Excitation energy transfer and charge separation are affected in Arabidopsis thaliana mutants lacking light-harvesting chlorophyll a/b binding protein Lhcb3

J Photochem Photobiol B. 2015 Dec:153:423-8. doi: 10.1016/j.jphotobiol.2015.11.002. Epub 2015 Nov 9.

Abstract

The composition of LHCII trimers as well as excitation energy transfer and charge separation in grana cores of Arabidopsis thaliana mutant lacking chlorophyll a/b binding protein Lhcb3 have been investigated and compared to those in wild-type plants. In grana cores of lhcb3 plants we observed increased amounts of Lhcb1 and Lhcb2 apoproteins per PSII core. The additional copies of Lhcb1 and Lhcb2 are expected to substitute for Lhcb3 in LHCII trimers M as well as in the LHCII "extra" pool, which was found to be modestly enlarged as a result of the absence of Lhcb3. Time-resolved fluorescence measurements reveal a deceleration of the fast phase of excitation dynamics in grana cores of the mutant by ~15 ps, whereas the average fluorescence lifetime is not significantly altered. Monte Carlo modeling predicts a slowing down of the mean hopping time and an increased stabilization of the primary charge separation in the mutant. Thus our data imply that absence of apoprotein Lhcb3 results in detectable differences in excitation energy transfer and charge separation.

Keywords: Charge separation; Excitation energy transfer; Light Harvesting Complex II trimers; Monte Carlo simulation; Photosystem II.

MeSH terms

  • Arabidopsis / genetics
  • Arabidopsis / metabolism*
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism*
  • Energy Transfer
  • Kinetics
  • Light-Harvesting Protein Complexes / genetics
  • Light-Harvesting Protein Complexes / metabolism*
  • Monte Carlo Method
  • Mutation
  • Photosynthesis
  • Protein Multimerization
  • Spectrometry, Fluorescence
  • Thylakoids / genetics
  • Thylakoids / metabolism

Substances

  • Arabidopsis Proteins
  • Light-Harvesting Protein Complexes