% 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{Rllen:850884,
      author       = {Röllen, Katrin and Granzin, Joachim and Batra-Safferling,
                      Renu and Stadler, Andreas Maximilian},
      title        = {{S}mall-angle {X}-ray scattering study of the kinetics of
                      light-dark transition in a {LOV} protein},
      journal      = {PLoS one},
      volume       = {13},
      number       = {7},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2018-04635},
      pages        = {e0200746},
      year         = {2018},
      abstract     = {Light, oxygen, voltage (LOV) photoreceptors consist of
                      conserved photo-responsive domains in bacteria, archaea,
                      plants and fungi, and detect blue-light via a flavin
                      cofactor. We investigated the blue-light induced
                      conformational transition of the dimeric photoreceptor
                      PpSB1-LOV-R66I from Pseudomonas putida in solution by using
                      small-angle X-ray scattering (SAXS). SAXS experiments of the
                      fully populated light- and dark-states under steady-state
                      conditions revealed significant structural differences
                      between the two states that are in agreement with the known
                      structures determined by crystallography. We followed the
                      transition from the light- to the dark-state by using SAXS
                      measurements in real-time. A two-state model based on the
                      light- and dark-state conformations could describe the
                      measured time-course SAXS data with a relaxation time τREC
                      of ~ 34 to 35 min being larger than the recovery time found
                      with UV/vis spectroscopy. Unlike the flavin
                      chromophore-based UV/vis method that is sensitive to the
                      local chromophore environment in flavoproteins, SAXS-based
                      assay depends on protein conformational changes and provides
                      with an alternative to measure the recovery kinetics.},
      cin          = {ICS-6 / Neutronenstreuung ; JCNS-1 / ICS-1},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)ICS-1-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30011332},
      UT           = {WOS:000438829800048},
      doi          = {10.1371/journal.pone.0200746},
      url          = {https://juser.fz-juelich.de/record/850884},
}