Form follows function -- how PufX increases the efficiency of the light-harvesting complexes of Rhodobacter sphaeroides

Abstract

Some species of purple bacteria as, e.g., Rhodobacter sphaeroides contain the protein PufX. Concurrently, the light harvesting complexes 1 (LH1) form dimers of open rings. In mutants without PufX, the LH1s are closed rings and photosynthesis breaks down, because the ubiquinone exchange at the reaction center is blocked. Thus, PufX is regarded essential for quinone exchange. In contrast to this view, which implicitly treats the LH1s as obstacles to photosynthesis, we propose that the primary purpose of PufX is to improve the efficiency of light harvesting by inducing the LH1 dimerization. Calculations with a dipole model, which compare the photosynthetic efficiency of various configurations of monomeric and dimeric core complexes, show that the dimer can absorb photons directly into the RC about 30% more efficient, when related to the number of bacteriochlorophylls, but that the performance of the more sophisticated dimeric LH1 antenna degrades faster with structural perturbations. The calculations predict an optimal orientation of the reaction centers relative to the LH1 dimer, which agrees well with the experimentally found configuration. For the increased required rigidity of the dimer additional modifications of the LH1 subunits are necessary, which would lead to the observed ubiquinone blockage, when PufX is missing.