Hydrolysis of the terminal phosphoanhydridic bond is a highly exergonic process. The amount of released energy depends on the conditions in a particular cell. Specifically, the energy released is dependent on concentrations of ATP, ADP and P.  As the concentrations of these molecules deviate from values at equilibrium, the value of Gibbs free energy change (ΔG) will be increasingly different. In standard conditions (ATP, ADP and P  concentrations are equal to 1M, water concentration is equal to 55 M) the value of ΔG is between -28 and -34 kJ/mol.
The range of the ΔG value exists because this reaction is dependent on the concentration of Mg cations, which stabilize the ATP molecule. The cellular environment also contributes to differences in the ΔG value since ATP hydrolysis is dependent not only on the studied cell, but also on the surrounding tissue and even the compartment within the cell. Variability in the ΔG values is therefore to be expected.
The relationship between the standard Gibbs free energy change ΔG and chemical equilibrium is revealing. This relationship is defined by the equation ΔG = -RT ln(K), where K is the equilibrium constant, which is equal to the reaction quotient Q in equilibrium. The standard value of ΔG for this reaction is, as mentioned, between -28 and -34 kJ/mol; however, experimentally determined concentrations of the involved molecules reveal that the reaction is not at equilibrium. Given this fact, a comparison between the equilibrium constant, K, and the reaction quotient, Q, provides insight. K takes into consideration reactions taking place in standard conditions, but in the cellular environment the concentrations of the involved molecules (namely, ATP, ADP, and P) are far from the standard 1 M. In fact, the concentrations are more appropriately measured in mM, which is smaller than M by three orders of magnitude. Using these nonstandard concentrations, the calculated value of Q is much less than one. By relating Q to ΔG using the equation ΔG = ΔG + RT ln(Q), where ΔG is the standard change in Gibbs free energy for the hydrolysis of ATP, it is found that the magnitude of ΔG is much greater than the standard value. The nonstandard conditions of the cell actually result in a more favorable reaction.
In one particular study, to determine ΔG in vivo in humans, the concentration of ATP, ADP, and P was measured using nuclear magnetic resonance. In human muscle cells at rest, the concentration of ATP was found to be around 4 mM and the concentration of ADP was around 9 μM. Inputing these values into the above equations yields ΔG = -64 kJ/mol. After ischemia, when the muscle is recovering from exercise, the concentration of ATP is as low as 1 mM and the concentration of ADP is around 7 μM. Therefore, the absolute ΔG would be as high as -69 kJ/mol.
By comparing the standard value of ΔG and the experimental value of ΔG, one can see that the energy released from the hydrolysis of ATP, as measured in humans, is almost twice as much as the energy produced under standard conditions.