The Free Energy of Hydrolysis of Adenosine to Inosine and Ammonia

The equilibrium constant for formation of adenosine from inosine and ammonia has been measured directly in the presence of adenosine deaminase at several pH values. The apparent free energy of hydrolysis of adenosine at pH 7.0 is -5.4 kcal per mole, and the free energy of hydrolysis to free ammonia...

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Bibliographic Details
Published in:The Journal of biological chemistry 1967-10, Vol.242 (20), p.4711-4714
Main Author: Wolfenden, R
Format: Article
Language:English
Subjects:
Ammonia
Buffers
Chemical Phenomena
Chemistry
Hydrogen-Ion Concentration
Nucleosides
Thermodynamics
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Summary:The equilibrium constant for formation of adenosine from inosine and ammonia has been measured directly in the presence of adenosine deaminase at several pH values. The apparent free energy of hydrolysis of adenosine at pH 7.0 is -5.4 kcal per mole, and the free energy of hydrolysis to free ammonia and inosine is -2.2 kcal per mole, at ionic strength 1.0, 25°, with water concentration taken as 1. These values, which are comparable with indirect summations of thermochemical and equilibrium data for adenine and adenylic acid, are discussed in relation to earlier values for the hydrolysis of arginine and of amino acid amides.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)99514-1