Thymoquinone Inhibits Escherichia coli ATP Synthase and Cell Growth |
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| Authors: | Zulfiqar Ahmad Thomas F. Laughlin Ismail O. Kady |
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| Affiliation: | 1Department of Biochemistry, Kirksville College of Osteopathic Medicine, A T Still University of Health Sciences, Kirksville, MO, 63501, United States of America;2Department of Chemistry, East Tennessee State University, Johnson City, TN, 37614, United States of America;University of Alabama at Birmingham, UNITED STATES |
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| Abstract: | We examined the thymoquinone induced inhibition of purified F1 or membrane bound F1FOE. coli ATP synthase. Both purified F1 and membrane bound F1FO were completely inhibited by thymoquinone with no residual ATPase activity. The process of inhibition was fully reversible and identical in both membrane bound F1Fo and purified F1 preparations. Moreover, thymoquinone induced inhibition of ATP synthase expressing wild-type E. coli cell growth and non-inhibition of ATPase gene deleted null control cells demonstrates that ATP synthase is a molecular target for thymoquinone. This also links the beneficial dietary based antimicrobial and anticancer effects of thymoquinone to its inhibitory action on ATP synthase. |
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