Binding of hydrogen ions

Binding of Hydrogen Ions and Magnesium Ions by Adenosine Triphosphate... 

BINDING OF HYDROGEN IONS AND MAGNESIUM IONS BY ADENOSINE TRIPHOSPHATE... 

Since it is possible to calculate the mole fractions of the various species of ATP at a specified pH, the average binding of hydrogen ions NH can be calculated by use of... 

Now the binding of hydrogen ions is given by the following partial derivatives of the binding polynomial ... 

In thermodynamics, this is referred to as a Maxwell equation. This equation is derived later in Section 4.8. Thus the effect of pMg on the binding of hydrogen ions is the same as the effect of pH on the binding of magnesium ions in short, these are reciprocal effects. The bindings of these two ions are referred to as linked functions. Equation 1.3-17 can be confirmed by plotting these two derivatives, and the same plot is obtained in both cases. This would be a lot of work to do by hand, but since Mathematical can take partial derivatives, this can be done readily with a computer. The two plots are identical and are given in Fig. 1.8. 

Since JVH and NMg can be calculated for these reactants, ArJVH and Ar/VMg can be calculated as a function of pH and pMg. However, when a computer is available there is an easier way to do this by using equation 1.3-13 for the binding of hydrogen ions and 1.3-14 for the binding of magnesium ions. For example, equation 1.5-1 can be written... 

Figure 1.11 Change in the binding of hydrogen ions in the hydrolysis of ATP as a function of pH and pMg at 298.15 K and 0.25 M ionic strength (see Problem 1.8).

Calculation of the Binding of Hydrogen Ions by Reactants and the Changes in Binding of Hydrogen Ions in Biochemical Reactions... 

The change in binding of hydrogen ions in the biochemical reaction is given by... 

CALCULATION OF THE BINDING OF HYDROGEN IONS BY REACTANTS AND THE CHANGES IN BINDING OF HYDROGEN IONS IN BIOCHEMICAL REACTIONS... 

If K increases with pH, ArNH is negative, which indicates that less hydrogen is bound by products than reactants. In this case H+ is produced by the reaction. The change in binding of hydrogen ions in a biochemical reaction can also be... 

Table 4.9 Changes in the Binding of Hydrogen Ions for the New Reactions in Gluconeogenesis at 298.15 K and 0.25 M Ionic Strength ...

Figure 4.6 Plot of the change in binding of hydrogen ions in the reaction ATP + H20 = ADP + Pj at / = 0, 0.10 and 0.25 M at 298.15 K. The more curved plot is at zero ionic strength. (See Problem 4.5.)...

The change in binding of hydrogen ions in the dissociation of the site-L-tartrate complex can be calculated by taking the derivative of log K with respect to pH (equation 4.7-5). The pH dependence of ArNH is shown in Fig. 7.6. 

Figure 9.4 Dependence of the binding of hydrogen ions on the pH at 298.15 K and ionic strength 0.25 M for the following five biochemical half-reactions (starting at the top) ...

The changes in binding of hydrogen ions in five biochemical half reactions are shown in Fig. 9.4. Since 8E °/dpH is always negative for a half-reaction, Ar/VH is... 

Equation 10.2-7 shows that there are three contributions to the transformed enthalpy of reaction in this case the effects of the standard enthalpies of formation of the species, the effect due to the change in binding of hydrogen ions, and the... 

The subscripts on the partial derivatives have been omitted because they are complicated, as indicated by the fundamental equation. The change in binding of coenzymes in a reaction can be studied at constant concentrations of coenzymes, just as the change in binding of hydrogen ions in a reaction can be studied at constant pH. The further transformed enthalpy H" of the system can be calculated by use of the Gibbs-Helmholtz equation or from G" = II" — TS". 

---