| Enormous numbers and varieties of experiments have been performed to elucidate the mechanisms of photosynthesis. Within the last twenty years, a host of new studies were enabled by the techniques of ultrafast laser spectroscopy. This work continues to explore the exchange of energy on the picosecond and even the femtosecond regime. Yet in even the relatively simple and determined structure of the photosynthetic centers in the bacteria Rhodobacter sphaeroides, the mechanisms and energetics are unclear. The early events in photosynthesis allow energy trapping through resonance energy transfer and charge separation, in what appears to be a mixture of classical and quantum mechanical motion with strong interactions with the surrounding environment.; The technique of transient thermal grating spectroscopy offers unique insight into the mechanisms of energy relaxation in photosynthesis. A pair of laser pulse are tuned to the excitation wavelength and crossed inside the sample. The resulting pattern of interference drives excitation and the subsequent relaxation forms a density grating which diffracts a time-delayed third beam. Thus the energies and the rates of motion may be discerned.; The peripheral light harvesting antenna (LH2) is composed of polypeptides that coordinate rings of bacteriochlorophyll. Upon excitation, energy migrates around the ring until intra-ring transfer may take place. Samples of LH2 were purified and studied. While characteristic times of energy release were determined, a volume change due to solvent interaction was found as well.; In the membrane spanning protein known as the reaction center, the energy of the light harvesting rings is ultimately transferred to a pair of chlorophyll. From here, the energy is localized onto an electron, which rapidly (picoseconds) transfers to other active pigments. Samples of wild-type and the mutated (M)214H reaction centers were purified and examined. By studying the temperature dependence of the signals, the free energy was determined as a function of time. Additionally, volume changes due to solvent-protein interaction were determined. |
