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Biophys J, October 2000, p. 1695-1705, Vol. 79, No. 4

Excitation Transfer in the Peridinin-Chlorophyll-Protein of Amphidinium carterae

Ana Damjanovic', Thorsten Ritz, and Klaus Schulten

Department of Physics and Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801 USA

Peridinin-chlorophyll-protein (PCP) is a unique light-harvesting protein that uses carotenoids as its primary light-absorbers. This paper theoretically investigates excitation transfer between carotenoids and chlorophylls in PCP of the dinoflagellate Amphidinium carterae. Calculations based on a description of the electronic states of the participating chromophores and on the atomic level structure of PCP seek to identify the mechanism and pathways of singlet excitation flow. After light absorption the optically allowed states of peridinins share their electronic excitation in excitonic fashion, but are not coupled strongly to chlorophyll residues in PCP. Instead, a gateway to chlorophyll Qy excitations is furnished through a low-lying optically forbidden excited state, populated through internal conversion. Carbonyl group and non-hydrogen side groups of peridinin are instrumental in achieving the respective coupling to chlorophyll. Triplet excitation transfer to peridinins, mediated by electron exchange, is found to efficiently protect chlorophylls against photo-oxidation.

Biophys J, October 2000, p. 1695-1705, Vol. 79, No. 4
© 2000 by the Biophysical Society   0006-3495/00/10/1695/11  $2.00


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