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Biophys J, June 2001, p. 2843-2855, Vol. 80, No. 6
and
*Department of Physics and Astronomy, Vrije Universiteit, 1081 HV
Amsterdam, The Netherlands; and
School of Biological
Sciences, Macquarie University, NSW 2109, Australia
The peridinin chlorophyll-a protein (PCP)
of dinoflagellates differs from the well-studied light-harvesting
complexes of purple bacteria and green plants in its large (4:1)
carotenoid to chlorophyll ratio and the unusual properties of its
primary pigment, the carotenoid peridinin. We utilized ultrafast
polarized transient absorption spectroscopy to examine the flow of
energy in PCP after initial excitation into the strongly allowed
peridinin S2 state. Global and target analysis of the
isotropic and anisotropic decays reveals that significant excitation
(25-50%) is transferred to chlorophyll-a directly from
the peridinin S2 state. Because of overlapping positive and
negative features, this pathway was unseen in earlier single-wavelength experiments. In addition, the anisotropy remains constant and high in
the peridinin population, indicating that energy transfer from
peridinin to peridinin represents a minor or negligible pathway. The
carotenoids are also coupled directly to chlorophyll-a
via a low-lying singlet state S1 or the recently identified
SCT. We model this energy transfer time scale as 2.3 ± 0.2 ps, driven by a coupling of ~47 cm
1.
This coupling strength allows us to estimate that the peridinin S1/SCT donor state transition moment is ~3 D.
Biophys J, June 2001, p. 2843-2855, Vol. 80, No. 6
© 2001 by the Biophysical Society 0006-3495/01/06/2843/13 $2.00
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