Influence of Protein Electromagnetic Field on Hydrogen Bonding

TL;DR

This paper explores how protein electromagnetic fields influence hydrogen bonding and proton transfer in enzymes, suggesting enzyme excitation can control reaction rates and outcomes, especially in DNA polymerization.

Contribution

It introduces a quantum-mechanical model showing enzyme excitation facilitates hydrogen bonding and proton tunneling via barrier squeezing, impacting biochemical reaction control.

Findings

Enzyme excitation can enhance proton tunneling and hydrogen bond formation.

Barrier squeezing by enzymes influences reaction rates and specificity.

Implications for DNA polymerization and biochemical reaction regulation.

Abstract

The quantum-mechanical mechanisms by which the enzymes catalyze the hydrogen transfer in biochemical reactions are considered. Up to date it was established both experimentally and theoretically that in many cases the proton tunnelling through the intermolecular potential barrier is essential. We argue that in this case the enzyme excitation and internal motion facilitate proton transfer between reactants by squeezing the potential barrier which otherwise is practically impenetrable. In the similar fashion, the enzymes can facilitate the formation of hydrogen (H) bonds between the molecules. By means of barrier squeezing, the enzymes not only facilitate such reactions but also can control their rate and their final outcome, depending of enzyme excitation. In particular, such effects can play the major role in DNA polymerization reactions where preliminary DNTP selection is quite important.