In vitro studies of the carotenoid peridinin, which is the primary pigment from the peridinin chlorophyll-a protein (PCP) light harvesting complex, showed a strong dependence on the lifetime of the peridinin lowest singlet excited state on solvent polarity. This dependence was attributed to the presence of an intramolecular charge transfer (ICT) state in the peridinin excited state manifold. The ICT state was also suggested to be a crucial factor in efficient peridinin to Chl-a energy transfer in the PCP complex. Here we extend our studies of peridinin dynamics to reconstituted PCP complexes, in which Chl-a was replaced by different chlorophyll species (Chl-b, acetyl Chl-a, Chl-d and BChl-a). Reconstitution of PCP with different Chl species maintains the energy transfer pathways within the complex, but the efficiency depends on the chlorophyll species. In the native PCP complex, the peridinin S1/ICT state has a lifetime of 2.7 ps, whereas in reconstituted PCP complexes it is 5.9 ps (Chl-b) 2.9 ps (Chl-a), 2.2 ps (acetyl Chl-a), 1.9 ps (Chl-d), and 0.45 ps (BChl-a). Calculation of energy transfer rates using the Förster equation explains the differences in energy transfer efficiency in terms of changing spectral overlap between the peridinin emission and the absorption spectrum of the acceptor. It is proposed that the lowest excited state of peridinin is a strongly coupled S1/ICT state, which is the energy donor for the major energy transfer channel. The significant ICT character of the S 1/ICT state in PCP enhances the transition dipole moment of the S1/ICT state, facilitating energy transfer to chlorophyll via the Förster mechanism. In addition to energy transfer via the S 1/ICT, there is also energy transfer via the S2 and hot S1/ICT states to chlorophyll in all reconstituted PCP complexes.