A novel mechanism for energy activation in biomolecules

TL;DR

This paper introduces a new understanding of energy activation in biomolecules, revealing a mechanism involving kinetic energy accumulation and phase space dynamics, which differs from traditional reaction rate theories.

Contribution

It proposes a novel mechanism for energy activation in biomolecules based on reaction stability and phase space analysis, highlighting a different process from standard theories.

Findings

Energy activation involves high kinetic energy accumulation.

Reaction stability is key to understanding energy activation.

The mechanism differs from traditional barrier crossing models.

Abstract

An activated process consists of energy activation and barrier crossing; the former is a prerequisite for the latter. Barrier crossing has been studied extensively, but energy activation has been overlooked due to a lack of means to gauge its progress. We define reaction stability as the probability that reactive trajectories pass a vicinity in phase space; it enabled us to analyze energy activation of a biomolecular isomerization. This process follows a mechanism fundamentally different from presumed mechanisms in standard reaction rate theories: it features accumulation of high kinetic energy in reaction coordinates, achieved by precise synergy between them coordinated by momentum space.