Transformation of chemical energy in biomolecular systems with hydrogen bonds

The mechanism underlying the excitation of the hydrogen bond with ATP hydrolysis was considered. Coulomb interactions of the proton of the hydrogen bond A-H...B with the electrical field of the covalent bond of ADP-P were calculated. It was shown that the electrical field of the covalent bond of ADP-P excites oscillations of the proton in the complex with the hydrogen bond A-H...B and displaces it from the equilibrium towards the covalent bond. The distortion of the potential curve depends on a change in the length of the covalent bond of ADP-P. Adiabatic potentials U0 and UN of the ADP-P system were calculated, which correspond to the ground and excited states of the H-bond proton. It was found that as the length of the bond of ADP-P (rho) increases, the branches of the adiabatic potential U0(rho) and UN(rho) intersect. At the intersection point, the system can transit to the branch UN(rho), which can lead to a reduction of the barrier and a break of the covalent bond of ADP-P. Presumably, this mechanism is universal for processes of transformation of the chemical energy of ATP to the energy of excited hydrogen bond, a mechanism for the maintenance of heat balance and reduction of entropy in a living organism.