Dinuclear copper complexes modeling hemocyanin

Remarkably, reduced T2D Lc does not react with atmospheric 02. The behavior of the dinuclear T3 center thus contrasts starkly with that displayed by other reduced dinuclear copper sites of enzymes such as hemocyanin and tyrosinase or synthetic model dinuclear complexes (see Chapter 8.15). " These promptly perform a two-electron reduction of O2 to the peroxide level (reversibly, in the case of hemocyanin). 

A trans-n- 1,2-Peroxo Dicopper(II) Complex. Our own efforts have resulted in the structural and spectroscopic characterization of five types of copper-dioxygen complexes (6), distinguished on the basis of the ligands used for their synthesis and on their distinctive structures or physical properties. Thus, the manner in which hemocyanin binds 02 is not the only one possible, and it is of considerable interest to deduce the structures, along with associated spectroscopy and reactivity of a variety of types. Dioxygen can bind to dinuclear transition metals in a variety of structural modes, shown in Figure 2. As mentioned, mode C is present in oxy-Hc and Kitajima s model complex (Scheme 1), whereas we have structural and spectroscopic evidence for types A (30-32), B (33-35), and F (36-38) for peroxo 022- binding, and mode D (39, 40) in the case of hydroperoxo (OOH ) complexes. 

Chalcogenides Solid-state Chemistry Copper Enzymes in Denitrification Copper Hemocyanin/Tyrosinase Models Copper Proteins Oxidases Copper Proteins with Dinuclear Active Sites Copper Proteins with Type 1 Sites Copper Proteins with Type 2 Sites Iron Sulfitf Models of Protein Active Sites Iron-Snlfiir Proteins Nickel Enzymes Cofactors Nickel Models of Protein Active Sites Polynuclear Organometallic Cluster Complexes. 

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