Molecular mechanisms for proton transport in membranes.

TLDR

Continuous chains of hydrogen bonds formed from protein side groups are assumed to be the fundamental structural element for proton transport. The study explores likely mechanisms for proton transport through biomembranes. The authors propose that continuous hydrogen‑bond chains in proteins, possibly modulated by conformational changes, can act as proton wires and enable a reversible proton pump that functions as a molecular motor driven by membrane electrochemical potential. Studies in ice predict that these hydrogen‑bond chains have low impedance and can function as proton wires.

Abstract

Likely mechanisms for proton transport through biomembranes are explored. The fundamental structural element is assumed to be continuous chains of hydrogen bonds formed from the protein side groups, and a molecular example is presented. From studies in ice, such chains are predicted to have low impedance and can function as proton wires. In addition, conformational changes in the protein may be linked to the proton conduction. If this possibility is allowed, a simple proton pump can be described that can be reversed into a molecular motor driven by an electrochemical potential across the membrane.