Thermodynamics of the disproportionation of adenosine 5'-diphosphate to adenosine 5'-triphosphate and adenosine 5'-monophosphate. I. Equilibrium model |
| |
Authors: | Goldberg R N Tewari Y B |
| |
Institution: | Chemical Thermodynamics Division, National Institute of Standards and Technology, Gaithersburg, Maryland 20899, USA |
| |
Abstract: | The thermodynamic treatment of the disproportionation reaction of adenosine 5′-diphosphate to adenosine 5′-triphosphate and adenosine 5′-monophosphate is discussed in terms of an equilibrium model which includes the effects of the multiplicity of ionic and metal bound species and the presence of long range electrostatic and short range repulsive interactions. Calculated quantities include equilibrium constants, enthalpies, heat capacities, entropies, and the stoichiometry of the overall reaction. The matter of how these calculations can be made self-consistent with respect to both calculated values of the ionic strength and the molality of the free magnesium ion is discussed. The thermodynamic data involving proton and magnesium-ion binding data for the nucleotides involved in this reaction have been evaluated. |
| |
Keywords: | Activity coefficients Adenosine 5′-diphosphate Adenosine 5′-monophosphate Adenosine 5′-triphosphate Adenylate kinase Enthalpy Enzyme catalysed reactions Entropy Equilibrium constants Gibbs energy Heat capacity Thermodynamics |
本文献已被 ScienceDirect PubMed 等数据库收录! |