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Biophysics
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Vol. 50, No. 1, January-February 2005, pp. 74-79
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Stable Isotopes of Mg2+ as Activators of the Suppressed ATP-Generating Function of Mitochondria D. A. Kuznetsov1, S. E. Arkhangel'skii1, A. G. Berdieva2, A. A. Markaryan2, P. Z. Khasigov2, T. M. Gatagonova2, S. A. Ktsoeva2, and M. A. Orlova3 1Semenov Institute of Chemical Physics, Russian Academy of Sciences, Moscow, 119991 Russia 2Sechenov Moscow Medical Academy, Moscow, 117421 Russia 3Lomonosov Moscow State University, Moscow, 119991 Russia Received September 16, 2003 in final form June 3, 2004 Key words: myocardial mitochondria, creatine kinase, 1-methylnicotinamide. The ATP-generating activity of mitochondria and mitochondrial creatine kinase was studied as a function of the isotopy of the magnesium pool of the incubation medium. The objects of investigation were in vitro systems containing preparations of isolated mitochondria and the enzyme from the myocardium of rats given a single injection of 1-methylnicotinamide to a dose of 1/2DL50. It was shown that the presence of paramagnetic cations of the 25Mg isotope leads to significant compensation for the intramitochondrial ATP deficiency caused by suppression of oxidative phosphorylation by 1-methylnicotinamide. This effect is virtually unachievable in systems whose magnesium pool comprises isotopes with zero nuclear spin (24Mg and 26Mg). The restoration of the mitochondrial ATP synthesis under induced inhibition of NAD/NADP-de-pendent reactions by 1-methylnicotinamide involves creatine kinase, whose activity is not suppressed by 1-methylnicotinamide. The high efficiency of restoration of this process is a spin-selective phenomenon and is reached mainly in the presence of 25Mg2+ cations. The significance of the obtained data for further investigation of the mechanisms of regulation of enzymatic catalysis was discussed. References - O. Okada, S. Telashima, M. Satoh, et al., J. Japan Pharm. Soc. 58, 211 (2000).
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PII: S0006350905010100
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