Abstract
In a previous paper (Hassan M Younis et al. Biotechnol Appl Biochem. “2002” 35: 9- 17)we have shown that the insecticide DDT exerts its action through its inhibition of the mitochondrial ATP synthase activity. Here I report on the kinetics and equilirium constants of the reaction between DDT and the purified enzyme in vitro. Analysis of the temperature dependence of kinetics and equilibrium constants allowed determination of the energetics of binding of DDT to the enzyme. The dissociation constant (Kd) for DDT bound to the enzyme was determined, and the changes in free energy, enthalpy and entropy that are associated with binding of DDT to The enzyme were all calculated. the significance of the results will be discussed in terms of a knowledge -based approach for development of better insecticides.
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