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@ARTICLE{Habuchi:46162,
      author       = {Habuchi, S. and Cotlet, M. and Gensch, T. and Bednarz, T.
                      and Haber-Pohlmeier, S. and Rozenski, J. and Dirix, G. and
                      Michiels, J. and Vanderleyden, J. and Heberle, J. and de
                      Schryver, F. C. and Hofkens, J.},
      title        = {{E}vidence for the isomerization and decarboxylation in the
                      photoconversion of the red fluorescent protein {D}s{R}ed},
      journal      = {Journal of the American Chemical Society},
      volume       = {127},
      issn         = {0002-7863},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-46162},
      pages        = {8977 - 8984},
      year         = {2005},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Recently, it has been shown that the red fluorescent
                      protein DsRed undergoes photoconversion on intense
                      irradiation, but the mechanism of the conversion has not yet
                      been elucidated. Upon irradiation with a nanosecond-pulsed
                      laser at 532 nm, the chromophore of DsRed absorbing at 559
                      nm and emitting at 583 nm (R form) converts into a super red
                      (SR) form absorbing at 574 nm and emitting at 595 nm. This
                      conversion leads to a significant change in the fluorescence
                      quantum yield from 0.7 to 0.01. Here we demonstrate that the
                      photoconversion is the result of structural changes of the
                      chromophore and one amino acid. Absorption, fluorescence,
                      and vibrational spectroscopy as well as mass spectrometry
                      suggest that a cis-to-trans isomerization of the chromophore
                      and decarboxylation of a glutamate (E215) take place upon
                      irradiation to form SR. At the same time, another
                      photoproduct (B) with an absorption maximum at 386 nm
                      appears upon irradiation. This species is assigned as a
                      protonated form of the DsRed chromophore. It might be a
                      mixture of several protonated DsRed forms as there is at
                      least two ways of formation. Furthermore, the
                      photoconversion of DsRed is proven to occur through a
                      consecutive two-photon absorption process. Our results
                      demonstrate the importance of the chromophore conformation
                      in the ground state on the brightness of the protein as well
                      as the importance of the photon flux to control/avoid the
                      photoconversion process.},
      keywords     = {Decarboxylation / Isomerism / Lasers / Luminescent
                      Proteins: chemistry / Luminescent Proteins: radiation
                      effects / Molecular Structure / Photolysis / Time Factors /
                      Luminescent Proteins (NLM Chemicals) / fluorescent protein
                      583 (NLM Chemicals) / J (WoSType)},
      cin          = {IBI-1 / IBI-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB57 / I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Chemistry, Multidisciplinary},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:15969574},
      UT           = {WOS:000230010600037},
      doi          = {10.1021/ja047023o},
      url          = {https://juser.fz-juelich.de/record/46162},
}