Abstract
The apparent K m value for inorganic phosphate (P i) of the chloroplastic ATPase has been measured under different conditions of light intensity, uncoupler concentration and energy-transfer inhibitor concentration. Systematic changes in the values were observed which were similar to but not identical with reported changes in the K m for ADP under similar conditions (Quick, W.P. and Mills, J.D. (1987) Biochim. Biophys. Acta 893, 197–207). Both sets of experimental data could be simulated using a mathematical model based on: (a) Michaelis-Menten kinetics of the ATPase with respect to ADP and P i; and (b) delocalised chemiosmotic energy coupling. We conclude that the changes observed in the K m are a result of systematic changes in the protonmotive force during the K m analysis.
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