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How mechanical energy of phosphorylating enzymes transforms into the energy of chemical bonds?

Anatolii Leonidovich Buchachenko 1
Anatolii Leonidovich Buchachenko
Dmitry Anatol'evich Kouznetsov 1
Dmitry Anatol'evich Kouznetsov
Published 2008-03-18
Focus articleVolume 18, Issue 2, 63-66
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Buchachenko A. L., Kouznetsov D. A. How mechanical energy of phosphorylating enzymes transforms into the energy of chemical bonds? // Mendeleev Communications. 2008. Vol. 18. No. 2. pp. 63-66.
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Buchachenko A. L., Kouznetsov D. A. How mechanical energy of phosphorylating enzymes transforms into the energy of chemical bonds? // Mendeleev Communications. 2008. Vol. 18. No. 2. pp. 63-66.
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TY - JOUR
DO - 10.1016/j.mencom.2008.03.001
UR - https://mendcomm.colab.ws/publications/10.1016/j.mencom.2008.03.001
TI - How mechanical energy of phosphorylating enzymes transforms into the energy of chemical bonds?
T2 - Mendeleev Communications
AU - Buchachenko, Anatolii Leonidovich
AU - Kouznetsov, Dmitry Anatol'evich
PY - 2008
DA - 2008/03/18
PB - Mendeleev Communications
SP - 63-66
IS - 2
VL - 18
ER -
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@article{2008_Buchachenko,
author = {Anatolii Leonidovich Buchachenko and Dmitry Anatol'evich Kouznetsov},
title = {How mechanical energy of phosphorylating enzymes transforms into the energy of chemical bonds?},
journal = {Mendeleev Communications},
year = {2008},
volume = {18},
publisher = {Mendeleev Communications},
month = {Mar},
url = {https://mendcomm.colab.ws/publications/10.1016/j.mencom.2008.03.001},
number = {2},
pages = {63--66},
doi = {10.1016/j.mencom.2008.03.001}
}
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Buchachenko, Anatolii Leonidovich, and Dmitry Anatol'evich Kouznetsov. “How mechanical energy of phosphorylating enzymes transforms into the energy of chemical bonds?.” Mendeleev Communications, vol. 18, no. 2, Mar. 2008, pp. 63-66. https://mendcomm.colab.ws/publications/10.1016/j.mencom.2008.03.001.
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Abstract

Recent discovery of huge magnesium isotope effect in the rate of enzymatic synthesis of ATP offers a new insight on the mechanochemistry of enzymes as the molecular machines. The activity of magnesium-dependent enzymes (ATPase, phosphocreatine, phosphoglycerate kinases), in which Mg2+ ion has a magnetic isotope nucleus 25Mg, was found to be two or three times higher than that of enzymes in which the Mg2+ ion has nonmagnetic, spinless isotopic nuclei 24Mg or 26Mg. This isotope effect demonstrates unambiguously that the ATP synthesis is a spin-dependent process in which the Mg2+ ion is a reagent. It transforms mechanical energy of unequilibrium conformations of enzyme macromolecule into the energy of the P–O bond in ATP.

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