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33) where the optical and CD feature at - 570 nm and the CD feature at - 480 nm correspond to these two transitions. Only one component of the higher-energy n~* ~ Cu(II) CT transition, the 350 nm optical peak, can be observed due to the intense UV protein absorption. This is assigned as the A~ component sT). The energy and intensity of these CT transitions can be correlated with the results of a simple model 66) to predict the likely bridging mode of peroxide at the site. CT transitions for two possible bridging geometries,/~-dioxo and/~-monooxo, can be treated as transition dipole vectors.
Acta 243, 203 (1971) 26. Rotilio, (3. : Biochemistry 11, 2187 (1972) 27. Lieberman, R. , Sands, R. , Fee, J. : J. Biol. Chem. 257, 336 (1982) 28. Tainer, J. A. ) Richardson, D. C. and Richardson, J. , Brookhaven Protein Structure Data Bank 1980 29. , Coleman, J. : J. Biol. Chem. 248, 3855 (1973) 30. : Struct. Bonding (Berlin) 17, 1 (1973) 31. (a) Fee, J. , (3aber, B. : J. Biol. Chem. , chapter 15, New York, Academic 1978 (c) Fee, J. , Mires, W. : J. Biol. Chem. 256, 1910 (1981) 32. , Malmstr6m, B.
Since EXAFS studies 82,83) have indicated that sulfur is not strongly interacting with the protein site, this leaves nitrogen and oxygen donor ligands as possible endogenous bridges. Model studies (see Table 4) have indicated that of possible biological ligands, only phenoxide, alkoxide or hydroxide bridges are capable of mediating the large exchange interaction found in the coupled binuclear copper protein site. This coupling is strongly dependent on the Cu-O-Cu angle (Goodenough-Kanamori rulesSS)), where angles approaching 180° are required for effective superexchange interaction and large antiferromagnetic splittings.