[Magnesium magnetic isotope effect: a key towards mechanochemistry of phosphorylating enzymes as molecular machines].
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.
Buchachenko
A L
AL
Kuznetsov
D A
DA
D000255:Adenosine Triphosphate / Q000096:biosynthesis / Q000737:chemistry; D001696:Biomechanical Phenomena; D003402:Creatine Kinase / Q000737:chemistry* / Q000502:physiology; D007554:Isotopes / Q000737:chemistry; D008274:Magnesium / Q000737:chemistry* / Q000502:physiology; D008280:Magnetics; D008954:Models, Biological; D010735:Phosphoglycerate Kinase / Q000737:chemistry* / Q000502:physiology; D010766:Phosphorylation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000502:physiology; D013113:Spin Labels
D007554:Isotopes; D013113:Spin Labels; D000255:Adenosine Triphosphate; D010735:Phosphoglycerate Kinase; D003402:Creatine Kinase; D006180:Proton-Translocating ATPases; D008274:Magnesium