[Magnesium magnetic isotope effect: a key towards mechanochemistry of phosphorylating enzymes as molecular machines].
Mol Biol (Mosk)
; 40(1): 12-9, 2006.
Article
em Ru
| MEDLINE
| ID: mdl-16523686
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfoglicerato Quinase
/
ATPases Translocadoras de Prótons
/
Creatina Quinase
/
Magnésio
/
Magnetismo
Idioma:
Ru
Ano de publicação:
2006
Tipo de documento:
Article