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A Consistent Model of Ultrafast Energy Transfer in Peridinin Chlorophyll-a Protein Using Two-Dimensional Electronic Spectroscopy and Förster Theory

Journal Article · · Journal of Physical Chemistry. B, Condensed Matter, Materials, Surfaces, Interfaces and Biophysical Chemistry
 [1];  [2];  [2];  [3];  [2]
  1. Princeton Univ., NJ (United States). Dept. of Chemistry; Princeton University
  2. Princeton Univ., NJ (United States). Dept. of Chemistry
  3. Macquarie Univ., Sydney NSW (Australia)
Solar light harvesting begins with electronic energy transfer in structurally complex light-harvesting antennae such as the peridinin chlorophyll-a protein from dinoflagellate algae. Peridinin chlorophyll-a protein is composed of a unique combination of chlorophylls sensitized by carotenoids in a 4:1 ratio, and ultrafast spectroscopic methods have previously been utilized in elucidating their energy transfer pathways and timescales. However, due to overlapping signals from various chromophores and competing pathways and timescales, a consistent model of intra-protein electronic energy transfer has been elusive. Here, we used broadband two-dimensional electronic spectroscopy, which alleviates the spectral congestion by dispersing excitation and detection wavelengths. Inter-chromophoric couplings appear as cross peaks in two-dimensional electronic spectra, and these spectral features were observed between the peridinin S2 states and chlorophyll-a Qx and Qy states. In addition, the inherently high time- and frequency-resolution of 2DES enabled accurate determination of the ultrafast energy transfer dynamics. Kinetic analysis near the peridinin S1 excited state absorption, which forms in 24 fs after optical excitation, reveals an ultrafast energy transfer pathway from the peridinin S2 state to the chlorophyll-a Qx state—a hitherto unconfirmed pathway critical for fast inter-chromophoric transfer. Lastly, we propose a model of ultrafast peridinin chlorophyll-a protein photophysics that (1) includes a conical intersection between peridinin S2 and S1 states in order to explain both the ultrafast peridinin S1 formation and the residual peridinin S2 population for energy transfer to chlorophyll-a, and (2) computationally- and experimentally-derived peridinin S2 site energies that support the observed ultrafast peridinin S2 to chlorophyll-a Qx energy transfer.
Research Organization:
Energy Frontier Research Centers (EFRC) (United States). Bioinspired Light-Escalated Chemistry (BioLEC); Princeton Univ., NJ (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22). Chemical Sciences, Geosciences & Biosciences Division
Grant/Contract Number:
SC0019370
OSTI ID:
1542564
Journal Information:
Journal of Physical Chemistry. B, Condensed Matter, Materials, Surfaces, Interfaces and Biophysical Chemistry, Journal Name: Journal of Physical Chemistry. B, Condensed Matter, Materials, Surfaces, Interfaces and Biophysical Chemistry Journal Issue: 30 Vol. 123; ISSN 1520-6106
Publisher:
American Chemical SocietyCopyright Statement
Country of Publication:
United States
Language:
English

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Figures / Tables (5)


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