@article{GoetzeKroenerBanerjeeetal.2014,
  author    = {Goetze, Jan P. and Kr{\"o}ner, Dominik and Banerjee, Shiladitya and Karasulu, Bora and Thiel, Walter},
  title     = {Carotenoids as a shortcut for chlorophyll Soret-to-Q band energy flow},
  series = {ChemPhysChem : a European journal of chemical physics and physical chemistry},
  volume    = {15},
  journal   = {ChemPhysChem : a European journal of chemical physics and physical chemistry},
  number    = {15},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1439-4235},
  doi       = {10.1002/cphc.201402233},
  pages     = {3391 -- 3400},
  year      = {2014},
  abstract  = {It is proposed that xanthophylls, and carotenoids in general, may assist in energy transfer from the chlorophyll Soret band to the Q band. Ground-state (1A(g)) and excited-state (1B(u)) optimizations of violaxanthin (Vx) and zeaxanthin (Zx) are performed in an environment mimicking the light-harvesting complex II (LHCII), including the closest chlorophyll b molecule (Chl). Time-dependent density functional theory (TD-DFT, CAM-B3LYP functional) is used in combination with a semi-empirical description to obtain the excited-state geometries, supported by additional DFT/multireference configuration interaction calculations, with and without point charges representing LHCII. In the ground state, Vx and Zx show similar properties. At the 1B(u) minimum, the energy of the Zx 1Bu state is below the Chl Q band, in contrast to Vx. Both Vx and Zx may act as acceptors of Soret-state energy; transfer to the Q band seems to be favored for Vx. These findings suggest that carotenoids may generally mediate Soret-to-Q energy flow in LHCII.},
  language  = {en}
}
@article{GoetzeGrecoMitricetal.2012,
  author    = {Goetze, Jan P. and Greco, Claudio and Mitric, Roland and Bonacic-Koutecky, Vlasta and Saalfrank, Peter},
  title     = {BLUF Hydrogen network dynamics and UV/Vis spectra: A combined molecular dynamics and quantum chemical study},
  series = {JOURNAL OF COMPUTATIONAL CHEMISTRY},
  volume    = {33},
  journal   = {JOURNAL OF COMPUTATIONAL CHEMISTRY},
  number    = {28},
  publisher = {WILEY-BLACKWELL},
  address   = {HOBOKEN},
  issn      = {0192-8651},
  doi       = {10.1002/jcc.23056},
  pages     = {2233 -- 2242},
  year      = {2012},
  abstract  = {Blue light sensing using flavin (BLUF) protein photoreceptor domains change their hydrogen bond network after photoexcitation. To explore this phenomenon, BLUF domains from R. sphaeroides were simulated using Amber99 molecular dynamics (MD). Five starting configurations were considered, to study different BLUF proteins (AppA/BlrB), Trp conformations (Win/Wout), structure determination (X-ray/NMR), and finally, His protonation states. We found dependencies of the hydrogen bonds on almost all parameters. Our data show an especially strong correlation of the Trp position and hydrogen bonds involving Gln63. The latter is in some contradiction to earlier results (Obanayama et al., Photochem. Photobiol. 2008, 84 10031010). Possible origins and implications are discussed. Our calculations support conjectures that Gln63 is more flexible with Trp104 in Win position. Using snapshots from MD and time-dependent density functional theory, UV/vis spectra for the chromophore were determined, which account for molecular motion of the protein under ambient conditions. In accord with experiment, it is found that the UV/vis spectra of BLUF bound flavin are red-shifted and thermally broadened for all calculated p ? p* transitions, relative to gas phase flavin at T = 0 K. However, differences in the spectra between the various BLUF configurations cannot be resolved with the present approach. (c) 2012 Wiley Periodicals, Inc.},
  language  = {en}
}