Singlet and Triplet State Spectra and Dynamics of Structurally Modified Peridinins

The peridinin-chlorophyll a-protein (PCP) is a light-harvesting pigment protein complex found in many species of marine algae. It contains the highly substituted carotenoid peridinin and chlorophyll a, which together facilitate the transfer of absorbed solar energy to the photosynthetic reaction center. Photoexcited peridinin exhibits unorthodox spectroscopic and kinetic behavior for a carotenoid, including a strong dependence of the Si excited singlet state lifetime on solvent environment. This effect has been attributed to the presence of an intramolecular charge transfer (ICT) state in the molecule. The present work explores the effect of changing the extent of it-electron conjugation and attached functional groups on the nature of the ICT state of peridinin and how these factors affect the excited singlet and triplet state spectra and kinetics of the carotenoid. In this investigation three peridinin analogues denoted C-1-R-peridinin, C-1-peridinin, and D-1-peridinin were synthesized and studied using steady-state absorption and fluorescence techniques and ultrafast time-resolved transient absorption spectroscopy. The study explores the effect on the singlet and triplet state spectra and dynamics of removing the allene group from the peridinin structure and either replacing it with a rigid furanoid ring, replacing it with an epoxide group, or extending the polyene chain into the beta-ionylidine ring.