Multiscale model of light harvesting by photosystem II in plants
Open accessAbstract
Significance: Plants thrive in natural sunlight in part because photosystem II (PSII) flexibly captures sunlight. PSII is composed of pigment–protein complexes that densely pack the thylakoid membrane in chloroplasts. We explain the mechanisms underlying the high quantum efficiency of PSII light harvesting in ideal conditions using a quantum mechanical model of excitation energy transport in the membrane. We show that the diffusion length of excitation energy determines the way in which modifications to the membrane affect PSII’s, and ultimately a plant’s, photosynthetic efficiency. The model could be useful for developing artificial light-harvesting materials that are robust to the fluctuations inherent in natural sunlight and rationally engineered crops that achieve higher yields in adverse environments.
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The 2D tryptophan photoexcitation diffusion length of 6.64 nm is surprisingly high in microtubules given their structural roles and the chlorophyll a equivalent value of 20-80 nm.
“The two-dimensional tryptophan photoexcitation diffusion length of 6.64 nm is surprisingly high in microtubules, given that they are optimized to play structural roles in the cell and that the equivalent value for chlorophyll a, which is optimized for electronic energy transfer, is only 20–80 nm.”
From Electronic energy migration in microtubules (2023) · cites this paper as [23]
The 2D diffusion length in microtubules is comparable to that observed in some photosynthetic complexes and organic photovoltaic devices.
“Stern–Volmer analysis revealed that the 2D diffusion length of tryptophan photoexcitation in microtubules is comparable to that observed in some photosynthetic complexes23−25 and organic photovoltaic devices.45−47”
From Electronic energy migration in microtubules (2023) · cites this paper as [23]
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Electronic energy migration in microtubules
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- Authors
- Amarnath, K., Bennett, D. I. G., Schneider, A. R., & Fleming, G. R.
- Affiliations
- Harvard University (US)
- University of California, Berkeley (US)
- Lawrence Berkeley National Laboratory (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2016-01-19
- Volume
- 113
- Issue
- 5
- Pages
- 1156-1161
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC4747709
- OpenAlex
- W2269204374
- Cited by
- 88
- References
- 48
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 9 · 2023: 11 · 2022: 3 · 2021: 16 · 2020: 7 · 2019: 8 · 2018: 10 · 2017: 9 · 2016: 7
- FWCI
- 6.07
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- arXiv (Cornell University) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- U.S. Department of Energy (DE-AC02-05CH11231, DEAC03-76SF000098)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Spectroscopy and Quantum Chemical Studies
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Photochemistry and Electron Transfer Studies
- Keywords
- photosystem II, light harvesting, multiscale modeling, excitation energy transfer, diffusion length, excited-state delocalization, thylakoid membranes, quantum efficiency, non-photochemical quenching, high light stress, antenna complexes, photochemical yield
- MeSH terms
- Energy Transfer, Fluorescence, Photosynthesis, Plant Proteins, Thylakoids, Photosystem II Protein Complex
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