Enrichment of the inner mitochondrial membrane with cholesterol induces an increase in ATPase activity with a decrease in the Km for ATP. Cholesterol also abolishes the discontinuity normally found in the Arrhenius plot of ATPase activity. Since no change is detected in the rate of proton translocation through the ATPase membrane sector, it is concluded that cholesterol incorporation induces changes in the hydrolytic step of ATPase via a conformational change transmitted from the membrane sector to the catalytic sector F1.
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Rindina et al. (1986) studied this question.
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