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Binding sites Binuclear copper complexes

The majority of cyanide-bridged dinuclear complexes described for the combination of metal ions belong to the biologically relevant class of Cu —Fe dimers. These compounds serve as models for the binuclear cyanide-inhibited site of cytochrome c oxidase, an enzyme that contains the heme-copper active site responsible for the O2 reduction chemistry (59). The lethal toxicity of cyanide was traced to its irreversible binding and inhibition of this active site in the enzyme (60). The biologically relevant aspects of these complexes were the subject of many reports (61,62). Our interest is in describing their crystal structure, which will be correlated to the magnetic properties in a later section. [Pg.170]


See other pages where Binding sites Binuclear copper complexes is mentioned: [Pg.199]    [Pg.540]    [Pg.199]    [Pg.13]    [Pg.116]    [Pg.130]    [Pg.204]    [Pg.130]    [Pg.131]    [Pg.205]    [Pg.121]    [Pg.264]    [Pg.3718]    [Pg.348]    [Pg.61]    [Pg.201]    [Pg.752]    [Pg.324]    [Pg.15]    [Pg.52]    [Pg.2148]    [Pg.6375]    [Pg.2147]    [Pg.6374]    [Pg.441]    [Pg.64]    [Pg.452]    [Pg.980]    [Pg.33]   
See also in sourсe #XX -- [ Pg.216 ]




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