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@ARTICLE{Maris:112075,
      author       = {Maris, A. and Melandri, S. and Evangelisti, L. and
                      Caminati, W. and Giuliano, B. M. and Plekan, O. and Feyer,
                      V. and Richter, R. and Coreno, M. and Prince, K. C.},
      title        = {{S}oft {X}-ray photoemission spectroscopy of selected
                      neurotransmitters in the gas phase},
      journal      = {Journal of electron spectroscopy and related phenomena},
      volume       = {185},
      issn         = {0368-2048},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-112075},
      pages        = {S244 - S251},
      year         = {2012},
      note         = {We gratefully acknowledge the assistance of our colleagues
                      at Elettra for providing good quality synchrotron light.
                      B.M.G. thanks FCT for financial support
                      (SFRH/BPD/44689/2008). A. Maris thanks N. Kosugi for sharing
                      his GSCF3 program with us and for essential discussions on
                      its use.},
      abstract     = {The valence molecular orbitals and core levels of tyramine,
                      tryptamine and tryptophol in the gas phase have been studied
                      using X-ray photoelectron spectroscopy (XPS) and theoretical
                      methods. The energies of the outer valence region spectrum
                      are found to be in agreement with previously reported He I
                      spectra, while new data on the inner valence molecular
                      orbitals are reported. The structures in the carbon,
                      nitrogen and oxygen core level spectra of these molecules
                      have been identified and assigned. These compounds are
                      characterised by conformers with hydrogen bonding in which
                      the pi systems of the phenol and indole groups act as
                      hydrogen acceptors, but a spectroscopic signature of this
                      hydrogen bond was not observed. This is in contrast with our
                      previous spectra of amino acids, where conformers with
                      specific hydrogen bonding showed strong effects in core
                      level spectra. We attribute the difference to the weaker
                      strength of the pi-hydrogen bonding. (C) 2012 Elsevier B.V.
                      All rights reserved.},
      keywords     = {J (WoSType)},
      cin          = {PGI-6},
      ddc          = {620},
      cid          = {I:(DE-Juel1)PGI-6-20110106},
      pnm          = {Grundlagen für zukünftige Informationstechnologien},
      pid          = {G:(DE-Juel1)FUEK412},
      shelfmark    = {Spectroscopy},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000308627700009},
      doi          = {10.1016/j.elspec.2012.06.007},
      url          = {https://juser.fz-juelich.de/record/112075},
}