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<p>A new mechanism of singlet-triplet conversion of electron pairs of diamagnetic substrates in the active sites of enzymes is proposed to explain the effect of nuclear spins and strong magnetic fields on the enzymatic synthesis of adenosine triphosphate (ATP) <i>in vitro</i> and <i>in vivo</i>. It is shown that the Fermi contact interaction, inducing a redistribution of electron density in enzyme-substrate complexes <sup>25</sup>Mg-ADP—ATPase, enables a decrease of the negative charge on the terminal groups of ADP. Thus, the nuclear spin of the <sup>25</sup>Mg isotope decreases the Coulomb repulsion of the negatively charged fragments of the substrates and increases the rate of the enzymatic formation of ATP. The theoretical results explain the experimentally observed effect of the nuclear spin of the <sup>25</sup>Mg isotope on the intracellular synthesis of ATP in <i>Escherichia coli</i> bacteria in strong magnetic fields.</p>

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Spin-dependent magnetosensitivity of enzymatic synthesis of adenosine triphosphate in strong magnetic fields

  • 期刊论文

  • 发表日期：

    2025年9月1日

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  • V. L. Berdinskiy,
  • U. G. Shevchenko

摘要

A new mechanism of singlet-triplet conversion of electron pairs of diamagnetic substrates in the active sites of enzymes is proposed to explain the effect of nuclear spins and strong magnetic fields on the enzymatic synthesis of adenosine triphosphate (ATP) in vitro and in vivo. It is shown that the Fermi contact interaction, inducing a redistribution of electron density in enzyme-substrate complexes 25Mg-ADP—ATPase, enables a decrease of the negative charge on the terminal groups of ADP. Thus, the nuclear spin of the 25Mg isotope decreases the Coulomb repulsion of the negatively charged fragments of the substrates and increases the rate of the enzymatic formation of ATP. The theoretical results explain the experimentally observed effect of the nuclear spin of the 25Mg isotope on the intracellular synthesis of ATP in Escherichia coli bacteria in strong magnetic fields.