Inhibition of chloroplast CF1-ATPase by vanadate

Citations of this article
Mendeley users who have this article in their library.
Get full text


Inhibition of ATPase activity by vanadate, having K1 2of 0.5 mM, was demonstrated in the CF1-ATPase. The Ca2+-dependent ATPase activity of the isolated enzyme was inhibited in an allosteric manner by vanadate with a Hill coefficient of 3.19 ± 0.6. Vanadate also inhibited ATPase and Pi-ATP exchange activities of the chloroplast membrane-bound enzyme. Using51V NMR it was demonstrated that ATP caused partial release of about 1.87 equivalents while ADP caused additional binding of approximately 1.46 equivalents of vanadate, when added to a solution containing CF1equilibrated with vanadate. The relevance of these results to a possible involvement of a pentacovalent phosphate as transition state intermediate in the hydrolysis of ATP by CF1-ATPase is discussed. © 1992.




Carmeli, C., Tadmor, O., Lifshitz, Y., Ophir, R., & Carmeli, S. (1992). Inhibition of chloroplast CF1-ATPase by vanadate. FEBS Letters, 299(3), 227–230.

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free