We examined the thymoquinone induced inhibition of purified F1 or membrane bound F1FO E. 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.
Thymoquinone Inhibits Escherichia coli ATP Synthase and Cell Growth
Zulfiqar Ahmad,T. F. Laughlin,Ismail O. Kady
Published 2015 in PLoS ONE
ABSTRACT
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- Publication year
2015
- Venue
PLoS ONE
- Publication date
2015-05-21
- Fields of study
Biology, Medicine, Chemistry
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- Source metadata
Semantic Scholar, PubMed
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