Ultrafast time-resolved spectroscopy of the light-harvesting complex 2 (LH2) from the photosynthetic bacterium Thermochromatium tepidum

Photosynth Res. 2011 Oct;110(1):49-60. doi: 10.1007/s11120-011-9692-7. Epub 2011 Oct 8.

Abstract

The light-harvesting complex 2 from the thermophilic purple bacterium Thermochromatium tepidum was purified and studied by steady-state absorption and fluorescence, sub-nanosecond-time-resolved fluorescence and femtosecond time-resolved transient absorption spectroscopy. The measurements were performed at room temperature and at 10 K. The combination of both ultrafast and steady-state optical spectroscopy methods at ambient and cryogenic temperatures allowed the detailed study of carotenoid (Car)-to-bacteriochlorophyll (BChl) as well BChl-to-BChl excitation energy transfer in the complex. The studies show that the dominant Cars rhodopin (N=11) and spirilloxanthin (N=13) do not play a significant role as supportive energy donors for BChl a. This is related with their photophysical properties regulated by long π-electron conjugation. On the other hand, such properties favor some of the Cars, particularly spirilloxanthin (N=13) to play the role of the direct quencher of the excited singlet state of BChl.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacteriochlorophylls / chemistry
  • Bacteriochlorophylls / physiology*
  • Carotenoids / chemistry*
  • Carotenoids / physiology
  • Chromatiaceae / chemistry*
  • Chromatiaceae / physiology
  • Cold Temperature
  • Energy Transfer
  • Kinetics
  • Light
  • Light-Harvesting Protein Complexes / chemistry*
  • Light-Harvesting Protein Complexes / isolation & purification
  • Photosynthesis / physiology
  • Spectrometry, Fluorescence / methods*
  • Temperature
  • Time Factors
  • Xanthophylls / chemistry
  • Xanthophylls / physiology

Substances

  • Bacteriochlorophylls
  • Light-Harvesting Protein Complexes
  • Xanthophylls
  • rhodovibrin
  • Carotenoids
  • rhodopin
  • spirilloxanthin