% 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”.

@ARTICLE{Weichselbaum:834626,
      author       = {Weichselbaum, Ewald and Österbauer, Maria and Knyazev,
                      Denis G. and Batishchev, Oleg V. and Akimov, Sergey A. and
                      Hai Nguyen, Trung and Zhang, Chao and Knör, Günther and
                      Agmon, Noam and Carloni, Paolo and Pohl, Peter},
      title        = {{O}rigin of proton affinity to membrane/water interfaces},
      journal      = {Scientific reports},
      volume       = {7},
      number       = {1},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2017-04534},
      pages        = {4553},
      year         = {2017},
      abstract     = {Proton diffusion along biological membranes is vitally
                      important for cellular energetics. Here we extended previous
                      time-resolved fluorescence measurements to study the time
                      and temperature dependence of surface proton transport. We
                      determined the Gibbs activation energy barrier ΔG‡r that
                      opposes proton surface-to-bulk release from Arrhenius plots
                      of (i) protons’ surface diffusion constant and (ii) the
                      rate coefficient for proton surface-to-bulk release. The
                      large size of ΔG‡r disproves that quasi-equilibrium
                      exists in our experiments between protons in the
                      near-membrane layers and in the aqueous bulk. Instead,
                      non-equilibrium kinetics describes the proton travel between
                      the site of its photo-release and its arrival at a distant
                      membrane patch at different temperatures. ΔG‡r contains
                      only a minor enthalpic contribution that roughly corresponds
                      to the breakage of a single hydrogen bond. Thus, our
                      experiments reveal an entropic trap that ensures channeling
                      of highly mobile protons along the membrane interface in the
                      absence of potent acceptors.},
      cin          = {IAS-5 / INM-9},
      ddc          = {000},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000404618400067},
      doi          = {10.1038/s41598-017-04675-9},
      url          = {https://juser.fz-juelich.de/record/834626},
}