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@ARTICLE{Maia:904485,
      author       = {Maia, Raiza N. A. and Ehrenberg, David and Oldemeyer,
                      Sabine and Knieps-Grünhagen, Esther and Krauss, Ulrich and
                      Heberle, Joachim},
      title        = {{R}eal-{T}ime {T}racking of {P}roton {T}ransfer from the
                      {R}eactive {C}ysteine to the {F}lavin {C}hromophore of a
                      {P}hotosensing {L}ight {O}xygen {V}oltage {P}rotein},
      journal      = {Journal of the American Chemical Society},
      volume       = {143},
      number       = {32},
      issn         = {0002-7863},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2021-06055},
      pages        = {12535 - 12542},
      year         = {2021},
      abstract     = {LOV (light oxygen voltage) proteins are photosensors
                      ubiquitous to all domains of life. A variant of the short
                      LOV protein from Dinoroseobacter shibae (DsLOV) exhibits an
                      exceptionally fast photocycle. We performed time-resolved
                      molecular spectroscopy on DsLOV-M49S and characterized the
                      formation of the thio-adduct state with a covalent bond
                      between the reactive cysteine (C72) and C4a of the FMN. By
                      use of a tunable quantum cascade laser, the weak absorption
                      change of the vibrational band of S–H stretching vibration
                      of C57 was resolved with a time resolution of 10 ns.
                      Deprotonation of C72 proceeded with a time constant of 12
                      μs which tallies the rise of the thio-adduct state. These
                      results provide valuable information for the mechanistic
                      interpretation of light-induced structural changes in LOV
                      domains, which involves the choreographed sequence of proton
                      transfers, changes in electron density distributions, spin
                      alterations of the latter, and transient bond formation and
                      breakage. Such molecular insight will help develop new
                      optogenetic tools based on flavin photoreceptors.},
      cin          = {IBG-1 / IMET},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBG-1-20101118 / I:(DE-Juel1)IMET-20090612},
      pnm          = {2171 - Biological and environmental resources for
                      sustainable use (POF4-217)},
      pid          = {G:(DE-HGF)POF4-2171},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34347468},
      UT           = {WOS:000686555000018},
      doi          = {10.1021/jacs.1c03409},
      url          = {https://juser.fz-juelich.de/record/904485},
}