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December 1, 1988Journal of Biological ChemistryOpen Access

Catalytic site occupancy during ATP hydrolysis by MF1-ATPase. Evidence for alternating high affinity sites during steady-state turnover.

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Authors

David CunninghamDavid CunninghamRutgers, The State University of New JerseyRCRichard L. CrossSUNY Upstate Medical University

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Cunningham et al. (1988) studied this question.

synapsesocial.com/papers/6a83fbdd4f77243e16b05f79https://doi.org/10.1016/s0021-9258(18)37360-5
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1On the rate of F1‐ATPase turnover during ATP hydrolysis by the single catalytic site Evidence that hydrolysis with a slow rate of product release does not occur at the alternating active site1987 · 17 citations
  2. 2Defective proton ATPase of uncA mutants of Escherichia coli. 5'-adenylyl 5'-imidodiphosphate binding and ATP hydrolysis1984 · 87 citations
  3. 3The effect of phosphate on light-induced exchange of ADP at the tight nucleotide binding site of CF1.1980 · 13 citations
  4. 4Adenine nucleotide binding sites on beef heart F1-ATPase. Asymmetry and subunit location.1987 · 94 citations