Evidence map›Paper›PMID 21504741›Full record

ArticleBiophysical journal2011

Extracting the excitonic Hamiltonian of the Fenna-Matthews-Olson complex using three-dimensional third-order electronic spectroscopy.

Dugan Hayes, Gregory S Engel

Abstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Redox conditions correlated with vibronic coupling modulate quantum beats in photosynthetic pigment-protein complexes.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Multidimensional spectroscopy of photoreactivity.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  9. Article
  10. Conformation of self-assembled porphyrin dimers in liposome vesicles by phase-modulation 2D fluorescence spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Dugan HayesDepartment of Chemistry and James Franck Institute, University of Chicago, Chicago, Illinois, USA.
Gregory S Engel

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We extend traditional two-dimensional (2D) electronic spectroscopy into a third Fourier dimension without the use of additional optical interactions. By acquiring a set of 2D spectra evenly spaced in waiting time and dividing the area of the spectra into voxels, we can eliminate population dynamics from the data and transform the waiting time dimension into frequency space. The resultant 3D spectrum resolves quantum beating signals arising from excitonic coherences along the waiting frequency dimension, thereby yielding up to 2n-fold redundancy in the set of frequencies necessary to construct a complete set of n excitonic transition energies. Using this technique, we have obtained, to our knowledge, the first fully experimental set of electronic eigenstates for the Fenna-Matthews-Olson (FMO) antenna complex, which can be used to improve theoretical simulations of energy transfer within this protein. Whereas the strong diagonal peaks in the 2D rephasing spectrum of the FMO complex obscure all but one of the crosspeaks at 77 K, extending into the third dimension resolves 19 individual peaks. Analysis of the independently collected nonrephasing data provides the same information, thereby verifying the calculated excitonic transition energies. These results enable one to calculate the Hamiltonian of the FMO complex in the site basis by fitting to the experimental linear absorption spectrum.

Indexed as

ElectronsAbsorptionBacterial ProteinsChlorobiumEnergy TransferLight-Harvesting Protein ComplexesSpectrum AnalysisBacterial ProteinsFMO bacteriochlorophyll protein, BacteriaLight-Harvesting Protein Complexes

Identifiers

PMID21504741
PMCPMC3077693

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.