Purple bacteria possess two ring-shaped protein complexes, light-harvesting 1 (LH1) and 2 (LH2), both of which function as antennas for solar energy utilization for photosynthesis but exhibit distinct absorption properties. The two antennas have differing amounts of bacteriochlorophyll (BChl) a; however, their significance in spectral tuning remains elusive. Here, we report a high-precision evaluation of the physicochemical factors contributing to the variation in absorption maxima between LH1 and LH2, namely, BChl a structural distortion, protein electrostatic interaction, excitonic coupling, and charge transfer (CT) effects, as derived from detailed spectral calculations using an extended version of the exciton model, in the model purple bacterium Rhodospirillum rubrum. Spectral analysis confirmed that the electronic structure of the excited state in LH1 extended to the BChl a 16-mer. Further analysis revealed that the LH1-specific redshift (∼61% in energy) is predominantly accounted for by the CT effect resulting from the closer inter-BChl distance in LH1 than in LH2. Our analysis explains how LH1 and LH2, both with chemically identical BChl a chromophores, use distinct physicochemical effects to achieve a progressive redshift from LH2 to LH1, ensuring efficient energy transfer to the reaction center special pair.