Study type: Medical/biological study (experimental study)

Effects of radio frequency magnetic fields on iron release from cage proteins med./bio.

Published in: Bioelectromagnetics 2009; 30 (5): 336-342

Aim of study (acc. to author)

To study the effects of radiofrequency magnetic fields in ferritin.

Background/further details

The iron cage protein ferritin is an obvious candidate to study the effects of radiofrequency magnetic fields at the molecular scale, because it has the highest net magnetic moment of all proteins and plays an essential biological role, being present in organisms from bacteria to humans. Ferritin oxidizes the harmful Fe2+ ions and stores them in the cavity, forming a ferrihydrite nanoparticle with up to 4,500 iron ions.



Exposure Parameters
Exposure 1: 250 kHz–2 MHz
Exposure duration: up to 9 h

Exposure 1

Main characteristics
Frequency 250 kHz–2 MHz
Exposure duration up to 9 h
Exposure setup
Exposure source
Distance between exposed object and exposure source 1 m
Setup 1 cm high Helmholtz coils with a diameter of 9 cm, separated by 5 cm
Measurand Value Type Method Mass Remarks
magnetic flux density 15 µT minimum calculated - -
magnetic flux density 30 µT - calculated - -
magnetic flux density 45 µT - calculated - -
magnetic flux density 60 µT maximum calculated - -
electric field strength 0.1 V/m - measured - at 250 kHz
electric field strength 0.4 V/m - measured - at 2 MHz

Exposed system:

Methods Endpoint/measurement parameters/methodology

Investigated system:
Time of investigation:
  • during exposure
  • after exposure

Main outcome of study (acc. to author)

The data show that the rates of iron chelation with ferrozine are reduced by up to a factor of three in proteins previously exposed to radiofrequency 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.

Study character:

Study funded by

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