What can change the value of Δ G for a reaction?

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The Gibbs free energy change (ΔG) for a reaction is a thermodynamic quantity that reflects the spontaneity of the reaction under specific conditions. ΔG is determined by the inherent properties of the reactants and products as well as their concentrations, temperature, and pressure.

While it might seem that ΔG remains constant for a given reaction at constant standard conditions, this statement is an oversimplification. The actual value of ΔG can vary based on certain conditions, particularly concentrations of reactants and products, and temperature changes.

For example, changing the temperature of the system can affect the values of enthalpy and entropy, which are integral in the calculation of ΔG using the equation ΔG = ΔH - TΔS. Furthermore, altering the concentrations of reactants or products can shift the position of equilibrium, thus changing the value of ΔG for a reaction under non-standard conditions.

In contrast, the reaction type influences the nature of ΔG in that different reactions may have intrinsic different energy changes associated with them, but saying nothing changes ΔG is not accurate since ΔG is dependent on multiple factors, including temperature and concentration.

In the context of the question, factors like enzyme concentration can speed up reaction rates but do not change

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