Folding of the polypeptide chain(s), conformational flexibility and reactivity of the metal active site of hemocyanin and tyrosinase

Summary The comparative accessibility of the active sites of hemocyanin and tyrosinase, two proteins containing a binuclear type-3 copper site, has been investigated. The approaches were: (a) the kinetic study of the reaction of hemocyanin with cyanide in the presence of conformation perturbants; (b) the comparison between the kinetic parameters of the cyanide reaction on hemocyanin and tyrosinase; (c) the study of the efficiency and reaction mechanism of hemocyanin interaction with a typical tyrosinase substrate like catechol. The results indicate that the active site of tyrosinase is much more exposed than that of hemocyanin.