Abstract

The LH1 complexes were isolated from the purple photosynthetic bacterium Rhodospirillum rubrum strain S1. They were initially solubilized using LDAO and then purified in the presence of Triton X-100. The purified complexes were then either used directly or following an exchange into LDAO. Stark spectroscopy was applied to probe the electrostatic field around the bacteriochlorophyll a (BChl a) and carotenoid binding sites in the LH1 complexes surrounded by these two different surfactant molecules. Polarizabilty change (deltaalpha)) and dipole moment change (deltamicrom) upon photoexcitation were determined for the BChl a Q(y) band. Both of these parameters show smaller values in the presence of LDAO than in Triton X-100. This indicates that polar detergent molecules, like LDAO, affect the electrostatic environment around BChl a, and modify the nonlinear optical parameters (deltaalpha and deltamicrom values). The electrostatic field around the BChl a binding site, which is generated by the presence of LDAO, was determined to be |E ( L )| = approximately 3.9 x 10(5) [V/cm]. Interestingly, this kind of electrostatic effect was not observed for the carotenoid-binding site. The present study demonstrates a unique electrostatic interaction between the polar detergent molecules surrounding the LH1 complex and the Q(y) absorption band of BChl a that is bound to the LH1 complex.

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