Exciton delocalization and energy transport mechanisms in R-phycoerythrin

Energy transport mechanisms in R-Phycoerythrin (RPE), a light harvesting protein located at the top of the phycobilisome antenna in red algae, are investigated using nonlinear optical spectroscopies and theoretical models. The RPE hexamer possesses a total of 30 bilin pigments, which can be subdivided into three classes based on their molecular structures and electronic resonance frequencies. Of particular interest to this study is the influence of exciton delocalization on the real-space paths traversed by photoexcitations as they concentrate on the lowest energy pigment sites. Transient grating measurements show that significant nuclear relaxation occurs at delay times less than 100 fs, whereas energy transport spans a wide range of time scales depending on the proximity of the initial and final states involved in the process. The fastest energy transport dynamics within the RPE complex are close to 1 ps; however, evidence for sub-100 fs exciton self-trapping is also obtained. In addition, photon echo experiments reveal vibronic interactions with overdamped and underdamped nuclear modes. To establish signatures of exciton delocalization, energy transport is simulated using both modified Redfield and Förster theories, which respectively employ delocalized and localized basis states. We conclude that exciton delocalization occurs between six pairs of phycoerythrobilin pigments (i.e., dimers) within the protein hexamer. It is interesting that these dimers are bound in locations analogous to the well-studied phycocyanobilin dimers of cyanobacterial allophycocyanin and c-phycocyanin in which wave function delocalization is also known to take hold. Strong conclusions regarding the electronic structures of the remaining pigments cannot be drawn based on the present experiments and simulations due to overlapping resonances and broad spectroscopic line widths, which prevent the resolution of dynamics at particular pigment sites.