% 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{Guo:49345,
      author       = {Guo, H. and Kottke, T. and Hegemann, P. and Dick, B.},
      title        = {{T}he {P}hot {LOLV}2 {D}omain and its {I}nteraction with
                      {LOV}1},
      journal      = {Biophysical journal},
      volume       = {89},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PreJuSER-49345},
      pages        = {402 - 412},
      year         = {2005},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Phot proteins are homologs of the blue-light receptor
                      phototropin. We report a comparative study of the
                      photocycles of the isolated, light-sensitive domains LOV1
                      and LOV2 from Chlamydomonas reinhardtii phot protein, as
                      well as the construct LOV1/2 containing both domains.
                      Transient absorption measurements revealed a short lifetime
                      of the LOV2-wt triplet state (500 ns), but a long lifetime
                      (287 micros) of the triplet in the mutant LOV2-C250S, in
                      which the reactive cysteine is replaced by serine. For LOV1,
                      in comparison, corresponding numbers of 800 ns and 4 micros
                      for the two conformers in LOV1-wt, and 27 micros for
                      LOV1-C57S have been reported. The triplet decay kinetics in
                      the mixed domains LOV1/2-wt, LOV1/2-C57S, and LOV1/2-C250S
                      can be analyzed as the superposition of the behavior of the
                      corresponding single domains. The situation is different for
                      the slow, thermal reaction of the photoadduct back to the
                      dark form. Whereas the individual domains LOV1 and LOV2 show
                      two decay components, the double domains LOV1/2-C57S and
                      LOV1/2-C250S both show only a single component. The
                      interaction of the two domains does therefore not manifest
                      itself during the lifetime of the triplet states, but
                      changes the decay behavior of the adduct states.},
      keywords     = {Animals / Anions / Cations / Chlamydomonas reinhardtii:
                      metabolism / Cryptochromes / Cysteine: chemistry / DNA
                      Adducts / Flavoproteins: chemistry / Hot Temperature /
                      Hydrogen-Ion Concentration / Ions / Kinetics / Light /
                      Models, Chemical / Mutation / Photons / Photoreceptor Cells,
                      Invertebrate: chemistry / Protein Binding / Protein
                      Structure, Tertiary / Serine: chemistry / Sodium Chloride:
                      pharmacology / Spectrophotometry / Temperature / Time
                      Factors / Anions (NLM Chemicals) / Cations (NLM Chemicals) /
                      Cryptochromes (NLM Chemicals) / DNA Adducts (NLM Chemicals)
                      / Flavoproteins (NLM Chemicals) / Ions (NLM Chemicals) /
                      Cysteine (NLM Chemicals) / Serine (NLM Chemicals) / Sodium
                      Chloride (NLM Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:15879473},
      pmc          = {pmc:PMC1366540},
      UT           = {WOS:000230114500043},
      doi          = {10.1529/biophysj.104.058230},
      url          = {https://juser.fz-juelich.de/record/49345},
}