Crystallization of the c14-rotor of the chloroplast ATP synthase reveals that it contains pigments.

The ATP synthase is one of the most important enzymes on earth as it couples the transmembrane electrochemical potential of protons to the synthesis of ATP from ADP and inorganic phosphate, providing the main ATP source of almost all higher life on earth. During ATP synthesis, stepwise protonation of a conserved carboxylate on each protein subunit of an oligomeric ring of 10-15 c-subunits is commonly thought to drive rotation of the rotor moiety (c(10-14)gammaepsilon) relative to stator moiety (alpha(3)beta(3)deltaab(2)). Here we report the isolation and crystallization of the c(14)-ring of subunit c from the spinach chloroplast enzyme diffracting as far as 2.8 A. Though ATP synthase was not previously known to contain any pigments, the crystals of the c-subunit possessed a strong yellow color. The pigment analysis revealed that they contain 1 chlorophyll and 2 carotenoids, thereby showing for the first time that the chloroplast ATP synthase contains cofactors, leading to the question of the possible roles of the functions of the pigments in the chloroplast ATP synthase.