Abstract
There have been several reports that the apparent Michaelis Menton constant (Km) of the chloroplastic ATPase (CF0-CF1) for its substrate ADP varies according to the experimental conditions (1–3); this has also been observed in liver submitochondrial particles (4,5). Reduction of the rate of ATP synthesis by lowering the light intensity (1–3) or by adding an electron transport inhibitor (2) was shown to decrease the apparent Km for ADP. However, reduction of the rate of ATP synthesis using an uncoupler elevated the apparent Km for ADP (1,3). These results have been interpreted in several ways and used as evidence to support models of ATP synthesis involving a direct activation of CF0-CF1 by ΔμH+ (2,4,5) or by electron transport (1,3).
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