What Is The Free Energy Change (ΔG) Of The Hydrolysis Of ATP To ADP?
The free-energy change (ΔG) of the hydrolysis of ATP to ADP and Pi may vary considerably with variations in pH temperature atmospheric pressure and concentrations of reactants and products.
The free-energy change (ΔG) of the hydrolysis of ATP to ADP and Pi is approximately -7.3 kcal/mole but it varies from species to species.
The free-energy change (ΔG) of the hydrolysis of ATP to ADP and Pi is constant at -7.3 kcal/mole.
The free-energy change (ΔG) of the hydrolysis of ATP to ADP and Pi may vary considerably with variations in pH, temperature, atmospheric pressure, and concentrations of reactants and products. The free-energy change (ΔG) of the hydrolysis of ATP to ADP and Pi is -7.3 kcal/mole under standard conditions.
Standard conditions are defined as a temperature of 298 K (or 250C), 1 atm, pH 7, and equal 1M concentrations present in all reactants and products. In living cells, conditions do not conform to standard conditions, primarily because reactant and product concentrations differ from 1 M.
For example, when ATP hydrolysis occurs under cellular conditions, the actual ΔG is about -13 kcal/mol, 78% greater than the energy released by ATP hydrolysis under standard conditions.