ATP Synthase: A Moonlighting Enzyme with Unprecedented Functions

TL;DR

This paper reveals a novel free energy component contributed by ATP synthase's electrostatic potential, which enhances the chemiosmotic voltage and challenges existing energy dissipation models.

Contribution

It introduces the concept of ATP synthase's electrostatic potential as a new free energy term reinforcing chemiosmotic voltage.

Findings

ATP synthase's electrostatic potential adds to chemiosmotic voltage

The new energy term is comparable in magnitude to dissipation energy

This insight challenges traditional views on ATP synthase energy dynamics

Abstract

ATP synthase's intrinsic molecular electrostatic potential (MESP) adds constructively to, and hence reinforces, the chemiosmotic voltage. This ATP synthase voltage represents a new free energy term that appears to have been overlooked. This term is at least roughly equal in order of magnitude and opposite in sign to the energy needed to be dissipated as a Maxwell's demon (Landauer principle).