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@ARTICLE{Mulkidjanian:57132,
      author       = {Mulkidjanian, A. Y. and Heberle, J. and Cherepanov, D. A.},
      title        = {{P}rotons @ interfaces: implications for biological energy
                      conversion},
      journal      = {Biochimica et biophysica acta / Bioenergetics},
      volume       = {1757},
      issn         = {0005-2728},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-57132},
      pages        = {913 - 930},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The review focuses on the anisotropy of proton transfer at
                      the surface of biological membranes. We consider (i) the
                      data from "pulsed" experiments, where light-triggered
                      enzymes capture or eject protons at the membrane surface,
                      (ii) the electrostatic properties of water at charged
                      interfaces, and (iii) the specific structural attributes of
                      proton-translocating enzymes. The pulsed experiments
                      revealed that proton exchange between the membrane surface
                      and the bulk aqueous phase takes as much as about 1 ms, but
                      could be accelerated by added mobile pH-buffers. Since the
                      accelerating capacity of the latter decreased with the
                      increase in their electric charge, it was concluded that the
                      membrane surface is separated from the bulk aqueous phase by
                      a barrier of electrostatic nature. The barrier could arise
                      owing to the water polarization at the negatively charged
                      membrane surface. The barrier height depends linearly on the
                      charge of penetrating ions; for protons, it has been
                      estimated as about 0.12 eV. While the proton exchange
                      between the surface and the bulk aqueous phase is retarded
                      by the interfacial barrier, the proton diffusion along the
                      membrane, between neighboring enzymes, takes only
                      microseconds. The proton spreading over the membrane is
                      facilitated by the hydrogen-bonded networks at the surface.
                      The membrane-buried layers of these networks can eventually
                      serve as a storage/buffer for protons (proton sponges). As
                      the proton equilibration between the surface and the bulk
                      aqueous phase is slower than the lateral proton diffusion
                      between the "sources" and "sinks", the proton activity at
                      the membrane surface, as sensed by the energy transducing
                      enzymes at steady state, might deviate from that measured in
                      the adjoining water phase. This trait should increase the
                      driving force for ATP synthesis, especially in the case of
                      alkaliphilic bacteria.},
      keywords     = {Biological Transport / Cations: chemistry / Electron
                      Transport Complex IV: chemistry / Energy Metabolism /
                      Kinetics / Membranes: physiology / Models, Biological /
                      Models, Molecular / Protein Conformation / Protons / Water:
                      chemistry / Cations (NLM Chemicals) / Protons (NLM
                      Chemicals) / Water (NLM Chemicals) / Electron Transport
                      Complex IV (NLM Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16624250},
      UT           = {WOS:000241481300005},
      doi          = {10.1016/j.bbabio.2006.02.015},
      url          = {https://juser.fz-juelich.de/record/57132},
}