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@ARTICLE{Petrovskaya:279614,
      author       = {Petrovskaya, L. E. and Balashov, S. P. and Lukashev, E. P.
                      and Imasheva, E. S. and Gushchin, Ivan and Dioumaev, A. K.
                      and Rubin, A. B. and Dolgikh, D. A. and Gordeliy, Valentin
                      and Lanyi, J. K. and Kirpichnikov, M. P.},
      title        = {{ESR} — {A} retinal protein with unusual properties from
                      {E}xiguobacterium sibiricum},
      journal      = {Biochemistry (Moscow)},
      volume       = {80},
      number       = {6},
      issn         = {1608-3040},
      address      = {Dordrecht [u.a.]},
      publisher    = {Springer Science + Business Media B.V},
      reportid     = {FZJ-2015-07498},
      pages        = {688 - 700},
      year         = {2015},
      abstract     = {This review covers the properties of a retinal protein
                      (ESR) from the psychrotrophic bacterium Exiguobacterium
                      sibiricum that functions as a light-driven proton pump. The
                      presence of a lysine residue at the position corresponding
                      to intramolecular proton donor for the Schiff base
                      represents a unique structural feature of ESR. We have shown
                      that Lys96 successfully facilitates delivery of protons from
                      the cytoplasmic surface to the Schiff base, thus acting as a
                      proton donor in ESR. Since proton uptake during the
                      photocycle precedes Schiff base reprotonation, we conclude
                      that this residue is initially in the uncharged state and
                      acquires a proton for a short time after Schiff base
                      deprotonation and M intermediate formation. Involvement of
                      Lys as a proton donor distinguishes ESR from the related
                      retinal proteins — bacteriorhodopsin (BR), proteorhodopsin
                      (PR), and xanthorhodopsin (XR), in which the donor function
                      is performed by residues with a carboxyl side chain. Like
                      other eubacterial proton pumps (PR and XR), ESR contains a
                      histidine residue interacting with the proton acceptor
                      Asp85. In contrast to PR, this interaction leads to shift of
                      the acceptor’s pK a to more acidic pH, thus providing its
                      ability to function over a wide pH range. The presence of a
                      strong H-bond between Asp85 and His57, the structure of the
                      proton-conducting pathways from cytoplasmic surface to the
                      Schiff base and to extracellular surface, and other
                      properties of ESR were demonstrated by solving its
                      three-dimensional structure, which revealed several
                      differences from known structures of BR and XR. The
                      structure of ESR, its photocycle, and proton transfer
                      reactions are discussed in comparison with homologous
                      retinal proteins.},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16 / PUB:(DE-HGF)36},
      UT           = {WOS:000357451000005},
      doi          = {10.1134/S000629791506005X},
      url          = {https://juser.fz-juelich.de/record/279614},
}