Resonance Raman spectroscopy of the photosystem II light-harvesting complex of green plants: a comparison of trimeric and aggregated states

Biochemistry. 1995 Feb 21;34(7):2333-7. doi: 10.1021/bi00007a029.

Abstract

Resonance Raman spectroscopy was performed on photosystem II light-harvesting complex (LHCII) in trimeric and oligomeric states with various excitation conditions. From these studies, it can be concluded that the structure of LHCII is altered during the trimer/oligomer transition. These structural changes affect the conformation of a population of carotenoid within the complex, which becomes twisted in the oligomeric form. Moreover, the interactions assumed by a chlorophyll a and a chlorophyll b are modified during the oligomerization process. This induces the formation of an H-bond to a formyl group of a chlorophyll b molecule and to a keto group of a chlorophyll a molecule. The extent to which these H-bonds to chlorophyll relate to the formation of the quencher cannot yet be precisely established. However, the structural changes they evidence may play a role in the control of the energy flux by LHCII complexes.

MeSH terms

  • Carotenoids / chemistry
  • Chlorophyll / chemistry
  • Chlorophyll A
  • Hydrogen Bonding
  • In Vitro Techniques
  • Light-Harvesting Protein Complexes
  • Photosynthetic Reaction Center Complex Proteins / chemistry*
  • Photosystem II Protein Complex
  • Spectrum Analysis, Raman
  • Spinacia oleracea

Substances

  • Light-Harvesting Protein Complexes
  • Photosynthetic Reaction Center Complex Proteins
  • Photosystem II Protein Complex
  • Chlorophyll
  • Carotenoids
  • chlorophyll b
  • Chlorophyll A