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@ARTICLE{Rokitskaya:904325,
      author       = {Rokitskaya, Tatyana I. and Maliar, Nina and Kovalev, Kirill
                      V. and Volkov, Oleksandr and Gordeliy, Valentin I. and
                      Antonenko, Yuri N.},
      title        = {{R}hodopsin {C}hannel {A}ctivity {C}an {B}e {E}valuated by
                      {M}easuring the {P}hotocurrent {V}oltage {D}ependence in
                      {P}lanar {B}ilayer {L}ipid {M}embranes},
      journal      = {Biochemistry (Moscow)},
      volume       = {86},
      number       = {4},
      issn         = {0006-2979},
      address      = {Dordrecht [u.a.]},
      publisher    = {Springer Science + Business Media B.V},
      reportid     = {FZJ-2021-05895},
      pages        = {409 - 419},
      year         = {2021},
      abstract     = {The studies of the functional properties of
                      retinal-containing proteins often include experiments in
                      model membrane systems, e.g., measurements of electric
                      current through planar bilayer lipid membranes (BLMs) with
                      proteoliposomes adsorbed on one of the membrane surfaces.
                      However, the possibilities of this method have not been
                      fully explored yet. We demonstrated that the voltage
                      dependence of stationary photocurrents for two
                      light-sensitive proteins, bacteriorhodopsin (bR) and
                      channelrhodopsin 2 (ChR2), in the presence of protonophore
                      had very different characteristics. In the case of the bR
                      (proton pump), the photocurrent through the BLM did not
                      change direction when the polarity of the applied voltage
                      was switched. In the case of the photosensitive channel
                      protein ChR2, the photocurrent increased with the increase
                      in voltage and the current polarity changed with the change
                      in the voltage polarity. The protonophore
                      4,5,6,7-tetrachloro-2-trifluoromethyl benzimidazole (TTFB)
                      was more efficient in the maximizing stationary
                      photocurrents. In the presence of carbonyl
                      cyanide-m-chlorophenylhydrazone (CCCP), the amplitude of the
                      measured photocurrents for bR significantly decreased, while
                      in the case of ChR2, the photocurrents virtually
                      disappeared. The difference between the effects of TTFB and
                      CCCP was apparently due to the fact that, in contrast to
                      TTFB, CCCP transfers protons across the liposome membranes
                      with a higher rate than through the decane-containing BLM
                      used as a surface for the proteoliposome adsorption.},
      cin          = {IBI-7},
      ddc          = {540},
      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       = {33941063},
      UT           = {WOS:000630849000001},
      doi          = {10.1134/S0006297921040039},
      url          = {https://juser.fz-juelich.de/record/904325},
}