STRUCTURE AND PROPERTIES OF HEMOCYANINS .V. BINDING OF OXYGEN AND COPPER IN HELIX POMATIA HEMOCYANIN

1. 1. Reintroduction of monovalent copper into apo-α-hemocyanin of Helix pomatia leads to the complete return of the properties of native α-hemocyanin. 2. 2. The copper atoms in hemocyanin are required for the reassociation of tenth and twentieth molecules. 3. 3. In the reintroduction process, the copper atoms are randomly distributed among the empty binding sites of apo-α-hemocyanin. All copper-binding sites are equivalent and grouped in pairs; each pair forms a functional group. 4. 4. Upon storage for a few months, part of the copper atoms in every hemocyanin molecule are oxidized to Cu2+. This affects the oxygenation properties. 5. 5. The oxygenation curves of fresh α- and β-hemocyanin are nonhyperbolic at alkaline pH values in the presence of Ca2+ and Mg2+. The influence of the pH on the oxygenation curves of α- and β-hemocyanin shows marked differences. © 1969.