Mousavy SJ, Riazi GH, Kamarei M, Aliakbarian H, Sattarahmady N, Sharifizadeh A, Safarian S, Ahmad F, Moosavi-Movahedi AA.(2009): Effects of mobile phone radiofrequency on the structure and function of the normal human hemoglobin. Int J Biol Macromol 44(3):278-285.
Normal hemoglobin is an essential component of the circulatory system of vertebrates. Its chief physiological function is to transport oxygen from the lung to the tissues. Hemoglobin must bind oxygen efficiently in the lungs and release it in the tissues. A protein that binds O2 with high affinity would bind it efficiently in the lung but would not release much of it in the tissue. A protein that binds O2 with sufficiently low affinity to release it in the tissue would not pick up much oxygen in the lungs. Hemoglobin solves this problem by undergoing a transition from a low-affinity state to a high-affinity state as more O2 molecules are bound. Interactions between the subunits in hemoglobin cause conformational changes that alter the affinity of the protein for oxygen. Previous research provides some evidence that radiofrequency electromagnetic fields (RF EMFs) may cause conformational changes in some proteins and hence in their biological properties.
The aim of this research was to study the effect of mobile phone EMFs on the oxygen affinity and structure of hemoglobin because of its importance as a sole oxygen transporter in blood.
Human adult hemoglobin was prepared from human red blood cells of healthy donors. Exposure to the RF 910 MHz and 940 MHz EMF were carried out by a spiral antenna in a temperature controlled incubator at 37.0±0.1°C. The exposed sample was matched with unexposed control kept in the same experimental conditions. To study potential effects of field intensity, 940 MHz RF with electric field intensities (EFI) of 21.7, 30.6, 48.6 and 77.0 V/m were applied. The effect of exposure duration was investigated in experiments in which hemoglobin was exposed to 940 MHz with EFI of 77 V/m for five fixed time periods: 15, 30, 60, 90 and 120 min. Oxygen affinity was measured by sodium dithionite (SDT) with UV-vis spectrometer. Structural hemoglobin changes were studied by circular dichroism and fluorescence spectroscopy.
Results and interpretation
The results of the in vitro experiments have shown that the oxygen binding ability of hemoglobin was affected (decreased) by exposure to mobile phone frequencies of 910 MHz and 940 MHz. This decrease was associated with both EMF intensity and exposure duration. The effects of the two frequencies (910 MHz and 940 MHz) were similar. The authors suggest that hemoglobin of a healthy human exposed to these frequencies would bind less oxygen in the lung and release more oxygen in the tissues. The results of the structural analysis suggest that this change in the functional activity of hemoglobin is due to changes in the tertiary structure of the protein at 37°C.
Mobile phone EMFs alter oxygen affinity and tertiary structure of hemoglobin. The decrease in oxygen affinity of hemoglobin corresponds to the EMFs intensity and duration of exposure.