Where is electronic energy stored in adenosine triphosphate?

J Phys Chem A. 2009 Apr 9;113(14):3360-8. doi: 10.1021/jp811085c.

Abstract

The gas-phase electronic energy of the hydrolysis of methyl triphosphate, a model of adenosine 5'-triphosphate (ATP), is partitioned into local (atomic and group) contributions. A modified definition of Lipmann's "group transfer potential" is proposed on the basis of the partitioning of the total electronic energy into atomic contributions within the framework of the quantum theory of atoms in molecules (QTAIM). The group transfer potential is defined here as the sum of the atomic energies forming the group in ATP minus the sum of the energies of the same atoms in inorganic phosphate. It is found that the transfer potential of the terminal phosphate group in ATP is significantly reduced, from +241.7 to +73.1 kcal/mol, as a result of complexation with magnesium. This is accompanied by a concomitant change in the energy of reaction from -168.6 to -24.9 kcal/mol. Regions within ATP where the electronic energy changes the most upon hydrolysis are identified. The study is conducted at the DFT/B3LYP/6-31+G(d,p) level of theory.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / chemistry*
  • Electrons*
  • Gases / chemistry
  • Hydrolysis
  • Magnesium / chemistry
  • Models, Chemical*
  • Models, Molecular
  • Molecular Conformation
  • Quantum Theory
  • Solvents / chemistry
  • Thermodynamics

Substances

  • Gases
  • Solvents
  • Adenosine Triphosphate
  • Magnesium