Modulation by bicarbonate, phosphate, and maleate of the kinetics of adenosinetriphosphatase activity and of the binding of manganese ions to chloroplast coupling factor 1

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Abstract
Bicarbonate, maleate and phosphate modulate ATPase activity in coupling factor 1 from [lettuce] chloroplasts. Kinetic analysis of the changes in the ratio between the apparent Km with and without effectors indicated that the stimulation of the activity by bicarbonate was a result of a decrease in the Km for MnATP2-. The inhibition by phosphate resulted from a decrease in the Ki for free ATP as a competitive inhibitor at pH 8. The effectors did not change Vmax at this pH. However, at pH 6.5, both Km and Vmax of ATPase activity with MnATP2- were changed by maleate, yet the mode of inhibition by free ATP remained unaltered. In addition to decreasing the Km, bicarbonate induced a 10-fold decrease in the Kd for binding of Mn2+ at the 2 tight binding sites in the presence of ATP at pH 8. At pH 6.5, maleate also decreased both the Km for MnATP2- and the Kd for Mn2+ binding. A decrease in the Km of a substrate induced by an effector is likely to be a result of a decrease in the binding constant of the substrate. Apparently, 2 tight binding sites of Mn2+ exist at the active sites of the enzyme.

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