Copper, Molybdenum, and Vanadium in biological systems by B.A. Averill, N.D. Chasteen, K. Kustin, G.C. McLeod, K.W.

By B.A. Averill, N.D. Chasteen, K. Kustin, G.C. McLeod, K.W. Penfield, E.I. Solomon, D.E. Wilcox

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Stoichiometrie addition of peroxide to native Rhus laccase at pH = 7 produces an increase in absorption I°2) at ~ 330 nm (Ae -- 800 M -1 cm -1) with no change in the EPR spectrum. While this demonstrates that peroxide binds to native laccase with an extremely high affinity at pH ~ 7, it is not clear whether these spectral changes are new O~ --, Cu(II) CT transitions or perturbations of the existing 330 nm band (vide infra). An important laccase derivative can be prepared :°3) that has the type 2 copper removed (Fig.

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. ) Nord, F. , p. 177, New York, Interscience 1970 33. Fee, J. : Struct. Bonding (Berlin) 23, 1 (1975) 34. Solomon, E. , Hare, J. , Gray, H. : Proc. Nat. Acad. Sci. USA 73, 1389 (1976) 35. Solomon, E.

Elimination of sulfur ligation leaves the most reasonable assignment of this feature as a phenolate-to-copper(II) CT transition (see Table 4). This indicates that tyrosine is bound to the binuclear cupric site and the most likely candidate for the endogenous bridge. Table 4. Properties of copper(II) complexes with phenolate, alkoxide and hydroxide ligands A. Optical features and exchange coupling for structurally defined binuclear copper(II) complexes Bridging Complex ligand type Cu +2 Geometry - 2J (cm-1) CT (nm) a d-d(2=a,) (nm) a Ref.

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