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

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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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J. Phys. : Solid St. Phys. 4, 2967 (1971) (c) Krishnan, V. : J. Chem. Phys. 68, 660 (1978) (d) Bates, C. : Proc. Phys. Soc. 83, 465 (1964) (e) Dietz, R. E. : Phys. Rev. 132, 1559 (1963) 38. Roberts, J. E. : J. Am. Chem. Soc. 102, 825 (1980) 39. : J. Biochem. (Tokyo) 55, 378 (1964) 40. Solomon, E. I. : J. Am. Chem. Soc. 97, 3878 (1975) Active Sites in Copper Proteins. An Electronic Structure Overview 55 McMiUan, D. , Holwerda, R. , Gray, H. : Proc. Nat. Acad. Sci. USA 71, 1339 (1974) (b) McMillan, D.

An analogous assignment of the 350 nm band as the lowest-energy AI component for this case indicates a reasonable total n~* ~ Cu(II) CT intensity and splitting of the symmetric and antisymmetric components. Finally, the binuclear splitting of each ~t* Cu(II) CT transition can be theoretically removed and the resultant zt~*-zt* splitting ( ~ 12 000 cm -1) of the/~-dioxo geometry is consistent with results obtained for cobalt(III) #-peroxo complexes (vide infra). This treatment and assignment of the charge transfer spectrum of oxy therefore strongly supports the/t-dioxo bridging geometry and finally leads to the spectroscopically effective active site shown in Fig.

It would also test the generality of the transition dipole vector coupling model used in assigning the peroxide bridging geometry of oxy (vide supra) and lead to a better understanding of excited-state distortions of a coupled binuclear site. A recent detailed spectroscopic study96) has addressed an interesting question raised by resonance Raman data of the oxy coupled binuclear site (Fig. 6): no C u - O metal ligand stretch is observed in resonance with the 350" nm O~zc*(A1) ---, Cu(II) C T transition (the - 2 8 0 cm -t vibrations which are enhanced have been associated with Cu-N(His) stretches 97).

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