As a model of photosynthetic unit (PSU), self-assembled aggregates of pigment-protein complexes from photosynthetic bacteria were prepared in a lipid bilayer by reconstitution of the light-harvesting 2 (LH2) complex and light-harvesting 1-reaction center (LH1-RC) complex through detergent removal of their micelles in the presence of lipids. By performing polarization-controlled fluorescence and fluorescence-excitation spectroscopy on single aggregates at a temperature of 5 K, the composition of individual aggregates was determined and excitation energy transfer (EET) between constituent complexes was observed. LH2 and LH1-RC from a bacterium, Rhodobacter (Rb.) sphaeroides, were found to form a trimeric aggregate in which EET takes place from one LH2 to two LH1-RCs. In contrast, a heterodimer of LH2 and LH1-RC in which EET works was found to assemble from a combination of complexes of different bacterial species, that is, LH2 from Rb. sphaeroides and LH1-RC from Rhodopseudomonas (Rps.) palustris.
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