Origin of Long-Lived Coherences in Light-Harvesting Complexes
Open accessAbstract
A vibronic exciton model is applied to explain the long-lived oscillatory features in the two-dimensional (2D) electronic spectra of the Fenna-Matthews-Olson (FMO) complex. Using experimentally determined parameters and uncorrelated site energy fluctuations, the model predicts oscillations with dephasing times of 1.3 ps at 77 K, which is in a good agreement with the experimental results. These long-lived oscillations originate from the coherent superposition of vibronic exciton states with dominant contributions from vibrational excitations on the same pigment. The oscillations obtain a large amplitude due to excitonic intensity borrowing, which gives transitions with strong vibronic character a significant intensity despite the small Huang-Rhys factor. Purely electronic coherences are found to decay on a 200 fs time scale.
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The smooth background is due mostly to the protein environment and noise processes from solvents.
“As we will see later the smooth background is due mostly to the protein environment as well as noise processes originating from solvents while the sharp features tend to originate from long-lived vibrations that belong to molecules that are held within the protein scaffold [26, 27].”
From Vibrations, quanta and biology (2013) · cites this paper as [27]
The sharp features tend to originate from long-lived vibrations that belong to molecules held within the protein scaffold.
“As we will see later the smooth background is due mostly to the protein environment as well as noise processes originating from solvents while the sharp features tend to originate from long-lived vibrations that belong to molecules that are held within the protein scaffold [26, 27].”
From Vibrations, quanta and biology (2013) · cites this paper as [27]
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- Authors
- Christensson, N., Kauffmann, H. F., Pullerits, T., & Mančal, T.
- Affiliations
- University of Vienna (AT)
- Lund University (SE)
- Charles University (CZ)
- Corresponding author
- Mančal, Tomáš
- Venue
- The Journal of Physical Chemistry B
- Publisher
- American Chemical Society (ACS)
- Published
- 2012-06-14
- Volume
- 116
- Issue
- 25
- Pages
- 7449-7454
- ISSN
- 1520-5207 (ISSN-L)
- 1520-6106
- PMC
- PMC3789255
- OpenAlex
- W2036168248
- Cited by
- 415
- References
- 32
- Citations by year
- 2026: 17 · 2025: 6 · 2024: 14 · 2023: 12 · 2022: 25 · 2021: 19 · 2020: 19 · 2019: 28 · 2018: 41 · 2017: 44 · 2016: 32 · 2015: 49 · 2014: 45 · 2013: 45 · 2012: 18
- FWCI
- 25.95
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- The Journal of Physical Chemistry B (publishedVersion, other-oa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- arXiv (Cornell University) (submittedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Topics
- 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
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Strong Light-Matter Interactions
- Keywords
- long-lived coherence, light-harvesting complexes, Fenna-Matthews-Olson complex, two-dimensional electronic spectra, dephasing, Huang-Rhys factor, vibrational excitation, electronic coherence
- MeSH terms
- Bacterial Proteins, Electrons, Models, Chemical, Models, Molecular, Quantum Theory, Chlorobium, Light-Harvesting Protein Complexes
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