Abstract：
:The phosphorylation of (Na+, K+)ATPase from the electric organ of the electric eel is dependent on Mg2+. The amount of phosphoenzyme formed was increased by K+ and decreased by Na+. Kinetic analyses indicate that a ternary complex of ATPase, Pi and Mg2+ is formed prior to phosphorylation of the protein. Calorimetric studies revealed extraordinarily large enthalpy changes associated with the binding of Mg2+ (-49 kcal/mol) and of Pi (-42 kcal/mol), indicating a thermodynamically significant conformational change in the enzyme. The dissociation constant for the binding of Mg2+ and Pi derived from calorimetric measurements is in good agreement with the value obtained from the kinetic studies. These results indicate that ion binding induces a conformational change in the enzyme which is a prerequisite for phosphorylation by Pi.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Kuriki Y,Halsey J,Biltonen R,Racker Edoi
10.1021/bi00668a002subject
Has Abstractpub_date
1976-11-16 00:00:00pages
4956-61issue
23eissn
0006-2960issn
1520-4995journal_volume
15pub_type
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