Most cited article - PubMed ID 26801214
Triplet-triplet energy transfer from chlorophylls to carotenoids in two antenna complexes from dinoflagellate Amphidinium carterae
The functions of both (bacterio) chlorophylls and carotenoids in light-harvesting complexes have been extensively studied during the past decade, yet, the involvement of BChl a high-energy Soret band in the cascade of light-harvesting processes still remains a relatively unexplored topic. Here, we present transient absorption data recorded after excitation of the Soret band in the LH2 complex from Rhodoblastus acidophilus. Comparison of obtained data to those recorded after excitation of rhodopin glucoside and B800 BChl a suggests that no Soret-to-Car energy transfer pathway is active in LH2 complex. Furthermore, a spectrally rich pattern observed in the spectral region of rhodopin glucoside ground state bleaching (420-550 nm) has been assigned to an electrochromic shift. The results of global fitting analysis demonstrate two more features. A 6 ps component obtained exclusively after excitation of the Soret band has been assigned to the response of rhodopin glucoside to excess energy dissipation in LH2. Another time component, ~ 450 ps, appearing independently of the excitation wavelength was assigned to BChl a-to-Car triplet-triplet transfer. Presented data demonstrate several new features of LH2 complex and its behavior following the excitation of the Soret band.
- Keywords
- Antenna complex, Carotenoids, Electrochromic shift, Energy transfer, Excess energy, LH2,
- MeSH
- Bacteriochlorophylls metabolism MeSH
- Beijerinckiaceae MeSH
- Glucosides MeSH
- Carotenoids * metabolism MeSH
- Light-Harvesting Protein Complexes * metabolism MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Bacteriochlorophylls MeSH
- Glucosides MeSH
- Carotenoids * MeSH
- rhodopin glucoside MeSH Browser
- Light-Harvesting Protein Complexes * MeSH
We have used time-resolved absorption and fluorescence spectroscopy with nanosecond resolution to study triplet energy transfer from chlorophylls to carotenoids in a protective process that prevents the formation of reactive singlet oxygen. The light-harvesting complexes studied were isolated from Chromera velia, belonging to a group Alveolata, and Xanthonema debile and Nannochloropsis oceanica, both from Stramenopiles. All three light-harvesting complexes are related to fucoxanthin-chlorophyll protein, but contain only chlorophyll a and no chlorophyll c. In addition, they differ in the carotenoid content. This composition of the complexes allowed us to study the quenching of chlorophyll a triplet states by different carotenoids in a comparable environment. The triplet states of chlorophylls bound to the light-harvesting complexes were quenched by carotenoids with an efficiency close to 100%. Carotenoid triplet states were observed to rise with a ~5 ns lifetime and were spectrally and kinetically homogeneous. The triplet states were formed predominantly on the red-most chlorophylls and were quenched by carotenoids which were further identified or at least spectrally characterized.
- Keywords
- Algae, Energy transfer, Light harvesting, Photoprotection, Photosynthesis, Transient spectroscopy,
- MeSH
- Anaerobiosis MeSH
- Time Factors MeSH
- Chlorophyll metabolism MeSH
- Spectrometry, Fluorescence MeSH
- Photochemical Processes * MeSH
- Stramenopiles metabolism MeSH
- Carotenoids metabolism MeSH
- Kinetics MeSH
- Chlorophyll Binding Proteins metabolism MeSH
- Light-Harvesting Protein Complexes metabolism MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Chlorophyll MeSH
- Carotenoids MeSH
- Chlorophyll Binding Proteins MeSH
- Light-Harvesting Protein Complexes MeSH