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| Citation key | ISI:A1997XU08200005 |
|---|---|
| Author | Sokolowski, A and Leutbecher, H and Weyhermuller, T and Schnepf, R and Both, E and Bill, E and Hildebrandt, P and Wieghardt, K |
| Pages | 444-453 |
| Year | 1997 |
| ISSN | 0949-8257 |
| Address | 175 FIFTH AVE, NEW YORK, NY 10010 |
| Journal | J. Biol. Inorg. Chem. |
| Volume | 2 |
| Number | 4 |
| Month | AUG |
| Publisher | SPRINGER VERLAG |
| Abstract | The reaction of the macrocycles 1,4,7-tris (3,5-di-tert-butyl-2-hydroxy-benzyl)-1,4,7-triazacyclononane, (LH3)-H-1, or 1,4,7-tris(3-tert-butyl-5-methoxy-2-hydroxy-benzyl)-1,4,7-triazacyclonon ane, (LH3)-H-2, with CU(ClO4)(2) . 6H(2)O in methanol (in the presence of Et3N) affords the green complexes [Cu-II((LH)-H-1)] (1), [Cu-II((LH)-H-2)]. CH3OH (2) and (in the presence of HClO4) [Cu-II((LH2)-H-1)](ClO4) (3) and [CUII((LH2)-H-2)] (ClO4) (4). The Cu-II ions in these complexes are five-coordinate (square-base pyramidal), and each contains a dangling, uncoordinated pendent arm (phenol). Complexes 1 and 2 contain two equatorially coordinated phenolate ligands, whereas in 3 and 4 one of these is protonated, affording a coordinated phenol. Electrochemically, these complexes can be oxidized by one electron, generating the phenoxyl-copper(II) species [Cu-II((LH)-H-1)](+.), [Cu((LH)-H-2)](+.), [Cu-II((LH2)-H-1)](2+.), and [Cu-II((LH2)-H-2)](2+); all of which are EPR-silent. These species are excellent models for the active form of the enzyme galactose oxidase (GO). Their spectroscopic features (UV-VIS, resonance Raman) are very similar to those reported for GO and unambiguously show that the complexes are phenoxyl-copper(II) rather than phenolato-copper(III) species. |
| Bibtex Type of Publication | Article |
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