Local Electromagnetic Fields Enable Fast Redox Sensing by Physically Accelerating Cysteine Oxidation

TL;DR

This paper demonstrates that local electromagnetic fields in biological environments can significantly accelerate cysteine oxidation rates, explaining rapid redox signaling in cells through physical effects rather than chemical changes.

Contribution

The study introduces a framework incorporating local electromagnetic fields into the Eyring equation, revealing how these fields accelerate cysteine oxidation without altering the fundamental chemistry.

Findings

Local EMFs can accelerate cysteine oxidation by orders of magnitude.

The framework predicts measurable vibrational Stark effects in peroxide complexes.

Reframes cysteine redox rates as field-dependent, not purely chemical, phenomena.

Abstract

Hydrogen peroxide oxidises cysteine residues to control protein function, yet bulk rate constants predict hours for changes that occur in cells in seconds. Here, this work shows that local electromagnetic fields (EMFs), ubiquitous in proteins, membranes and nanodomains, can lawfully modulate the Eyring barrier and orientate reactants, accelerating cysteine oxidation without changing the underlying chemistry. Embedding a field term into the Eyring expression, demonstrated that plausible local EMFs with realistic dipole changes accelerate rate constants by orders of magnitude. This local acceleration reconciles the discrepancy between predicted vs. observed rates of H2O2-mediated cysteine oxidation. The framework generates falsifiable predictions, such as vibrational Stark readouts in thiolate peroxide complexes should fall within predicted ranges, and reframes rate-constants as mutable, field conditioned parameters. Cysteine redox sensing is fast not because the chemistry is exotic, but because the physics is local.