ArticlePhysical chemistry chemical physics : PCCP2023
Living on the edge: light-harvesting efficiency and photoprotection in the core of green sulfur bacteria.
Article in Physical chemistry chemical physics : PCCP, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 15 citations in OpenAlex.
- Relation between Structure and Functionality in Photosynthetic Antenna Complex of Green Sulfur Bacteria: Efficiency under Natural Sunlight Pumping.The journal of physical chemistry. B · 2026Article
- Light harvesting mechanism of the multi-pigment reaction center with three chlorophyll species adapted to both visible and far-red light.Photosynthesis research · 2026Article
- Nuclear quantum effects slow down the energy transfer in biological light-harvesting complexes.Science advances · 2025Article
- A Simple Expression for the Screening of Excitonic Couplings between Chlorophylls as Inferred for Photosystem I Trimers.International journal of molecular sciences · 2024Article
- Supramolecular chirality in self-assembly of zinc protobacteriochlorophyll-d analogs possessing enantiomeric esterifying groups.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2024Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
Photosynthetic green sulfur bacteria are able to survive under extreme low light conditions. Nevertheless, the light-harvesting efficiencies reported so far, in particular for Fenna-Matthews-Olson (FMO) protein-reaction center complex (RCC) supercomplexes, are much lower than for photosystems of other species. Here, we approach this problem with a structure-based theory. Compelling evidence for a light-harvesting efficiency around 95% is presented for native (anaerobic) conditions that can drop down to 47% when the FMO protein is switched into a photoprotective mode in the presence of molecular oxygen. Light-harvesting bottlenecks are found between the FMO protein and the RCC, and the antenna of the RCC and its reaction center (RC) with forward energy transfer time constants of 39 ps and 23 ps, respectively. The latter time constant removes an ambiguity in the interpretation of time-resolved spectra of RCC probing primary charge transfer and provides strong evidence for a transfer-to-the trap limited kinetics of excited states. Different factors influencing the light-harvesting efficiency are investigated. A fast primary electron transfer in the RC is found to be more important for a high efficiency than the site energy funnel in the FMO protein, quantum effects of nuclear motion, or variations in the mutual orientation between the FMO protein and the RCC.
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