = {Animals / Cell Line / Circadian Rhythm / Cryptochromes /
                      DNA Repair / Deoxyribodipyrimidine Photo-Lyase: chemistry /
                      Drosophila: chemistry / Drosophila: metabolism / Drosophila
                      Proteins: chemistry / Drosophila Proteins: metabolism /
                      Flavin-Adenine Dinucleotide: chemistry / Flavin-Adenine
                      Dinucleotide: metabolism / Flavoproteins: chemistry /
                      Flavoproteins: metabolism / Oxidation-Reduction /
                      Photochemistry / Photoreceptor Cells, Invertebrate:
                      chemistry / Photoreceptor Cells, Invertebrate: metabolism /
                      Cryptochromes (NLM Chemicals) / Drosophila Proteins (NLM
                      Chemicals) / Flavoproteins (NLM Chemicals) / Flavin-Adenine
                      Dinucleotide (NLM Chemicals) / Deoxyribodipyrimidine
                      Photo-Lyase (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:17298948},
      UT           = {WOS:000245942800071},
      doi          = {10.1074/jbc.M608872200},
      url          = {https://juser.fz-juelich.de/record/59166},
}