Effects of radio frequency magnetic fields on iron release from cage proteins.
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 microT for several hours. The effect is non-thermal and depends on the frequency-amplitude product of the magnetic field.
Céspedes
Oscar
O
Applied Quantum Physics Department, Graduate School of Engineering, Kyushu University, Fukuoka, Japan. cespius@yahoo.com
Ueno
Shoogo
S
D000818:Animals; D001052:Apoferritins / Q000737:chemistry / Q000378:metabolism; D005293:Ferritins / Q000737:chemistry* / Q000378:metabolism; D005297:Ferrozine / Q000737:chemistry / Q000378:metabolism; D006736:Horses; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000737:chemistry* / Q000378:metabolism; D007502:Iron Chelating Agents / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D053758:Nanoparticles / Q000737:chemistry; D011487:Protein Conformation; D011846:Radio Waves; D013997:Time Factors
D007502:Iron Chelating Agents; D005297:Ferrozine; D005293:Ferritins; D001052:Apoferritins; D007501:Iron