Toward synthetic analogues of linked redox and catalytic multimetal sites in proteins

A model of the histidine-cysteine bridged dicopper array

Way-Zen Lee, William B. Tolman

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

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, LCuSCPh3 and LCu-(py) (L = β-diketiminate, py = pyridyl), confirmed retention of the dicopper structure in solution.

Original languageEnglish
Pages (from-to)5656-5658
Number of pages3
JournalInorganic Chemistry
Volume41
Issue number22
DOIs
Publication statusPublished - 2002 Nov 4

Fingerprint

Nitrite Reductases
histidine
nitrites
oxidase
X ray crystallography
X Ray Crystallography
cysteine
Staphylococcal Protein A
Histidine
Cyclic voltammetry
crystallography
Oxidation-Reduction
Cysteine
Catalytic Domain
Oxidoreductases
electron transfer
Electrons
analogs
Ligands
proteins

ASJC Scopus subject areas

  • Inorganic Chemistry

Cite this

Toward synthetic analogues of linked redox and catalytic multimetal sites in proteins : A model of the histidine-cysteine bridged dicopper array. / Lee, Way-Zen; Tolman, William B.

In: Inorganic Chemistry, Vol. 41, No. 22, 04.11.2002, p. 5656-5658.

Research output: Contribution to journalArticle

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