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Effects of radio frequency magnetic fields on iron release from cage proteins
Author(s) -
Céspedes Oscar,
Ueno Shoogo
Publication year - 2009
Publication title -
bioelectromagnetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.435
H-Index - 81
eISSN - 1521-186X
pISSN - 0197-8462
DOI - 10.1002/bem.20488
Subject(s) - superparamagnetism , bioelectromagnetics , magnetization , ferritin , magnetic field , specific absorption rate , magnetic nanoparticles , cage , materials science , nuclear magnetic resonance , radio frequency , nanoparticle , chemistry , ferrihydrite , absorption (acoustics) , condensed matter physics , nanotechnology , physics , composite material , biochemistry , mathematics , adsorption , quantum mechanics , combinatorics , antenna (radio) , telecommunications , computer science
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.