Calculating apparent equilibrium constants of enzyme-catalyzed reactions at pH 7
Robert A. Alberty
Abstract
Robert A. Alberty
Abstract
Apparent equilibrium constants K' of biochemical reactions at pH 7 and standard apparent reduction potentials of half reactions at pH 7 can be calculated using a table of standard transformed Gibbs energies of formation Delta(f)G'(0) at pH 7. A table is provided for 136 reactants at 25 degrees C, pH 7, and ionic strengths of 0, 0.10, and 0.25 M. Examples are given to illustrate the use of the table.
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Apparent equilibrium constants K' of biochemical reactions at pH 7 and standard apparent reduction potentials of half reactions at pH 7 can be calculated using a table of standard transformed Gibbs energies of formation Delta(f)G'(0) at pH 7. A table is provided for 136 reactants at 25 degrees C, pH 7, and ionic strengths of 0, 0.10, and 0.25 M. Examples are given to illustrate the use of the table.
Key concepts: Chemistry, Ionic strength, Gibbs free energy, Equilibrium constant, Table (database), Ionic bonding, Thermodynamics, Catalysis