Cryo-EM structure of the Rhodospirillum rubrum RC-LH1 complex at 2.5Å

The reaction centre light-harvesting 1 (RC-LH1) complex is the core functional component of bacterial photosynthesis. We determined the cryo-electron microscopy (cryo-EM) structure of the RC-LH1 complex from Rhodospirillum rubrum at 2.5 Å resolution, which reveals a unique monomeric bacteriochlorophyll with a phospholipid ligand in the gap between the RC and LH1 complexes. The LH1 complex comprises a circular array of 16 αβ-polypeptide subunits that completely surrounds the RC, with a preferential binding site for a quinone, designated Q_P, on the inner face of the encircling LH1 complex. Quinols, initially generated at the RC Q_B site, are proposed to transiently occupy the Q_P site prior to traversing the LH1 barrier and diffusing to the cytochrome bc₁ complex. Thus, the Q_P site, which is analogous to other such sites in recent cryo-EM structures of RC-LH1 complexes, likely reflects a general mechanism for exporting quinols from the RC-LH1 complex.