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Updated: Oct 2, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Published on: September 14, 2014
alpha, beta-Bidentate CrADP abolishes the negative cooperativity of yeast mitochondrial F1-ATPase
Abstract:
The hydrolysis of MgATP and MgITP by mitochondrial F1-ATPase from Saccharomyces cerevisiae is competitively inhibited by alpha, beta-CrADP, alpha, beta, gamma-CrATP and beta, gamma-CrATP. The apparent K1 values of the three complexes are in the range of the half-saturating MgATP concentration. The negative cooperativity (nH = 0.7) of MgATP hydrolysis is totally abolished by alpha, beta-CrADP (nH = 1.0), while it is not affected by the CrATP. It is concluded that alpha, beta-CrADP binds exclusively at the regulatory site and that CrATP binds exclusively to the catalytic site.
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