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@ARTICLE{Vlasov:866925,
      author       = {Vlasov, A. V. and Kovalev, K. V. and Marx, S.-H. and Round,
                      E. S. and Gushchin, I. Yu. and Polovinkin, V. A. and Tsoy,
                      N. M. and Okhrimenko, I. S. and Borshchevskiy, V. I. and
                      Büldt, G. D. and Ryzhykau, Yu. L. and Rogachev, A. V. and
                      Chupin, V. V. and Kuklin, A. I. and Dencher, N. A. and
                      Gordeliy, V. I.},
      title        = {{U}nusual features of the c-ring of {F}1{FO} {ATP}
                      synthases},
      journal      = {Scientific reports},
      volume       = {9},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2019-05978},
      pages        = {18547},
      year         = {2019},
      abstract     = {Membrane integral ATP synthases produce adenosine
                      triphosphate, the universal “energy currency” of most
                      organisms. However, important details of proton driven
                      energy conversion are still unknown. We present the first
                      high-resolution structure (2.3 Å) of the in meso
                      crystallized c-ring of 14 subunits from spinach
                      chloroplasts. The structure reveals molecular mechanisms of
                      intersubunit contacts in the c14-ring, and it shows
                      additional electron densities inside the c-ring which form
                      circles parallel to the membrane plane. Similar densities
                      were found in all known high-resolution structures of
                      c-rings of F1FO ATP synthases from archaea and bacteria to
                      eukaryotes. The densities might originate from isoprenoid
                      quinones (such as coenzyme Q in mitochondria and
                      plastoquinone in chloroplasts) that is consistent with
                      differential UV-Vis spectroscopy of the c-ring samples,
                      unusually large distance between polar/apolar interfaces
                      inside the c-ring and universality among different species.
                      Although additional experiments are required to verify this
                      hypothesis, coenzyme Q and its analogues known as electron
                      carriers of bioenergetic chains may be universal cofactors
                      of ATP synthases, stabilizing c-ring and prevent ion leakage
                      through it.},
      cin          = {ICS-6},
      ddc          = {600},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31811229},
      UT           = {WOS:000501745000001},
      doi          = {10.1038/s41598-019-55092-z},
      url          = {https://juser.fz-juelich.de/record/866925},
}