Oxygenases copper complexes

CU2O2 structure 13 3 (a tran5- X-l,2-peroxo complex). In both cases association of two mononuclear copper(I) centers takes place. These functional mimics of O2 activating systems provide the key information for further design of dinuclear copper complexes with oxygenase activity. 

Interaction of dioxygen species with Fe aq and with Fe " aq has been very briefly reviewed. In relation to 0x0-, peroxo-, and superoxo-complexes as models for intermediates in oxygenase activity, a brief report on a 2000 symposium on activation of oxygen summarizes the then-current situation in the search for a mechanism common to mono- and dinuclear iron sites, mono- and dinuclear copper sites, and copper-iron sites. The outline proposals comprise ... 

A large number of investigations of the mechanism of electron transfer reactions of macromolecule-metal complexes in biological systems has been reported. These investigations were concerned with not only natural metalloenzymes such as cytochromes, ferredoxin, blue coppers, oxygenase, peroxidase, catalase, hemoglobin, and ruberodoxin, but also modified metalloenzymes 47). 

It should be noted that besides the multicopper site oxygenases, there are also oxygenases having a single-copper site.35 These interact with the 02 molecule by forming a Cu11—02 complex rather than a Cun(( )Cun complex. 

This trend is due obviously to the relevance of catalytic oxidation to biological processes such as dioxygen transport, and the action of oxygenase and oxidase enzymes related to metabolism. The stmctural and functional modeling of metalloenzymes, particularly of those containing iron and copper, by means of low-molecular complexes of iron, copper, mthenium, cobalt, manganese, etc., have provided a wealth of indirect information helping to understand how the active centers of metalloenzymes may operate. 

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