分子陀螺与弱ELF磁场的生物学效应
Molecular gyroscopes and biological effects of weak ELF magnetic fields
摘要：
已知极低频磁场会影响生物系统。在许多情况下，生物效应在磁场的生物效应参数中显示出“窗口”：最引人注目的是，相对强的磁场有时不会引起明显的效应，而10- 100 $μ$ T量级的较小磁场会引起明显的效应。在这种情况下，线性共振物理过程不能解释频率窗口。振幅窗口现象表明了一种非线性的物理机制。最近有人提出这种非线性机制来解释这些“窗口”。它考虑了量子干涉效应对蛋白质结合的底物离子。磁场引起离子量子态的干涉，改变离子-蛋白质解离的概率。这种离子干扰机制预测了发生生物效应的特定磁场频率和振幅窗口。这与很多实验一致。然而，根据该机制，蛋白质腔内离子量子态的寿命$Γ^{-1}$应该是不切实际的值，对于频带10- 100 Hz大于0.01 s。在本文中，一个生物物理机制已被提出，（i）保留有吸引力的功能的离子干扰机制和（ii）使用陀螺运动的原则，并删除了必要假设大的寿命。该机制考虑了分子组的密度矩阵的动力学，分子组通过两个共价键连接到蛋白质腔的壁，即，分子陀螺仪数值计算表明分子陀螺几乎是自由转动的。对于28埃的腔尺寸，范德华力引起的弛豫时间约为0.01 s。
英文摘要：
Extremely-low-frequency magnetic fields are known to affect biological systems. In many cases, biological effects display `windows' in biologically effective parameters of the magnetic fields: most dramatic is the fact that relatively intense magnetic fields sometimes do not cause appreciable effect, while smaller fields of the order of 10--100 $μ$T do. Linear resonant physical processes do not explain frequency windows in this case. Amplitude window phenomena suggest a nonlinear physical mechanism. Such a nonlinear mechanism has been proposed recently to explain those `windows'. It considers quantum-interference effects on protein-bound substrate ions. Magnetic fields cause an interference of ion quantum states and change the probability of ion-protein dissociation. This ion-interference mechanism predicts specific magnetic-field frequency and amplitude windows within which biological effects occur. It agrees with a lot of experiments. However, according to the mechanism, the lifetime $Γ^{-1}$ of ion quantum states within a protein cavity should be of unrealistic value, more than 0.01 s for frequency band 10--100 Hz. In this paper, a biophysical mechanism has been proposed that (i) retains the attractive features of the ion interference mechanism and (ii) uses the principles of gyroscopic motion and removes the necessity to postulate large lifetimes. The mechanism considers dynamics of the density matrix of the molecular groups, which are attached to the walls of protein cavities by two covalent bonds, i.e., molecular gyroscopes. Numerical computations have shown almost free rotations of the molecular gyros. The relaxation time due to van der Waals forces was about 0.01 s for the cavity size of 28 angströms.
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