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

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Authors
De Ninno, A.
Prosdocimi, M.
Ferrari, V.
Gerardi, G.
Barbaro, F.
Badon, T.
Bernardini, D.
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Abstract
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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.
Comment: 18 pages, 4 figures
Keywords
Physics - Biological Physics, Physics - General Physics
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