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@ARTICLE{Lamm:1052090,
      author       = {Lamm, Gerrit H. U. and Zabelskii, Dmitrii and Balandin,
                      Taras and Gordeliy, Valentin and Wachtveitl, Josef},
      title        = {{C}ombined {M}utational and {S}pectroscopic {S}tudy on the
                      {C}alcium-{R}elated {K}inetic {E}ffects on the {V}ir{C}h{R}1
                      {P}hotocycle},
      journal      = {The journal of physical chemistry / B},
      volume       = {129},
      number       = {11},
      issn         = {1520-6106},
      address      = {Washington, DC},
      publisher    = {Americal Chemical Society},
      reportid     = {FZJ-2026-00755},
      pages        = {2946 - 2957},
      year         = {2025},
      abstract     = {The viral rhodopsin 1 subfamily consists of microbial
                      rhodopsins, such as VirChR1, with a light-gated cation
                      channeling functionality, which is inhibited by calcium. For
                      VirChR1, S14, E54, and N225 have been proposed as key
                      residues for calcium binding. They form a highly conserved
                      SEN-triad in channelrhodopsins near the functionally
                      important central gate. Here, we present a time-resolved
                      UV/vis spectroscopic study on the VirChR1 variants S14A,
                      E54A, and N225A in a calcium-dependent manner. Comparison
                      with the calcium-associated effects observed for the wild
                      type shed light on the role of the respective residues for
                      the calcium interaction. While S14A shows less pronounced,
                      yet similar, signals, indicative of a reduced calcium
                      affinity, E54A exhibits nearly calcium-independent
                      photocycle kinetics, highlighting its crucial role for
                      calcium binding. The N225A variant shows altered photocycle
                      kinetics, in both the absence and presence of calcium,
                      demonstrating its critical role in the formation of the
                      functionally important central gate in VirChR1.},
      cin          = {IBI-7},
      ddc          = {530},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1021/acs.jpcb.4c08416},
      url          = {https://juser.fz-juelich.de/record/1052090},
}