Light-Driven Reconfiguration of a Xanthophyll Violaxanthin in the Photosynthetic Pigment-Protein Complex LHCII: A Resonance Raman Study

J Phys Chem B. 2016 May 19;120(19):4373-82. doi: 10.1021/acs.jpcb.6b01641. Epub 2016 May 10.

Abstract

Resonance Raman analysis of the photosynthetic complex LHCII, immobilized in a polyacrylamide gel, reveals that one of the protein-bound xanthophylls, assigned as violaxanthin, undergoes light-induced molecular reconfiguration. The phototransformation is selectively observed in a trimeric structure of the complex and is associated with a pronounced twisting and a trans-cis molecular configuration change of the polyene chain of the carotenoid. Among several spectral effects accompanying the reconfiguration there are ones indicating a carotenoid triplet state. Possible physiological importance of the light-induced violaxanthin reconfiguration as a mechanism associated with making the pigment available for enzymatic deepoxidation in the xanthophyll cycle is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Isomerism
  • Light*
  • Light-Harvesting Protein Complexes / chemistry*
  • Light-Harvesting Protein Complexes / isolation & purification
  • Light-Harvesting Protein Complexes / metabolism
  • Microscopy, Confocal
  • Plant Proteins / chemistry*
  • Plant Proteins / isolation & purification
  • Plant Proteins / metabolism
  • Protein Structure, Quaternary
  • Spectrum Analysis, Raman
  • Spinacia oleracea / metabolism
  • Xanthophylls / chemistry*
  • Xanthophylls / isolation & purification
  • Xanthophylls / metabolism

Substances

  • Light-Harvesting Protein Complexes
  • Plant Proteins
  • Xanthophylls
  • violaxanthin