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Biophys J, October 2000, p. 1706-1717, Vol. 79, No. 4

and
*Dipartimento Scientifico e Tecnologico, Università degli
Studi di Verona, Facoltà di Scienze, Strada LeGrazie 15, I-37134
Verona, Italy; and
Max Plank Institut fur Strahlenchemie,
Mülheim am der Ruhr, Stilftstrasse 34, Germany
The energy transfer rates between chlorophylls in the
light harvesting complex CP29 of higher plants at room temperature were calculated ab initio according to the Förster mechanism
(Förster T. 1948, Ann. Physik. 2:55-67).
Recently, the transition moment orientation of CP29 chlorophylls was
determined by differential linear dichroism and absorption spectroscopy
of wild-type versus mutant proteins in which single chromophores were
missing (Simonetto R., Crimi M., Sandonà D., Croce R., Cinque G.,
Breton J., and Bassi R. 1999. Biochemistry.
38:12974-12983). In this way the Qy transition energy and
chlorophyll a/b affinity of each binding site was
obtained and their characteristics supported by reconstruction of
steady-state linear dichroism and absorption spectra at room temperature. In this study, the spectral form of individual chlorophyll a and b ligands within the protein
environment was experimentally determined, and their extinction
coefficients were also used to evaluate the absolute overlap integral
between donors and acceptors employing the Stepanov relation for both
the emission spectrum and the Stokes shift. This information was used
to calculate the time-dependent excitation redistribution among CP29
chlorophylls on solving numerically the Pauli master equation of the
complex: transient absorption measurements in the (sub)picosecond time scale were simulated and compared to pump-and-probe experimental data
in the Qy region on the native CP29 at room temperature
upon selective excitation of chlorophylls b at 640 or
650 nm. The kinetic model indicates a bidirectional excitation transfer
over all CP29 chlorophylls a species, which is
particularly rapid between the pure sites A1-A2 and A4-A5. Chlorophylls
b in mixed sites act mostly as energy donors for
chlorophylls a, whereas site B5 shows high and
bidirectional coupling independent of the pigment hosted.
Biophys J, October 2000, p. 1706-1717, Vol. 79, No. 4
© 2000 by the Biophysical Society 0006-3495/00/10/1706/12 $2.00
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