Abstract
Magnetic isotope effects have been recently discovered in living nature. They were observed for the first time in experiments on cells enriched with various magnesium isotopes, magnetic 25Mg or non-magnetic ones. A catalytic effect of the magnetic isotope of magnesium was discovered in experiments with myosin, the most important biomolecular motor utilizing the energy of ATP to perform mechanical work. The rate of ATP hydrolysis with the magnetic 25Mg isotope is 2.0–2.5 times higher than that obtained with nonmagnetic 24Mg or 26Mg. A similar effect of the nuclear spin catalysis was experimentally observed for zinc isotopes. The rate of ATP hydrolysis in the case of magnetic 67Zn increased by 40–50% as compared to that observed experimentally for nonmagnetic isotopes (64Zn or 68Zn). Catalytic effects of the magnetic isotope of magnesium were also experimentally found for H+-ATPase isolated from yeast mitochondria and ATPase of the plasma membrane of the myometrium. The magnetic isotope effect indicates unambiguously that the chemomechanical processes involve a limiting step catalyzed by biomolecular motors, which depends on the electronic spin state, and that this step is accelerated in the presence of nuclear spin of the magnetic isotope.
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Based on the materials presented on the XXXII Symposium “Modern Chemical Physics” (September 19–28, 2020, Tuapse, Russia).
Published in Russian in Izvestiya Akademii Nauk. Seriya Khimicheskaya, No. 9, pp. 1633–1639, September, 2021.
This work was financially supported by the Ministry of Science and Higher Education of the Russian Federation (Theme No. AAAA-A19-119092390041-5).
The experiments in the cited works were carried out in full compliance with the European Convention for the Protection of Animals used for Scientific Experiments and Other Scientific Purposes (Strasbourg, March 18, 1986).
The author declares no competing interests.
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Koltover, V.K. Nuclear spin catalysis in biochemical physics. Russ Chem Bull 70, 1633–1639 (2021). https://doi.org/10.1007/s11172-021-3264-6
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DOI: https://doi.org/10.1007/s11172-021-3264-6