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@ARTICLE{Yaroshevich:904316,
      author       = {Yaroshevich, Igor A. and Maksimov, Eugene G. and Sluchanko,
                      Nikolai N. and Zlenko, Dmitry V. and Stepanov, Alexey V. and
                      Slutskaya, Ekaterina A. and Slonimskiy, Yury B. and
                      Botnarevskii, Viacheslav S. and Remeeva, Alina and Gushchin,
                      Ivan and Kovalev, Kirill and Gordeliy, Valentin I. and
                      Shelaev, Ivan V. and Gostev, Fedor E. and Khakhulin, Dmitry
                      and Poddubnyy, Vladimir V. and Gostev, Timofey S. and
                      Cherepanov, Dmitry A. and Polívka, Tomáš and Kloz,
                      Miroslav and Friedrich, Thomas and Paschenko, Vladimir Z.
                      and Nadtochenko, Victor A. and Rubin, Andrew B. and
                      Kirpichnikov, Mikhail P.},
      title        = {{R}ole of hydrogen bond alternation and charge transfer
                      states in photoactivation of the {O}range {C}arotenoid
                      {P}rotein},
      journal      = {Communications biology},
      volume       = {4},
      number       = {1},
      issn         = {2399-3642},
      address      = {London},
      publisher    = {Springer Nature},
      reportid     = {FZJ-2021-05886},
      pages        = {539},
      year         = {2021},
      abstract     = {Here, we propose a possible photoactivation mechanism of a
                      35-kDa blue light-triggered photoreceptor, the Orange
                      Carotenoid Protein (OCP), suggesting that the reaction
                      involves the transient formation of a protonated
                      ketocarotenoid (oxocarbenium cation) state. Taking advantage
                      of engineering an OCP variant carrying the Y201W mutation,
                      which shows superior spectroscopic and structural
                      properties, it is shown that the presence of Trp201 augments
                      the impact of one critical H-bond between the ketocarotenoid
                      and the protein. This confers an unprecedented homogeneity
                      of the dark-adapted OCP state and substantially increases
                      the yield of the excited photoproduct S*, which is important
                      for the productive photocycle to proceed. A 1.37 Å
                      crystal structure of OCP Y201W combined with femtosecond
                      time-resolved absorption spectroscopy, kinetic analysis, and
                      deconvolution of the spectral intermediates, as well as
                      extensive quantum chemical calculations incorporating the
                      effect of the local electric field, highlighted the role of
                      charge-transfer states during OCP photoconversion.},
      cin          = {IBI-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33972665},
      UT           = {WOS:000656215600008},
      doi          = {10.1038/s42003-021-02022-3},
      url          = {https://juser.fz-juelich.de/record/904316},
}