Beschreibung:
<jats:p><jats:bold>A<jats:sc>bstract</jats:sc>: </jats:bold> In steady‐state conditions and for concentrations of the K<jats:sup>+</jats:sup>‐congener Rb<jats:sup>+</jats:sup> less than 2.5 mM, Rb<jats:sup>+</jats:sup>‐dependent ATPase activity is significantly higher than the steady‐state rate of breakdown of Rb<jats:sup>+</jats:sup>‐occluded states, a discrepancy that disappears at sufficiently high [Rb<jats:sup>+</jats:sup>]. Direct experimental evidence is provided that supports the explanation that the binding of a single Rb<jats:sup>+</jats:sup> to the phosphoenzyme conformer <jats:italic>E</jats:italic><jats:sub>2</jats:sub>P accelerates dephosphorylation without leading to the occlusion of the cation.</jats:p>