Exciton interactions in the light-harvesting antenna of photosynthetic bacteria studied with triplet-singlet spectroscopy and singlet-triplet annihilation on the B820 subunit form of Rhodospirillum rubrum

The pigment-protein complex, B820, isolated from the long-wavelength antenna (LH-1) of the photosynthetic purple bacterium Rhodospirillum rubrum was studied with polarized nanosecond laser spectroscopy. The polarized triplet (T)-singlet (S) spectrum was obtained at 77 K. The spectrum is significantly different from the T-S spectrum of monomeric BChl a, and can be explained by assuming that upon excitation the absorption band at 825 nm, which is due to a dimeric pair of BChl a molecules, disappears from the absorption spectrum, and is replaced by a monomer absorption band peaking at 809 nm. From the energy-dependence of the triplet yield, the high polarization of the bleaching, and the absence of singlet-triplet quenching we conclude that the B820 complex contains only one dimer of interacting BChl a molecules.