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@ARTICLE{Chaves:878597,
      author       = {Chaves, Gustavo and Bungert‐Plümke, Stefanie and
                      Franzen, Arne and Mahorivska, Iryna and Musset, Boris},
      title        = {{Z}inc modulation of proton currents in a new
                      voltage‐gated proton channel suggests a mechanism of
                      inhibition},
      journal      = {The FEBS journal},
      volume       = {287},
      number       = {22},
      issn         = {1742-4658},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2020-02935},
      pages        = {4996-5018},
      year         = {2020},
      abstract     = {The HV1 voltage‐gated proton (HV1) channel is a key
                      component of the cellular proton extrusion machinery and is
                      pivotal for charge compensation during the respiratory burst
                      of phagocytes. The best‐described physiological inhibitor
                      of HV1 is Zn2+. Externally applied ZnCl2 drastically reduces
                      proton currents reportedly recorded in Homo sapiens, Rattus
                      norvegicus, Mus musculus, Oryctolagus cuniculus, Rana
                      esculenta, Helix aspersa, Ciona intestinalis, Coccolithus
                      pelagicus, Emiliania huxleyi, Danio rerio, Helisoma
                      trivolvis, and Lingulodinium polyedrum, but with
                      considerable species variability. Here, we report the
                      effects of Zn2+ and Cd2+ on HV1 from Nicoletia phytophila,
                      NpHV1. We introduced mutations at potential Zn2+
                      coordination sites and measured Zn2+ inhibition in different
                      extracellular pH, with Zn2+ concentrations up to 1000 μm.
                      Zn2+ inhibition in NpHV1 was quantified by the slowing of
                      the activation time constant and a positive shift of the
                      conductance–voltage curve. Replacing aspartate in the
                      S3‐S4 loop with histidine (D145H) enhanced both the
                      slowing of activation kinetics and the shift in the
                      voltage–conductance curve, such that Zn2+ inhibition
                      closely resembled that of the human channel. Histidine is
                      much more effective than aspartate in coordinating Zn2+ in
                      the S3‐S4 linker. A simple Hodgkin Huxley model of NpHV1
                      suggests a decrease in the opening rate if it is inhibited
                      by zinc or cadmium. Limiting slope measurements and
                      high‐resolution clear native gel electrophoresis (hrCNE)
                      confirmed that NpHV1 functions as a dimer. The data support
                      the hypothesis that zinc is coordinated in between the dimer
                      instead of the monomer. Zinc coordination sites may be
                      potential targets for drug development.},
      cin          = {IBI-1},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IBI-1-20200312},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32160407},
      UT           = {WOS:000558784200001},
      doi          = {10.1111/febs.15291},
      url          = {https://juser.fz-juelich.de/record/878597},
}