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the aim of the work was to study the reverse ph-dependent regulation of the enzymatic activity of the catalytic part of AtP synthase (ec 3.6.3.14) of chloroplast – coupling factor cF1. It was shown that the short-term incubation of isolated cF1 in the media with ph 4.5 or 3.5 leads to inactivation of ca 2+-AtPase, which is rapidly (t1/2 ~ 1 min) restored in the medium containing 0.5-10 mm bicarbonate at ph 7.8. After acid treatment, the rate of mg2+-ATPase reaction was also stimulated in the presence of 1 mM bicarbonate (рН 7.8; 37 °С). The increase in Ca2+and mg2+-АТР activity of CF1 associated with the addition of Nahco3 solution was completely eliminated after the introduction of 50 mM acetazolamide – a specific inhibitor of carbonic anhydrase. the obtained results suggest the existence of the bound bicarbonate in the cF1 structure, which apparently participates in proton transfer.

Reversible pH-dependent activation/inactivation of CF(1)-ATPase of spinach chloroplasts