Dependence of Mitochondrial ATP Synthesis on the Nuclear Magnetic Moment of Magnesium Ions

Бучаченко, А. Л.; Kuznetsov, Dmitry A.; Arkhangelsky, Stanislav E.; Орлова, М. А.; Markaryan, A. A.; Berdieva, A. G.; Khasigov, P. Z.

doi:10.1023/b:dobi.0000033528.69032.9b

Cited by 26 publications

(27 citation statements)

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“…In a series of papers by Buchachenko and Kuznetsov (BK) together with various co-workers (7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22), a radical pair mechanism has been proposed for enzymatic phosphorylation of adenosine diphosphate (ADP) to adenosine triphosphate (ATP). This mechanism is influenced by the presence of a magnesium isotope with a nuclear spin.…”

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confidence: 99%

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Reexamination of magnetic isotope and field effects on adenosine triphosphate production by creatine kinase

Crotty

Silkstone

Poddar

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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The influence of isotopically enriched magnesium on the creatine kinase catalyzed phosphorylation of adenosine diphosphate is examined in two independent series of experiments where adenosine triphosphate (ATP) concentrations were determined by a luciferase-linked luminescence end-point assay or a real-time spectrophotometric assay. No increase was observed between the rates of ATP production with natural Mg, 24 Mg, and 25 Mg, nor was any significant magnetic field effect observed in magnetic fields from 3 to 1,000 mT. Our results are in conflict with those reported by Buchachenko et al. [J Am Chem Soc 130:12868–12869 (2008)], and they challenge these authors’ general claims that a large (two- to threefold) magnetic isotope effect is “universally observable” for ATP-producing enzymes [Her Russ Acad Sci 80:22–28 (2010)] and that “enzymatic phosphorylation is an ion-radical, electron-spin-selective process” [Proc Natl Acad Sci USA 101:10793–10796 (2005)].

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confidence: 99%

“…These enzymes are mitochondrial ATP synthase (8,11,16), phosphoglycerate kinase (9, 13), pyruvate kinase (12), and creatine kinase (9,12,15,20). The effects increased linearly with the amount of 25 Mg in the isotopic mixture (13).…”

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confidence: 99%

Reexamination of magnetic isotope and field effects on adenosine triphosphate production by creatine kinase

Crotty

Silkstone

Poddar

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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“…Indeed, the structures of the protein parts and catalytic sites of phosphorylating enzymes, such as ATP synthase, creatine kinase, and phosphoglycerate kinase (PGK) (2-10), are well known. There is an understanding of their functioning as molecular rotary motors (referring to ATP synthase) or molecular pumps (creatine kinase, for instance); however, within the area of enzymatic reaction chemistry, all ideas are limited to speculations circulating mostly around nucleophilic mechanisms.An insight into the chemical mechanism follows from a recently discovered and remarkable phenomenon: a dependence of the phosphorylating activity of enzymes on Mg isotopy (11,12). This unusual effect was found for creatine kinase and ATP synthase (13).…”

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confidence: 99%

Magnetic isotope effect of magnesium in phosphoglycerate kinase phosphorylation

Бучаченко

Kouznetsov²,

Орлова³

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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Phosphoglycerate kinase (PGK) is found to be controlled by a 25 Mg 2؉ -related magnetic isotope effect. Mg 2؉ nuclear spin selectivity manifests itself in PGK-directed ADP phosphorylation, which has been clearly proven by comparison of ATP synthesis rates estimated in reaction mixtures with different Mg isotopy parameters. Both pure 25 Mg 2؉ (nuclear spin 5͞2, magnetic moment ؉0.85) and 24 Mg 2؉ (spinless, nonmagnetic nucleus) species as well as their mixtures were used in experiments. In the presence of 25 Mg 2؉ , ATP production is 2.6 times higher compared with the yield of ATP reached in 24 Mg 2؉ -containing PGK-based catalytic systems. The chemical mechanism of this phenomenon is discussed. A key element of the mechanism proposed is a nonradical pair formation in which 25 Mg ؉ radical cation and phosphate oxyradical are involved. 25 Mg In one of their brilliant papers, Weber and Senior (1) pointed out that, despite great progress in our knowledge on the structure and our understanding of the molecular dynamics and functioning of ATP-synthesizing enzymes, the chemical mechanism of phosphorylation remains enigmatic: ''Our understanding of ATP synthesis remains rudimentary in molecular terms.'' Thus, our current understanding of ATP-synthesizing enzymes is still rudimentary at the molecular level and the key reaction responsible for the formation of the energy-carrying chemical bond POOOP remains obscure. Indeed, the structures of the protein parts and catalytic sites of phosphorylating enzymes, such as ATP synthase, creatine kinase, and phosphoglycerate kinase (PGK) (2-10), are well known. There is an understanding of their functioning as molecular rotary motors (referring to ATP synthase) or molecular pumps (creatine kinase, for instance); however, within the area of enzymatic reaction chemistry, all ideas are limited to speculations circulating mostly around nucleophilic mechanisms.An insight into the chemical mechanism follows from a recently discovered and remarkable phenomenon: a dependence of the phosphorylating activity of enzymes on Mg isotopy (11,12). This unusual effect was found for creatine kinase and ATP synthase (13). The rate of ATP production by enzymes in which the Mg 2ϩ ion has magnetic nucleus 25 Mg (nuclear spin, 5͞2; magnetic moment, Ϫ0.855 Bohr magneton) was shown to be two to three times higher than that induced by the same enzymes carrying spinless, nonmagnetic nuclei 24 Mg and 26 Mg. The discovery of this attention-catching isotope effect convincingly and unequivocally demonstrates that enzymatic phosphorylation is an ion-radical, electron-spin-selective process in which Mg ion Mg 2ϩ manifests itself as a reagent.The present study deals with our search for other examples of nuclear spin selectivity in biological processes. PGK (EC 2.7.11.08), a typical two-domain enzyme catalyzing the transfer of a phosphate group from ␣-phosphoglycerate to ADP, which leads to ATP production in eukaryotic cells (14), has been chosen for this purpose. Like creatine kinase, PGK contains Mg 2ϩ in its nu...

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“…Opening the magnetic isotope effect on ATP synthesis magnetic isotope magnesium 25 Mg 2+ [4][5][6], also for 67 Zn 2+ [7] and 43 Ca 2+ [8] showed that the rate of enzymatic reaction depends on the presence of the nuclear magnetic moment of the metal ion in the active phosphorylation site of the enzyme. Until the discovery of magnetic isotope effects in biochemistry [4] in the enzymatic phosphorylationthe possible influence of magnetic isotopes on living organisms is not expected.…”

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confidence: 99%

“…Until the discovery of magnetic isotope effects in biochemistry [4] in the enzymatic phosphorylationthe possible influence of magnetic isotopes on living organisms is not expected.…”

Section: Resultsmentioning

confidence: 99%

Neutron (Magnetic Isotope) Catalysis for Example Isotopes 24,25,26Mg in Cells E. Coli

Zhakenovich¹,

Valentina²,

Nessipbay³

et al. 2015

JCCE

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Dependence of Mitochondrial ATP Synthesis on the Nuclear Magnetic Moment of Magnesium Ions

Cited by 26 publications

References 4 publications

Reexamination of magnetic isotope and field effects on adenosine triphosphate production by creatine kinase

Reexamination of magnetic isotope and field effects on adenosine triphosphate production by creatine kinase

Magnetic isotope effect of magnesium in phosphoglycerate kinase phosphorylation

Neutron (Magnetic Isotope) Catalysis for Example Isotopes 24,25,26Mg in Cells E. Coli

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