ArticleBiophysical journal2009
Low light adaptation: energy transfer processes in different types of light harvesting complexes from Rhodopseudomonas palustris.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 39 citations in OpenAlex.
- Article
- Cryo-EM structures of light-harvesting 2 complexes fromProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Effects of low-molecular-weight polyols on the hydration status of the light-harvesting complex 2 from Rhodobacter sphaeroides 2.4.1.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021Article
- Article
- The molecular mechanisms of light adaption in light-harvesting complexes of purple bacteria revealed by a multiscale modeling.Chemical science · 2019Article
- Simulating Fluorescence-Detected Two-Dimensional Electronic Spectroscopy of Multichromophoric Systems.The journal of physical chemistry. B · 2019Article
- Spatially-resolved fluorescence-detected two-dimensional electronic spectroscopy probes varying excitonic structure in photosynthetic bacteria.Nature communications · 2018Article
- Energy transfer in purple bacterial photosynthetic units from cells grown in various light intensities.Photosynthesis research · 2018Article
- Dark States in the Light-Harvesting complex 2 Revealed by Two-dimensional Electronic Spectroscopy.Scientific reports · 2016Article
- Essential Genome of the Metabolically Versatile Alphaproteobacterium Rhodopseudomonas palustris.Journal of bacteriology · 2015Article
- Elementary Energy Transfer Pathways in Allochromatium vinosum Photosynthetic Membranes.Biophysical journal · 2015Article
- Statistical considerations on the formation of circular photosynthetic light-harvesting complexes from Rhodopseudomonas palustris.Photosynthesis research · 2014Article
- Differential assembly of polypeptides of the light-harvesting 2 complex encoded by distinct operons during acclimation of Rhodobacter sphaeroides to low light intensity.Photosynthesis research · 2012Article
- Tracking energy transfer between light harvesting complex 2 and 1 in photosynthetic membranes grown under high and low illumination.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Differential assembly of polypeptides of the light-harvesting 2 complex encoded by distinct operons during acclimation of Rhodobacter sphaeroides to low light intensity.Photosynthesis research · 2011Article
- Direct visualization of exciton reequilibration in the LH1 and LH2 complexes of Rhodobacter sphaeroides by multipulse spectroscopy.Biophysical journal · 2011Article
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8 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Energy transfer processes in photosynthetic light harvesting 2 (LH2) complexes isolated from purple bacterium Rhodopseudomonas palustris grown at different light intensities were studied by ground state and transient absorption spectroscopy. The decomposition of ground state absorption spectra shows contributions from B800 and B850 bacteriochlorophyll (BChl) a rings, the latter component splitting into a low energy and a high energy band in samples grown under low light (LL) conditions. A spectral analysis reveals strong inhomogeneity of the B850 excitons in the LL samples that is well reproduced by an exponential-type distribution. Transient spectra show a bleach of both the low energy and high energy bands, together with the respective blue-shifted exciton-to-biexciton transitions. The different spectral evolutions were analyzed by a global fitting procedure. Energy transfer from B800 to B850 occurs in a mono-exponential process and the rate of this process is only slightly reduced in LL compared to high light samples. In LL samples, spectral relaxation of the B850 exciton follows strongly nonexponential kinetics that can be described by a reduction of the bleach of the high energy excitonic component and a red-shift of the low energetic one. We explain these spectral changes by picosecond exciton relaxation caused by a small coupling parameter of the excitonic splitting of the BChl a molecules to the surrounding bath. The splitting of exciton energy into two excitonic bands in LL complex is most probably caused by heterogenous composition of LH2 apoproteins that gives some of the BChls in the B850 ring B820-like site energies, and causes a disorder in LH2 structure.
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