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@ARTICLE{Matsubara:40448,
      author       = {Matsubara, S. and Naumann, M. and Martin, J. M. and Nichol,
                      C. and Rascher, U. and Morosinotto, T. and Bassi, R. and
                      Osmond, B.},
      title        = {{S}lowly reversible de-epoxidation of lutein-epoxide in
                      deep shade leaves of a tropical tree legume may 'lock-in'
                      lutein-based photoprotection during acclimation to strong
                      light},
      journal      = {The journal of experimental botany},
      volume       = {56},
      issn         = {0022-0957},
      address      = {Oxford},
      publisher    = {Univ. Press},
      reportid     = {PreJuSER-40448},
      pages        = {461 - 468},
      year         = {2005},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The kinetics of response to strong light have been examined
                      in deeply shaded leaves of the tropical tree legume (Inga
                      sp.) which have extraordinarily high levels of the
                      alpha-xanthophyll lutein-epoxide that are co-located in
                      pigment-protein complexes of the photosynthetic apparatus
                      with the beta-xanthophyll violaxanthin. As in other species,
                      rapidly reversible photoprotection (measured as
                      non-photochemical chlorophyll fluorescence quenching) is
                      initiated within the time frame of sun-flecks (minutes),
                      before detectable conversion of violaxanthin to
                      antheraxanthin or zeaxanthin. Photoprotection is stabilized
                      within hours of exposure to strong light by simultaneously
                      engaging the reversible violaxanthin cycle and a slowly
                      reversible conversion of lutein-epoxide to lutein. It is
                      proposed that this lutein 'locks in' a primary mechanism of
                      photoprotection during photoacclimation in this species,
                      converting efficient light-harvesting antennae of the shade
                      plant into potential excitation dissipating centres. It is
                      hypothesized that lutein occupies sites L2 and V1 in
                      light-harvesting chlorophyll protein complexes of
                      photosystem II, facilitating enhanced photoprotection
                      through the superior singlet and/or triplet chlorophyll
                      quenching capacity of lutein.},
      keywords     = {Acclimatization: physiology / Circadian Rhythm / Electron
                      Transport / Fabaceae: metabolism / Fabaceae: physiology /
                      Fabaceae: radiation effects / Light / Lutein: analogs $\&$
                      derivatives / Lutein: metabolism / Photosynthetic Reaction
                      Center Complex Proteins: physiology / Pigments, Biological:
                      metabolism / Plant Leaves: physiology / Trees: physiology /
                      Tropical Climate / Photosynthetic Reaction Center Complex
                      Proteins (NLM Chemicals) / Pigments, Biological (NLM
                      Chemicals) / Lutein (NLM Chemicals) / J (WoSType)},
      cin          = {ICG-III},
      ddc          = {580},
      cid          = {I:(DE-Juel1)VDB49},
      pnm          = {Chemie und Dynamik der Geo-Biosphäre},
      pid          = {G:(DE-Juel1)FUEK257},
      shelfmark    = {Plant Sciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:15501906},
      UT           = {WOS:000226610500015},
      doi          = {10.1093/jxb/eri012},
      url          = {https://juser.fz-juelich.de/record/40448},
}