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Cited by 1,072Spectroscopy and Quantum Chemical StudiesPhotochemistry and Electron Transfer StudiesPhotosynthetic Processes and Mechanisms

The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.

Long-lived quantum coherence in photosynthetic complexes at physiological temperature

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Panitchayangkoon, Gitt, Hayes, Dugan, Fransted, Kelly A., Caram, Justin R., Harel, Elad, Wen, Jianzhong, Blankenship, Robert E., Engel, Gregory S.·2010·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.1005484107PMC PMC2919932
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Abstract

Photosynthetic antenna complexes capture and concentrate solar radiation by transferring the excitation to the reaction center that stores energy from the photon in chemical bonds. This process occurs with near-perfect quantum efficiency. Recent experiments at cryogenic temperatures have revealed that coherent energy transfer—a wave-like transfer mechanism—occurs in many photosynthetic pigment-protein complexes. Using the Fenna–Matthews–Olson antenna complex (FMO) as a model system, theoretical studies incorporating both incoherent and coherent transfer as well as thermal dephasing predict that environmentally assisted quantum transfer efficiency peaks near physiological temperature; these studies also show that this mechanism simultaneously improves the robustness of the energy transfer process. This theory requires long-lived quantum coherence at room temperature, which never has been observed in FMO. Here we present evidence that quantum coherence survives in FMO at physiological temperature for at least 300 fs, long enough to impact biological energy transport. These data prove that the wave-like energy transfer process discovered at 77 K is directly relevant to biological function. Microscopically, we attribute this long coherence lifetime to correlated motions within the protein matrix encapsulating the chromophores, and we find that the degree of protection afforded by the protein appears constant between 77 K and 277 K. The protein shapes the energy landscape and mediates an efficient energy transfer despite thermal fluctuations.

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Metadata

Authors
Panitchayangkoon, G., Hayes, D., Fransted, K. A., Caram, J. R., Harel, E., Wen, J., Blankenship, R. E., & Engel, G. S.
Affiliations
  • University of Chicago (US)
  • Washington University in St. Louis (US)
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2010-07-06
Volume
107
Issue
29
Pages
12766-12770
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.1005484107
PMC
PMC2919932
OpenAlex
W2102296190
Cited by
1,072
References
33
Citations by year
2026: 39 · 2025: 41 · 2024: 42 · 2023: 34 · 2022: 39 · 2021: 47 · 2020: 50 · 2019: 61 · 2018: 66 · 2017: 71 · 2016: 83 · 2015: 86 · 2014: 93 · 2013: 94 · 2012: 103
FWCI
54.78
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • arXiv (Cornell University) (submittedVersion)
  • arXiv (Cornell University)
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
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
Keywords
quantum coherence, photosynthetic antenna complexes, Fenna-Matthews-Olson complex, coherent energy transfer, thermal dephasing, physiological temperature, energy transfer efficiency
MeSH terms
Protein Conformation, Quantum Theory, Temperature, Time Factors, Microscopy, Scanning Tunneling, Photosynthetic Reaction Center Complex Proteins

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