Toward Synthetic Analogues of Linked Redox and Catalytic Multimetal Sites in Proteins: A Model of the Histidine−Cysteine Bridged Dicopper Array
In: Inorganic Chemistry, Jg. 41 (2002-10-03), S. 5656-5658
Online
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Zugriff:
Contiguous HisCys residues link a type 1 Cu electron-transfer site to a catalytic Cu-containing site in nitrite reductase and the multicopper oxidases. In efforts to understand the role of the linker in these multimetallic arrays and to design new catalysts, a mixed-valent dicopper complex comprising a bridging thiolate/N-donor ligand that models the CuHisCysCu motif was prepared and characterized by X-ray crystallography. Comparison of spectroscopic and cyclic voltammetry data to those of the mononuclear analogues of each portion of the complex, LCuSCPh(3) and LCu(py) (L = beta-diketiminate, py = pyridyl), confirmed retention of the dicopper structure in solution.
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Toward Synthetic Analogues of Linked Redox and Catalytic Multimetal Sites in Proteins: A Model of the Histidine−Cysteine Bridged Dicopper Array
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Autor/in / Beteiligte Person: | Way Zen Lee ; Tolman, William B. |
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Zeitschrift: | Inorganic Chemistry, Jg. 41 (2002-10-03), S. 5656-5658 |
Veröffentlichung: | American Chemical Society (ACS), 2002 |
Medientyp: | unknown |
ISSN: | 1520-510X (print) ; 0020-1669 (print) |
DOI: | 10.1021/ic025937a |
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