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@ARTICLE{Schenkl:51340,
      author       = {Schenkl, S. and van Mourik, F. and Friedman, N. and Sheves,
                      M. and Schlesinger, R. and Haacke, S. and Chergui, M.},
      title        = {{I}nsights into excited-state and isomerization dynamics of
                      bacteriorhodopsin from ultrafast transient {UV} absorption},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {103},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {Academy},
      reportid     = {PreJuSER-51340},
      pages        = {4101 - 4106},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {A visible-pump/UV-probe transient absorption is used to
                      characterize the ultrafast dynamics of bacteriorhodopsin
                      with 80-fs time resolution. We identify three spectral
                      components in the 265- to 310-nm region, related to the
                      all-trans retinal, tryptophan (Trp)-86 and the isomerized
                      photoproduct, allowing us to map the dynamics from reactants
                      to products, along with the response of Trp amino acids. The
                      signal of the photoproduct appears with a time delay of
                      approximately 250 fs and is characterized by a steep rise (
                      approximately 150 fs), followed by additional rise and decay
                      components, with time scales characteristic of the J
                      intermediate. The delayed onset and the steep rise point to
                      an impulsive formation of a transition state on the way to
                      isomerization. We argue that this impulsive formation
                      results from a splitting of a wave packet of torsional modes
                      on the potential surface at the branching between the
                      all-trans and the cis forms. Parallel to these dynamics, the
                      signal caused by Trp response rises in approximately 200 fs,
                      because of the translocation of charge along the conjugate
                      chain, and possible mechanisms are presented, which trigger
                      isomerization.},
      keywords     = {Bacteriorhodopsins: chemistry / Bacteriorhodopsins:
                      genetics / Biophysical Phenomena / Biophysics /
                      Halobacterium salinarum: chemistry / Halobacterium
                      salinarum: genetics / Isomerism / Kinetics / Mutagenesis,
                      Site-Directed / Spectrophotometry, Ultraviolet /
                      Thermodynamics / Tryptophan: chemistry / Bacteriorhodopsins
                      (NLM Chemicals) / Tryptophan (NLM Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {000},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Multidisciplinary Sciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16537491},
      pmc          = {pmc:PMC1449653},
      UT           = {WOS:000236429300032},
      doi          = {10.1073/pnas.0506303103},
      url          = {https://juser.fz-juelich.de/record/51340},
}