The H+/ATP ratio of the ATP synthase from the cyanobacterium Synechococcus 6716 varies with growth temperature and light intensity

The proton translocation stoichiometry (H+/ATP ratio) and other bioenergetic features were investigated in membrane vesicles from the moderately thermophile Synechococcus 6716 grown at 38 degrees C and 50 degrees C with saturating light intensity, and at 38 degrees C with limiting light intensity. At 50 degrees C growth is slower but proceeds to a higher cell density than at 38 degrees C. Increasing the growth temperature from 38 degrees C to 50 degrees C resulted in an altered membrane fatty acid composition, with increased length and saturation of the acyl chains. At 38 degrees C and lower light intensity chain length was somewhat decreased and saturation increased to a small extent. Membrane vesicles from cells grown at 50 degrees C performed cyclic photophosphorylation at lower light intensities and lower threshold Delta<(mu)over bar>(H)+ than vesicles from cells, grown at 38 degrees C. The 50 degrees C vesicles also displayed a diminished light-induced proton uptake, but ATP synthesis activity and the attained Delta G(p), remained constant. Moreover, ATP synthesis became more resistant to uncoupling. From acid-base transition induced ATP synthesis experiments the H+/ATP ratios were determined to be 3.9, 3.1 and 3.3 for membrane vesicles from cells grown at 50 degrees C, 38 degrees C and light-limited 38 degrees C, respectively. In vesicles from cells grown at 50 degrees C, ATP hydrolysis is inhibited by a lower valinomycin-induced K+-diffusion potential than in vesicles from cells grown at 38 degrees C. A molecular mechanism to explain changes in H+/ATP as well as the physiological implications are discussed.