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@ARTICLE{Lamm:1028213,
      author       = {Lamm, Gerrit H. U. and Zabelskii, Dmitrii and Balandin,
                      Taras and Gordeliy, Valentin and Wachtveitl, Josef},
      title        = {{C}alcium-{S}ensitive {M}icrobial {R}hodopsin
                      {V}ir{C}h{R}1: {A} {F}emtosecond to {S}econd {P}hotocycle
                      {S}tudy},
      journal      = {The journal of physical chemistry letters},
      volume       = {15},
      number       = {20},
      issn         = {1948-7185},
      address      = {Washington, DC},
      publisher    = {ACS},
      reportid     = {FZJ-2024-04407},
      pages        = {5510 - 5516},
      year         = {2024},
      abstract     = {Viral rhodopsins are light-gated cation channels
                      representing a novel class of microbial rhodopsins. For
                      viral rhodopsin 1 subfamily members VirChR1 and OLPVR1,
                      channel activity is abolished above a certain calcium
                      concentration. Here we present a calcium-dependent
                      spectroscopic analysis of VirChR1 on the femtosecond to
                      second time scale. Unlike channelrhodopsin-2, VirChR1
                      possesses two intermediate states P1 and P2 on the ultrafast
                      time scale, similar to J and K in ion-pumping rhodopsins.
                      Subsequently, we observe multifaceted photocycle kinetics
                      with up to seven intermediate states. Calcium predominantly
                      affects the last photocycle steps, including the appearance
                      of additional intermediates P6Ca and P7 representing the
                      blocked channel. Furthermore, the photocycle of the
                      counterion variant D80N is drastically altered, yielding
                      intermediates with different spectra and kinetics compared
                      to those of the wt. These findings demonstrate the central
                      role of the counterion within the defined reaction sequence
                      of microbial rhodopsins that ultimately defines the protein
                      function.},
      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},
      pubmed       = {38749015},
      UT           = {WOS:001226083900001},
      doi          = {10.1021/acs.jpclett.4c00693},
      url          = {https://juser.fz-juelich.de/record/1028213},
}