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Dioxygen Activation by Biomimetic Dinuclear Complexes

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Bioinorganic Chemistry of Copper

Abstract

Metalloproteins containing dinuclear and polynuclear centers are very important in the biological reactions of dioxygen.1 Among these, we have been mostly interested in the dicopper sites of the dioxygen carrier hemocyanin2 and the monooxygenase tyrosinase,3 in the polynuclear copper site of ascorbate oxidase4 and, more recently, in the heme-copper site of cytochrome oxidase.5 Our work with biomimetic dinuclear copper complexes started with the investigation of a series of two-coordinate copper(I)-bis(imine) complexes. The reason for this choice was that in the reaction mechanism for tyrosinase proposed by Solomon et al.6 a dinuclear two-coordinate copper(I) site for the deoxy form of the protein was involved.

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Casella, L., Gullotti, M. (1993). Dioxygen Activation by Biomimetic Dinuclear Complexes. In: Karlin, K.D., Tyeklár, Z. (eds) Bioinorganic Chemistry of Copper. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-6875-5_23

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