Isothermal titration calorimetry reveals a zinc ion as an atomic switch in the diadenosine polyphosphates

The Journal of Biological Chemistry
Julian A TannerAndrew D Miller

Abstract

Diadenosine polyphosphates (diadenosine 5',5'''-P(1),P(n)-polyphosphate (Ap(n)A)) are 5'-5'''-phosphate-bridged dinucleosides that have been proposed to act as signaling molecules in a variety of biological systems. Isothermal titration calorimetry was used to measure the affinities of a variety of metal cations for ATP, diadenosine 5',5'''-P(1),P(3)-triphosphate (Ap(3)A), diadenosine 5',5'''-P(1),P(4)-tetraphosphate (Ap(4)A), and diadenosine 5',5'''-P(1),P(5)-pentaphosphate (Ap(5)A). The binding of Mg(2+), Ca(2+), and Mn(2+) to ATP is shown to take place with the beta,gamma-phosphates (primary site) and be endothermic in character. The binding of Ni(2+), Cd(2+), and Zn(2+) to ATP is found to take place at both the primary site and at a secondary site identified as N-7 of the adenine ring. Binding to this second site is exothermic in character. Generally, the binding of metal cations to diadenosine polyphosphates involves a similar primary site to ATP. No exothermic binding events are identified. Critically, the binding of Zn(2+) to diadenosine polyphosphates proves to be exceptional. This appears to involve a very high affinity association involving the N-7 atoms of both adenine rings in each Ap(n)A, as well as the more usual ...Continue Reading

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