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Zeeman-Stark modeling of the RF EMF interaction with ligand binding A. Chiabrera, B. Bianco, E. Moggia, J.J. Kaufman
Bioelectromagnetics, Volume 21, Issue 4 , Pages 312 - 324, © 2000 Wiley-Liss, Inc. PMID: 10797459
The influence of radiofrequency electromagnetic exposure on ligand binding to hydrophobic receptor proteins is a plausible early event of the interaction mechanism. A comprehensive quantum Zeeman-Stark model has been developed which takes into account the energy losses of the ligand ion due to its collisions inside the receptor crevice, the attracting nonlinear endogenous force due to the potential energy of the ion in the binding site, the out of equilibrium state of the ligand-receptor system due to the basal cell metabolism, and the thermal noise. The biophysical output is the change of the ligand binding probability that, in some instances, may be affected by a suitable low intensity exogenous electromagnetic input exposure, e.g., if the depth of the potential energy well of a putative receptor protein matches the energy of the radiofrequency photon. These results point toward both the possibility of the electromagnetic control of biochemical processes and the need for a new database of safety standards.
Biochemists Turn To Quantum Physics
Charge is a property of electrons most people are familiar with while another property, spin, is lesser known and typically the preserve of physicists. Electron spin occurs in one of two opposing directions - up or down - and biochemists want to start factoring electron spin into their computer simulations of biochemical reactions to make them more accurate.
"Physicists have long known that, according to the laws of quantum mechanics, there are some chemical reactions in our bodies that are 'forbidden' - such as hemoglobin's binding oxygen in our lungs when we breathe. But they do happen nonetheless. So, because these reactions involve electron spin, we decided to take a closer look at them," explained Rodriguez. "Nature loves balance, and you see evidence of it in both charge and spin," Rodriguez continued. "For example, electrons of opposite spin like to pair up with each other as they fly around the nucleus. This allows their spins to balance one another, just as positive and negative charges do between protons and electrons. Even when you have hundreds of electrons forming an immense cloud around a complex molecule, you still see balance in both charge and spin. But sometimes the electrons in metalloproteins seem to be playing a trick on us. As we see with hemoglobin, nature appears to be conserving electronic charge while sacrificing this conservation in spin."
As many of these supposedly forbidden reactions involve biomolecules and transition metals, which can flip back and forth between different spin states under certain conditions, Rodriguez theorized that it was this variability in spin state that was influencing the rate of these reactions. ..."We are creating a new field that attempts to understand biochemical processes at the most fundamental level - that of quantum mechanics. It could be the most important step toward making biochemistry a predictive science rather than a descriptive one," he concluded.