ArticleNature chemistry2022
Observation of robust energy transfer in the photosynthetic protein allophycocyanin using single-molecule pump-probe spectroscopy.
Article in Nature chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 35 citations in OpenAlex.
- Unveiling long-range forces in light-harvesting proteins: Pivotal roles of temperature and light.Science advances · 2025Article
- Resonant Vibrational Enhancement of Downhill Energy Transfer in theThe journal of physical chemistry letters · 2024Article
- Solution-phase sample-averaged single-particle spectroscopy of quantum emitters with femtosecond resolution.Nature materials · 2024Article
- ApcE plays an important role in light-induced excitation energy dissipation in the Synechocystis PCC6803 phycobilisomes.Photosynthesis research · 2024Article
- Phycobilisome's Exciton Transfer Efficiency Relies on an Energetic Funnel Driven by Chromophore-Linker Protein Interactions.Journal of the American Chemical Society · 2023Article
- Beneficial effects of seaweed-derived components on metabolic syndrome via gut microbiota modulation.Frontiers in nutrition · 2023Review
- Real-Time Feedback-Driven Single-Particle Tracking: A Survey and Perspective.Small (Weinheim an der Bergstrasse, Germany) · 2022Review
- Facing the fluctuations.Nature chemistry · 2022Article
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4 authors at 2 institutions in 2 countries.
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Abstract
Photosynthetic organisms convert sunlight to electricity with near unity quantum efficiency. Absorbed photoenergy transfers through a network of chromophores positioned within protein scaffolds, which fluctuate due to thermal motion. The resultant variation in the individual energy transfer steps has not yet been measured, and so how the efficiency is robust to this variation has not been determined. Here, we describe single-molecule pump-probe spectroscopy with facile spectral tuning and its application to the ultrafast dynamics of single allophycocyanin, a light-harvesting protein from cyanobacteria. We disentangled the energy transfer and energetic relaxation from nuclear motion using the spectral dependence of the dynamics. We observed an asymmetric distribution of timescales for energy transfer and a slower and more heterogeneous distribution of timescales for energetic relaxation, which was due to the impact of the protein environment. Collectively, these results suggest that energy transfer is robust to protein fluctuations, a prerequisite for efficient light harvesting.
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