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Anion complexes of copper ii and cobalt ii bovine carbonic anhydrase ec 4.2.1.1 as models for the copper site of blue copper proteins



Anion complexes of copper ii and cobalt ii bovine carbonic anhydrase ec 4.2.1.1 as models for the copper site of blue copper proteins



European Journal of Biochemistry 64(2): 453-457



The presence of 2 intense transitions in the optical absorption spectrum of the sulfide and 2-mercaptoethanol complexes of Cu(II) and Co(II)-substituted bovine carbonic anhydrase [EC 4.2.1.1] suggests that charge-transfer interactions between S and an acceptor group of the protein play an important role in the stabilization of these complexes. The spectra of Co(II) bovine carbonic anhydrase sulfides are similar to the spectrum of Co(II) stellacyanin while the spectra of the corresponding Cu(II) enzymes are different. A possible explanation is that Cu(II) is pentacoordinate in native stellacyanin unlike Cu(II) bovine carbonic anhydrase sulfides and Co(II) enzymes. Tetrahedral Co(II) stellacyanin is proposed as a model of the reduced Cu site.

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