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This research calculates thermodynamic parameters to understand how pH and magnesium concentration affect reactions involving adenosine phosphates.

June 1, 1969Journal of Biological Chemistry285 citationsOpen Access

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Standard Gibbs Free Energy, Enthalpy, and Entropy Changes as a Function of pH and pMg for Several Reactions Involving Adenosine Phosphates

RAR.A. AlbertyMassachusetts Institute of Technology

Key Points

This research calculates thermodynamic parameters to understand how pH and magnesium concentration affect reactions involving adenosine phosphates.
Calculated standard Gibbs free energy, enthalpy, and entropy changes for several reactions.
Considered the effects of pH and magnesium concentration at 25°C and 0.2 ionic strength.
Analyzed multiple reactions including ATP hydrolysis and phosphorylation.
Standard Gibbs free energy changes varied with pH and pMg for all reactions examined.
Enthalpy and entropy changes were computed, providing insights into reaction spontaneity and equilibrium.
Specific reactions displayed distinct thermodynamic profiles based on pH and magnesium levels.

Abstract

The standard Gibbs free energy change AGZ,,, number (nn) of moles of H+ produced, number (nMg) of moles of Mg2+ produced, standard enthalpy change AH:,,, and standard entropy change AC&, have been calculated as functions of pH and pMg for the following phosphohydrolyase and phosphotransferase reactions at 25" and 0.2 ionic strength: ATP + Hz0 = ADP + Pi (1) ATP + AMP = 2ADP (2) ATP + Hz0 = AMP + PPi (3) ADP + Hz0 = AMP + Pi (4) ATP + 2HzO = AMP + 2Pi (5) PPi + Hz0 = 2Pi (6)

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Cite This Study

R.A. Alberty (Sun,) studied this question.

synapsesocial.com/papers/6a714382fe4101aa97e07fe0 https://doi.org/https://doi.org/10.1016/s0021-9258(18)93127-3

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