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. Author manuscript; available in PMC: 2014 Jul 9.
Published in final edited form as: Biochemistry. 2013 Jun 25;52(27):10.1021/bi4004364. doi: 10.1021/bi4004364

FIGURE 6. Correlation of the strong-to-weak transition of the NBP and the ATPase rate as a function of Mg.

FIGURE 6

A, The equilibrium constant (Kpocket) of the strong-to-weak transition of the NBP is plotted as a function of free Mg. B, The rates of the NBP transitioning into the weak ADP binding state (k−pocket), ligand release (k−ligand) and the ATPase rate (kcat) are plotted as a function of free Mg. There is a strong correlation between the rate limiting transition of the NBP into the weak ADP binding state and the ATPase rates at all free Mg concentrations. Data are fit to Eq. 14. C, The van’t Hoff plots of Kligand measured in the presence (2 mM and 10 mM MgCl2) and absence of Mg (4 mM EDTA). The thermodynamic parameters are summarized in Table 3.