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Effects of radio frequency magnetic fields on iron release from cage proteins

✍ Scribed by Oscar Céspedes; Shoogo Ueno

Publisher
John Wiley and Sons
Year
2009
Tongue
English
Weight
327 KB
Volume
30
Category
Article
ISSN
0197-8462

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✦ Synopsis

Abstract

Ferritin, the iron cage protein, contains a superparamagnetic ferrihydrite nanoparticle formed from the oxidation and absorption of Fe^2+^ ions. This nanoparticle increases its internal energy when exposed to alternating magnetic fields due to magnetization lag. The energy is then dissipated to the surrounding proteic cage, affecting its functioning. In this article we show that the rates of iron chelation with ferrozine, an optical marker, are reduced by up to a factor of 3 in proteins previously exposed to radio frequency magnetic fields of 1 MHz and 30 µT for several hours. The effect is non‐thermal and depends on the frequency‐amplitude product of the magnetic field. Bioelectromagnetics 30:336–342, 2009. © 2009 Wiley‐Liss, Inc.

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## Abstract The protein ferritin has a natural ferrihydrite nanoparticle that is superparamagnetic at room temperature. For native horse spleen ferritin, we measure the low field magnetic susceptibility of the nanoparticle as 2.2 × 10^−6^ m^3^ kg^−1^ and its Néel relaxation time at about 10^−10^ s.