Recent advances in the study of hemocyanin (Hc) are reviewed briefly.
Although subunit structues of molluscan and arthropodous Hc have been analyzed extensively by electron microscopic and ultracentrifugal techniques, the nature of cooperative interactions between the subunits is not well known yet. Ligand binding properties of Hc are described by the cooperativity model of Monod-Wyman-Changeux, though considerable modifications of the model are needed to fit experimental data.
The binuclear cuprous structure of active site of Hc has been established recently by physicochemical methods such as electron paramagnetic resonance and resonance Raman spectroscopy. N atoms are suggested as ligands of the cuprous ions.
Crystallographic studies of Hc are being attempted, and it will give informations about the structure of "copper pocket" of Hc.

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