ArticleThe journal of physical chemistry letters2020
Static Disorder in Excitation Energies of the Fenna-Matthews-Olson Protein: Structure-Based Theory Meets Experiment.
Article in The journal of physical chemistry letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Minimization of Disorder as a Key Design Principle for Natural Sizes of Light Harvesting 2 Complexes.The journal of physical chemistry letters · 2026Article
- Consistent and Generalizable Effective Model Hamiltonian Framework for Studying Nonadiabatic Dynamics in the Condensed Phase.Journal of chemical theory and computation · 2025Review
- Living on the edge: light-harvesting efficiency and photoprotection in the core of green sulfur bacteria.Physical chemistry chemical physics : PCCP · 2023Article
- Multiple Facets of Modeling Electronic Absorption Spectra of Systems in Solution.ACS physical chemistry Au · 2023Review
- Towards a quantitative description of excitonic couplings in photosynthetic pigment-protein complexes: quantum chemistry driven multiscale approaches.Physical chemistry chemical physics : PCCP · 2022Article
- Quantum-Classical Approach for Calculations of Absorption and Fluorescence: Principles and Applications.Journal of chemical theory and computation · 2021Article
- Photosynthesis tunes quantum-mechanical mixing of electronic and vibrational states to steer exciton energy transfer.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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Authors and funding
8 authors.
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Abstract
Inhomogeneous broadening of optical lines of the Fenna-Matthews-Olson (FMO) light-harvesting protein is investigated by combining a Monte Carlo sampling of low-energy conformational substates of the protein with a quantum chemical/electrostatic calculation of local transition energies (site energies) of the pigments. The good agreement between the optical spectra calculated for the inhomogeneous ensemble and the experimental data demonstrates that electrostatics is the dominant contributor to static disorder in site energies. Rotamers of polar amino acid side chains are found to cause bimodal distribution functions of site energy shifts, which can be probed by hole burning and single-molecule spectroscopy. When summing over the large number of contributions, the resulting distribution functions of the site energies become Gaussians, and the correlations in site energy fluctuations at different sites practically average to zero. These results demonstrate that static disorder in the FMO protein is in the realm of the central limit theorem of statistics.
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