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@ARTICLE{Laan:41922,
      author       = {Laan, W. and Bednarz, T. and Heberle, J. and Hellingwerf,
                      K.},
      title        = {{C}hromophore composition of a heterologously expressed
                      {BLUF}-domain},
      journal      = {Photochemical $\&$ photobiological sciences},
      volume       = {3},
      issn         = {1474-905X},
      address      = {Cambridge},
      publisher    = {Royal Society of Chemistry},
      reportid     = {PreJuSER-41922},
      pages        = {1011 - 1016},
      year         = {2004},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Upon heterologous expression of the BLUF (for: Blue-Light
                      sensing Using Flavin) domain from AppA, a transcriptional
                      anti-repressor from Rhodobacter sphaeroides, in Escherichia
                      coli, photoactive holo-protein is formed through
                      non-covalent binding of a flavin. Whereas it is generally
                      assumed that FAD is the physiological chromophore of this
                      photo-perception domain in vivo, E. coli can (and does)
                      insert, depending on the growth conditions, all naturally
                      occurring flavins, i.e. riboflavin, FMN and FAD into this
                      protein domain. The nature of the particular flavin bound
                      affects the photochemical- and particularly the fluorescence
                      properties of the N-terminal domain of this photosensory
                      protein.},
      keywords     = {Bacterial Proteins: chemistry / Bacterial Proteins:
                      genetics / Bacterial Proteins: radiation effects / Cloning,
                      Molecular / Escherichia coli / Flavoproteins: chemistry /
                      Flavoproteins: genetics / Flavoproteins: radiation effects /
                      Light / Recombinant Proteins: chemistry / Recombinant
                      Proteins: radiation effects / Rhodobacter sphaeroides /
                      Spectrometry, Fluorescence / Spectroscopy, Fourier Transform
                      Infrared / AppA protein, Rhodobacter sphaeroides (NLM
                      Chemicals) / Bacterial Proteins (NLM Chemicals) /
                      Flavoproteins (NLM Chemicals) / Recombinant 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:15570388},
      UT           = {WOS:000225406800006},
      doi          = {10.1039/b410923f},
      url          = {https://juser.fz-juelich.de/record/41922},
}