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@ARTICLE{Majerus:3640,
      author       = {Majerus, T. and Kottke, T.},
      title        = {{T}ime-{R}esolved {F}ourier {T}ransform {I}nfrared {S}tudy
                      on {P}hotoadduct {F}ormation and {S}econdary {S}tructural
                      {C}hanges within the {P}hototropin {LOV} {D}omain},
      journal      = {Biophysical journal},
      volume       = {96},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PreJuSER-3640},
      pages        = {1462 - 1470},
      year         = {2009},
      note         = {This work was Supported by the Helmholtz Genicinschaft
                      (grant VHNG-014) and Deutsche Forschungsgemeinschaft (grant
                      FOR 526).},
      abstract     = {Phototropins are plant blue-light photoreceptors containing
                      two light-, oxygen-, or voltage-sensitive (LOV) domains and
                      a C-terminal kinase domain. The two LOV domains bind
                      noncovalently flavin mononucleotide as a chromophore. We
                      investigated the photocycle of fast-recovery mutant
                      LOV2-I403V from Arabidopsis phototropin 2 by step-scan
                      Fourier transform infrared spectroscopy. The reaction of the
                      triplet excited state of flavin with cysteine takes place
                      with a time constant of 3 micros to yield the covalent
                      adduct. Our data provide evidence that the flavin is
                      unprotonated in the productive triplet state, disfavoring an
                      ionic mechanism of bond formation. An intermediate adduct
                      species was evident that displayed changes in secondary
                      structure in the helix or loop region, and relaxed with a
                      time constant of 120 micros. In milliseconds, the final
                      adduct state is formed by further alterations of secondary
                      structure, including beta-sheets. A comparison with
                      wild-type adduct spectra shows that the mutation does not
                      interfere with the functionality of the domain. All signals
                      originate from within the LOV domain, because the construct
                      does not comprise the adjacent Jalpha helix required for
                      signal transduction. The contribution of early and late
                      adduct intermediates to signal transfer to the Jalpha helix
                      outside of the domain is discussed.},
      keywords     = {Arabidopsis: chemistry / Arabidopsis Proteins /
                      Cryptochromes / Cysteine: chemistry / Flavoproteins:
                      chemistry / Flavoproteins: genetics / Kinetics / Lasers /
                      Light / Models, Molecular / Mutation / Protein Structure,
                      Secondary / Protein Structure, Tertiary / Spectroscopy,
                      Fourier Transform Infrared / Arabidopsis Proteins (NLM
                      Chemicals) / CRY1 protein, Arabidopsis (NLM Chemicals) /
                      Cryptochromes (NLM Chemicals) / Flavoproteins (NLM
                      Chemicals) / Cysteine (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ISB-2-20090406},
      pnm          = {ohne FE},
      pid          = {G:(DE-Juel1)FUEK307},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19217862},
      pmc          = {pmc:PMC2717236},
      UT           = {WOS:000266377800021},
      doi          = {10.1016/j.bpj.2008.11.016},
      url          = {https://juser.fz-juelich.de/record/3640},
}