Hemocyanin carbon monoxide binding

J.O. Alben and L.Y. Fager, "Structure of the Carbon Monoxide Binding Site of Hemocyanins Studied by Fourier Transform Infrared Spectroscopy". Biochemistry, 11, 4786 (1972). 

The possible similarity of this Cu—Cu pair to that observed in t T osinase [207) and hemocyanin [208) deserves consideration, but the overall functional differences are evident. The most obvious difference between T q)e 3 Cu and the Cu binding sites of hemocyanin and tyrosinase concerns interaction with carbon monoxide. Laccases are not inhibited by CO [113) and therefore have a low or non-existent affinity for this molecule. In contrast, both tyrosinase and hemocyanin have a demonstrable affinity for CO. It is reasonable that CuCu pairs, like isolated Cu ions, are capable of a wide variety of structure-function combinations. 

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