Structure-function correlations in copper clusters in proteins

E. I. Solomon, J. L. Cole, M. J. Baldwin
1990 Pure and Applied Chemistry  
A coupled binuclear copper active site is present in a wide variety of proteins and enzymes which perform different biological functions utilizing 0,. In the multicopper oxidases, the Type 2 and Type 3 centers comprise a trinuclear Cu cluster which represents the active site for the multielectron reduction of 0,. A coupled binuclear copper active site is present in a wide variety of proteins and enzymes which perform different biological functions utilizing 02. The hemocyanins (Hc) reversibly
more » ... s (Hc) reversibly bind 02, the tyrosinases (Ty) are monoxygenases which hydroxylate monophenols to o-diphenols and oxidize these to o-quinones, and the multicopper oxidases (laccase (Lc), ascorbate oxidase and ceruloplasmin), which contain additional copper centers (Type 1 and Type 2) catalyze the four electron reduction of 02 to water. Our original chemical and spectroscopic studies over a series of protein active site derivatives of Hc and Ty demonstrated (ref.
doi:10.1351/pac199062061063 fatcat:vu36g32dnfbk5lbniv4uhwjdzu