Half-apo Derivatives of Hemocyanins

Abstract

A number of experimental evidences have indicated that the two copper ions in the site of hemocyanin (Hc) are differently shielded by the protein matrix, thus showing asymmetrical chemical behaviour (1, 2,3). In particular, one metal ion can be selectively removed by CN⁻ from the active site of mollusc Hc leading to the formation of an half-apo derivative still containing one metal ion (3,4). The first ion has been called “fast reacting copper” and the second “slow reacting copper” (5,6).