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@ARTICLE{Kovalev:1025970,
      author       = {Kovalev, Kirill and Tsybrov, Fedor and Alekseev, Alexey and
                      Shevchenko, Vitaly and Soloviov, Dmytro and Siletsky, Sergey
                      and Bourenkov, Gleb and Agthe, Michael and Nikolova, Marina
                      and von Stetten, David and Astashkin, Roman and Bukhdruker,
                      Sergey and Chizhov, Igor and Royant, Antoine and Kuzmin,
                      Alexander and Gushchin, Ivan and Rosselli, Riccardo and
                      Rodriguez-Valera, Francisco and Ilyinskiy, Nikolay and
                      Rogachev, Andrey and Borshchevskiy, Valentin and Schneider,
                      Thomas R. and Bamberg, Ernst and Gordeliy, Valentin},
      title        = {{M}echanisms of inward transmembrane proton translocation},
      journal      = {Nature structural $\&$ molecular biology},
      volume       = {30},
      number       = {7},
      issn         = {1545-9993},
      address      = {London [u.a.]},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2024-03247},
      pages        = {970 - 979},
      year         = {2023},
      abstract     = {Proton transport is indispensable for cell life. It is
                      believed that molecular mechanisms of proton movement
                      through different types of proton-conducting molecules have
                      general universal features. However, elucidation of such
                      mechanisms is a challenge. It requires
                      true-atomic-resolution structures of all key
                      proton-conducting states. Here we present a comprehensive
                      function-structure study of a light-driven bacterial inward
                      proton pump, xenorhodopsin, from Bacillus coahuilensis in
                      all major proton-conducting states. The structures reveal
                      that proton translocation is based on proton wires regulated
                      by internal gates. The wires serve as both selectivity
                      filters and translocation pathways for protons. The
                      cumulative results suggest a general concept of proton
                      translocation. We demonstrate the use of serial
                      time-resolved crystallography at a synchrotron source with
                      sub-millisecond resolution for rhodopsin studies, opening
                      the door for principally new applications. The results might
                      also be of interest for optogenetics since xenorhodopsins
                      are the only alternative tools to fire neurons.},
      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       = {37386213},
      UT           = {WOS:001020309800001},
      doi          = {10.1038/s41594-023-01020-9},
      url          = {https://juser.fz-juelich.de/record/1025970},
}