Singlet and triplet energy transfer in the peridinin-chlorophyll a protein from Amphidinium carterae

James A. Bautista, RG Hiller, FP Sharples, David Gosztola, Michael R. Wasielewski, Harry A. Frank

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Abstract

The spectroscopic properties of peridinin in solution, and the efficiency and dynamics of energy transfer from peridinin to chlorophyll a in the peridinin-chlorophyll-protein (PCP) from Amphidinium carterae, were studied by steady-state absorption, fluorescence, fluorescence excitation, and fast transient optical spectroscopy. Steady-state measurements of singlet energy transfer from peridinin to chlorophyll revealed an 88 +/- 2% efficiency. Fast-transient absorption experiments showed that the excited S-1 state of peridinin decayed in 13.4 +/- 0.6 ps in methanol and 3.1 +/- 0.3 ps in the PCP complex after direct excitation of the carotenoid. The onset of the bleaching of the chlorophyll absorption band at 672 nm, signifying the arrival of the excitation from the carotenoid, occurred in 3.2 +/- 0.3 ps. These data show that the primary route of energy transfer from peridinin to chlorophyll in the PCP complex is through the S1 state of peridinin. Nanosecond time-resolved transient optical, spectroscopy revealed that chlorophyll triplet states are efficiently quenched by peridinin whose triplet state subsequently decays with a lifetime of 10 +/- 1 mu s in the PCP complex. Close association between the peridinins and chlorophylls, which is clearly evident in the 3-D structure of the PCP complex, along with proper alignment of pigments and energy state matching are responsible for the high efficiencies of the photochemical processes.

Original languageEnglish
Pages (from-to)2267-2273
Number of pages7
JournalJournal of Physical Chemistry A
Volume103
Issue number14
Publication statusPublished - 8 Apr 1999

Keywords

  • LIGHT-HARVESTING COMPLEX
  • A-PROTEIN
  • PHOTOSYNTHETIC BACTERIA
  • MOLECULAR-STRUCTURE
  • CRYSTAL-STRUCTURE
  • CAROTENOIDS
  • DYNAMICS
  • RELAXATION
  • POLYENES
  • B800-850

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