| Range |
-36.07 to -37.64 Table - link kJ/mole
|
| Organism |
Generic |
| Reference |
Alberty, R. A. Thermodynamics of biochemical reactions, Wiley Interscience 2003 John Wiley & Sons, Inc. Chapter 4 Thermodynamics of Biochemical Reactions at Specified pH p. 74 table 4.1 |
| Primary Source |
Robert A. Alberty, Effect of Temperature on Standard Transformed Gibbs Energies of Formation of Reactants at Specified pH and Ionic Strength and Apparent Equilibrium Constants of Biochemical Reactions, (2001) J . Phys. Chem B, 105, 7865-7870 DOI: 10.1021/jp011308v |
| Comments |
"When standard enthalpies of all of the species involved in a reaction are available, K' can be calculated at desired temperatures not too far from 298.15 K. The effect of temperature on the standard transformed Gibbs energy of hydrolysis of ATP is shown in Table 4.1 (see Problem 4.6)." |
| Entered by |
Uri M |
| ID |
106580 |