Abstract
Circular dichroism spectroscopy is used to investigate the thermostability of six arthropod hemocyanins (Hcs), representatives of the subphyla Crustacea (infraorder Brachyura) and Chelicerate (infraorders Xiphosura and Arachnida), and three molluscan Hcs from gastropod organisms. Melting points ( T m) are determined from the temperature dependence of ellipticity of dioxygen-binding proteins from Maia squinado, Callinectes sapidus, Carcinus maenas, Limulus polyphemus, Buthus sindicus, Androctonus australis, Megathura crenulata, Haliotis tuberculata, and Rapana thomasiana. Both, arthropod and molluscan Hcs, are thermostable proteins with melting temperatures in the region 68–91°C. Binuclear dioxygen-binding sites contribute significantly to the thermostability and increase the T m values of the apo-forms by 3–16°C. An elevated thermostability is observed in the case of the Limulus polyphemus Hc. One of the reasons is the high degree of hemocyanin oligomerization.
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