Slowly 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

J Exp Bot. 2005 Jan;56(411):461-8. doi: 10.1093/jxb/eri012. Epub 2004 Oct 22.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 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

Substances

  • Photosynthetic Reaction Center Complex Proteins
  • Pigments, Biological
  • Lutein