Journal
NATURE CHEMISTRY
Volume 4, Issue 5, Pages 396-404Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEM.1302
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Funding
- Natural Sciences and Engineering Research Council of Canada
- US Air Force Office of Scientific Research [FA9550-10-1-0260]
- DARPA (QuBE)
- Australian Research Council
- US National Science Foundation [MCB-0519743, MCB-1021725]
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The effective absorption cross-section of a molecule (acceptor) can be greatly increased by associating it with a cluster of molecules that absorb light and transfer the excitation energy to the acceptor molecule. The basic mechanism of such light harvesting by Forster resonance energy transfer (FRET) is well established, but recent experiments have revealed a new feature whereby excitation is coherently shared among donor and acceptor molecules during FRET. In the present study, two-dimensional electronic spectroscopy was used to examine energy transfer at ambient temperature in a naturally occurring light-harvesting protein (PE545 of the marine cryptophyte alga Rhodomonas sp. strain CS24). Quantum beating was observed across a range of excitation frequencies. The shapes of those features in the two-dimensional spectra were examined. Through simulations, we show that two-dimensional electronic spectroscopy provides a probe of the adiabaticity of the free energy landscape underlying light harvesting.
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