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@ARTICLE{Haker:28482,
      author       = {Haker, A. and Hendriks, J. and van Stokkum, I. H. M. and
                      Heberle, J. and Hellingwerf, K. J. and Crielaard, W. and
                      Gensch, T.},
      title        = {{T}he two photocycles of photoactive yellow protein from
                      {R}hodobacter sphaeroides},
      journal      = {The journal of biological chemistry},
      volume       = {278},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PreJuSER-28482},
      pages        = {8442 - 8451},
      year         = {2003},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The absorption spectrum of the photoactive yellow protein
                      from Rhodobacter sphaeroides (R-PYP) shows two maxima,
                      absorbing at 360 nm (R-PYP(360)) and 446 nm (R-PYP(446)),
                      respectively. Both forms are photoactive and part of a
                      temperature- and pH-dependent equilibrium (Haker, A.,
                      Hendriks, J., Gensch, T., Hellingwerf, K. J., and Crielaard,
                      W. (2000) FEBS Lett. 486, 52-56). At 20 degrees C, for PYP
                      characteristic, the 446-nm absorbance band displays a
                      photocycle, in which the depletion of the 446-nm ground
                      state absorption occurs in at least three phases, with time
                      constants of <30 ns, 0.5 micros, and 17 micros.
                      Intermediates with both blue- and red-shifted absorption
                      maxima are transiently formed, before a blue-shifted
                      intermediate (pB(360), lambda(max) = 360 nm) is established.
                      The photocycle is completed with a monophasic recovery of
                      the ground state with a time constant of 2.5 ms. At 7
                      degrees C these photocycle transitions are slowed down 2- to
                      3-fold. Upon excitation of R-PYP(360) with a UV-flash (330
                      +/- 50 nm) a species with a difference absorption maximum at
                      approximately 435 nm is observed that returns to R-PYP(360)
                      on a minute time scale. Recovery can be accelerated by a
                      blue light flash (450 nm). R-PYP(360) and R-PYP(446) differ
                      in their overall protein conformation, as well as in the
                      isomerization and protonation state of the chromophore, as
                      determined with the fluorescent polarity probe Nile Red and
                      Fourier Transform Infrared spectroscopy, respectively.},
      keywords     = {Bacterial Proteins: chemistry / Bacterial Proteins:
                      physiology / Models, Molecular / Photoreceptors, Microbial:
                      chemistry / Photoreceptors, Microbial: physiology /
                      Photosynthesis / Protein Conformation / Rhodobacter
                      sphaeroides: physiology / Spectrometry, Fluorescence /
                      Spectroscopy, Fourier Transform Infrared / Bacterial
                      Proteins (NLM Chemicals) / Photoreceptors, Microbial (NLM
                      Chemicals) / photoactive yellow protein, Bacteria (NLM
                      Chemicals) / J (WoSType)},
      cin          = {IBI-1 / IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB57 / I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:12496261},
      UT           = {WOS:000181466800091},
      doi          = {10.1074/jbc.M209343200},
      url          = {https://juser.fz-juelich.de/record/28482},
}