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@ARTICLE{Smolentseva:905009,
      author       = {Smolentseva, Anastasia and Goncharov, Ivan M. and Yudenko,
                      Anna and Bogorodskiy, Andrey and Semenov, Oleg and
                      Nazarenko, Vera V. and Borshchevskiy, Valentin and Fonin,
                      Alexander V. and Remeeva, Alina and Jaeger, Karl-Erich and
                      Krauss, Ulrich and Gordeliy, Valentin and Gushchin, Ivan},
      title        = {{E}xtreme dependence of {C}hloroflexus aggregans {LOV}
                      domain thermo- and photostability on the bound flavin
                      species},
      journal      = {Photochemical $\&$ photobiological sciences},
      volume       = {20},
      number       = {12},
      issn         = {1474-905X},
      address      = {Cambridge},
      publisher    = {Royal Society of Chemistry},
      reportid     = {FZJ-2022-00320},
      pages        = {1645 - 1656},
      year         = {2021},
      abstract     = {Light-oxygen-voltage (LOV) domains are common photosensory
                      modules that found many applications in fluorescence
                      microscopy and optogenetics. Here, we show that the
                      Chloroflexus aggregans LOV domain can bind different flavin
                      species (lumichrome, LC; riboflavin, RF; flavin
                      mononucleotide, FMN; flavin adenine dinucleotide, FAD)
                      during heterologous expression and that its physicochemical
                      properties depend strongly on the nature of the bound
                      flavin. We show that whereas the dissociation constants for
                      different chromophores are similar, the melting temperature
                      of the protein reconstituted with single flavin species
                      varies from ~ 60 °C for LC to ~ 81 °C for FMN, and
                      photobleaching half-times vary almost 100-fold. These
                      observations serve as a caution for future studies of LOV
                      domains in non-native conditions yet raise the possibility
                      of fine-tuning various properties of LOV-based fluorescent
                      probes and optogenetic tools by manipulating the chromophore
                      composition.},
      cin          = {IMET / IBG-1 / IBI-7},
      ddc          = {620},
      cid          = {I:(DE-Juel1)IMET-20090612 / I:(DE-Juel1)IBG-1-20101118 /
                      I:(DE-Juel1)IBI-7-20200312},
      pnm          = {2171 - Biological and environmental resources for
                      sustainable use (POF4-217) / 5241 - Molecular Information
                      Processing in Cellular Systems (POF4-524)},
      pid          = {G:(DE-HGF)POF4-2171 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {34796467},
      UT           = {WOS:000720258200001},
      doi          = {10.1007/s43630-021-00138-3},
      url          = {https://juser.fz-juelich.de/record/905009},
}