% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@INPROCEEDINGS{Chiariello:911690,
      author       = {Chiariello, Gabriella and Alfonso-Prieto, Mercedes and
                      Ippoliti, Emiliano},
      title        = {{M}olecular {O}rigin of the {U}nusual {P}roton/{F}luoride
                      {S}toichiometry of {CLC}-{T}ype {F}luoride {T}ransporters},
      volume       = {450},
      address      = {Jülich},
      publisher    = {Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag},
      reportid     = {FZJ-2022-04944},
      isbn         = {978-3-95806-646-5},
      series       = {Publication Series of the John von Neumann Institute for
                      Computing (NIC) NIC Series 51},
      pages        = {189-198},
      year         = {2022},
      comment      = {NIC Symposium 2022 Proceedings},
      booktitle     = {NIC Symposium 2022 Proceedings},
      abstract     = {Fluoride (F–) is present in natural water sources at
                      concentrations that are toxic to unicellular organisms.
                      Thus, prokaryotes have evolved export transporters for this
                      anion to ensure their survival. One such group of fluoride
                      transporters are the F−/H+ exchangers belonging to the CLC
                      family (CLCF s). The X-ray structure of the Enterococcus
                      casseliflavus CLCF (CLCF -eca) contains a glutamate (E318)
                      in the central anion-binding site, which is absent in the
                      conventional CLCs and has been suggested as one of the
                      determinants enabling fluoride transport. Here we use
                      classical and subnanosecond QM/MM metadynamics simulations
                      to investigate the molecular basis of the 1:1
                      proton:fluoride stoichiometry in CLCF -eca. The proton
                      release mechanism relies on the formation of the E318-F-E118
                      triad, stabilised by a complex H-bond network in which both
                      glutamates interact with F−. The interplay between the two
                      glutamates enables protonation of fluoride and proton
                      release as HF into the intracellular solution. Our results
                      demonstrate how glutamate insertion into the central
                      anion-binding site of CLCF-eca permits F− release coupled
                      to H+ inward movement, resulting in effective and selective
                      F− transport.},
      month         = {Sep},
      date          = {2022-09-29},
      organization  = {NIC Symposium, Jülich (Germany), 29
                       Sep 2022 - 30 Sep 2022},
      cin          = {IAS-5 / INM-9},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)8 / PUB:(DE-HGF)7},
      url          = {https://juser.fz-juelich.de/record/911690},
}