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.
Cite
@article{arxiv.0801.2920,
title = {Effect of ELF e.m. fields on metalloprotein redox-active sites},
author = {A. De Ninno and M. Prosdocimi and V. Ferrari and G. Gerardi and F. Barbaro and T. Badon and D. Bernardini},
journal= {arXiv preprint arXiv:0801.2920},
year = {2008}
}