PMID: 16523686Mar 10, 2006Paper

Magnesium magnetic isotope effect: a key towards mechanochemistry of phosphorylating enzymes as molecular machines

Molekuliarnaia biologiia
Anatoly L Buchachenko, D A Kuznetsov

Abstract

A discovery of the huge magnesium isotope effect in enzymatic ATP synthesis provides a new insight into mechanochemistry of enzymes as the molecular machines. It has been found that the catalytic activity values of ATPase, creatine kinase and phosphoglycerate kinase are 2 to 4-fold higher once their active sites contain magnetic (25Mg) not spinless, non-magnetic (24Mg, 26Mg), magnesium cation isotopes. This clearly proves that the ATP synthesis is a spin-selective process involving Mg2+ as the electron accepting reagent. The formation of ATP takes place in an ion-radical pair resulted by two partners, ATP oxyradical and Mg+. The magnesium bivalent cation is a key player in this process, this ion transforms the protein molecule mechanics into a mere chemistry. This ion is a most critical detail of structure of the magnesium dependent phosphorylation enzymes as the mechanochemical molecular machines.

References

Jul 8, 1999·Proceedings of the National Academy of Sciences of the United States of America·H OmoteM Futai
Jun 6, 2000·Biochimica Et Biophysica Acta·J Weber, A E Senior
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Feb 18, 2005·Nature·Yannick RondelezHiroyuki Noji

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Citations

May 9, 2008·European Biophysics Journal : EBJ·Alexander A Tulub, V E Stefanov
Dec 27, 2011·Proceedings of the National Academy of Sciences of the United States of America·Darragh CrottyJ M D Coey
Jul 3, 2015·Frontiers in Human Neuroscience·Alexander V ChervyakovMichael A Piradov

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