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Comparative Study
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Metal ion interactions with Limulus polyphemus and Callinectes sapidus hemocyanins: stoichiometry and structural and functional consequences of calcium(II), cadmium(II), zinc(II), and mercury(II) binding.
Biochemistry 1983 September 28
Hemocyanins are oligomeric metalloproteins containing binuclear copper centers that reversibly combine with oxygen molecules. The structural stability and functional properties of these proteins are modified by divalent cations. Equilibrium dialysis was used to study the reversible interaction of Callinectes sapidus and Limulus polyphemus hemocyanins with the divalent cations calcium, cadmium, zinc, copper, and mercury. The number of binding sites and association constants for each cation were obtained from an analysis of the binding data by a nonlinear least-squares minimization procedure. Spectral analysis showed Limulus hemocyanin to possess two mercury-reactive sulfhydryl groups per subunit (Kassoc = 2.02 X 10(45) M-1). Callinectes hemocyanin contains only one such group (Kassoc = 2.29 X 10(34) M-1). Cadmium and zinc are shown to substitute for calcium ions. Oxygen binding studies with Limulus hemocyanin showed that all five divalent metal ions increase its oxygen affinity. Calcium ions increase cooperativity of oxygen binding, while heavy-metal ions have an opposite effect. Binding of two mercuric ions per Limulus hemocyanin subunit irreversibly fixes the 48 subunit aggregate in a high-affinity noncooperative conformational state. These results offer a striking contrast to the functional consequences of heavy-metal ion interactions with Callinectes hemocyanin [Brouwer, M., Bonaventura, C., & Bonaventura, J. (1982) Biochemistry 21, 2529-2538]. The functional alterations associated with metal ion interactions are discussed within the context of an extension of the two-state model for allosteric transitions of Monod et al. [Monod, J., Wyman, J., & Changeux, J.P. (1965) J. Mol. Biol. 12, 88-118]. Incubation of Limulus oxy- or deoxyhemocyanin with mercuric chloride results in the conversion of 60% of the binuclear copper sites to stable half-apo sites. The remaining active sites are stable with respect to mercury-induced copper displacement when oxygen is bridging both coppers. In the absence of oxygen these sites will eventually lose both copper atoms. Under the same conditions 50% of the binuclear copper sites of Callinectes deoxyhemocyanin are converted to half-apo sites. In this case oxygen completely protects against copper displacement [Brouwer, M., Bonaventura, C., & Bonaventura, J. (1982) Biochemistry 21, 2529-2538]. The binuclear copper center of Busycon carica is not affected at all, demonstrating profound differences between the active sites of hemocyanins of a chelicerate arthropod (Limulus), a crustacean arthropod (Callinectes), and a gastropod mollusc (Busycon).
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