Effect of ELF e.m. fields on metalloprotein redox-active sites

TL;DR

This study investigates how extremely low frequency electromagnetic fields influence the activity of metalloproteins by affecting their metal ions, revealing specific effects on enzyme radical generation and activity.

Contribution

It demonstrates that weak electromagnetic fields at specific Larmor frequencies can modulate the activity of metalloproteins, a novel insight into bioelectromagnetic interactions.

Findings

XO radical generation increases at Fe2+ Larmor frequency

SOD1 activity decreases at Cu2+ Larmor frequency

Electromagnetic fields can influence enzyme radical processes

Abstract

The peculiarity of the distribution and geometry of metallic ions in enzymes pushed us to set the hypothesis that metallic ions in active-site act like tiny antennas able to pick up very feeble e.m. signals. Enzymatic activity of Cu2+, Zn2+ Superoxide Dismutase (SOD1) and Fe2+ Xanthine Oxidase (XO) has been studied, following in vitro generation and removal of free radicals. We observed that Superoxide radicals generation by XO is increased by a weak field having the Larmor frequency fL of Fe2+ while the SOD1 kinetics is sensibly reduced by exposure to a weak field having the frequency fL of Cu2+ ion.