Atomic force microscopic analysis of the light-harvesting complex 2 from purple photosynthetic bacterium Thermochromatium tepidum

Structural information on the circular arrangements of repeating pigment–polypeptide subunits in antenna proteins of purple photosynthetic bacteria is a clue to a better understanding of molecular mechanisms for the ring-structure formation and efficient light harvesting of such antennas. Here, we have analyzed the ring structure of light-harvesting complex 2 (LH2) from the thermophilic purple bacterium Thermochromatium tepidum ( tepidum -LH2) by atomic force microscopy. The circular arrangement of the tepidum -LH2 subunits was successfully visualized in a lipid bilayer. The average top-to-top distance of the ring structure, which is correlated with the ring size, was 4.8 ± 0.3 nm. This value was close to the top-to-top distance of the octameric LH2 from Phaeospirillum molischianum ( molischianum -LH2) by the previous analysis. Gaussian distribution of the angles of the segments consisting of neighboring subunits in the ring structures of tepidum -LH2 yielded a median of 44°, which corresponds to the angle for the octameric circular arrangement (45°). These results indicate that tepidum -LH2 has a ring structure consisting of eight repeating subunits. The coincidence of an octameric ring structure of tepidum -LH2 with that of molischianum -LH2 is consistent with the homology of amino acid sequences of the polypeptides between tepidum -LH2 and molischianum -LH2.