Thiolate Ligands in Metallothionein Confer Redox Activity on Zinc Clusters

Thiolate Ligands in Metallothionein Confer Redox Activity on Zinc Clusters

We postulate a novel and general mechanism in which the redox-active sulfur donor group of cyst(e)ine confers oxidoreductive characteristics on stable zinc sites in proteins. Thus, the present, an earlier, and accompanying manuscripts [Maret, W., Larsen, K. S. & Vallee, B. L. (1997) Proc. Natl....

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1998-03, Vol.95 (7), p.3478-3482
Hauptverfasser: Maret, Wolfgang, Vallee, Bert L.
Format: Artikel
Sprache:eng
Schlagworte:
Atoms
Biochemistry
Biological Sciences
Disulfides
Escherichia coli
Kinetics
Ligands
Metallothionein - chemistry
Oxidation
Oxidation-Reduction
Proteins
Sulfur
Sulfur - chemistry
Thiols
Zinc
Zinc - chemistry
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Zusammenfassung:We postulate a novel and general mechanism in which the redox-active sulfur donor group of cyst(e)ine confers oxidoreductive characteristics on stable zinc sites in proteins. Thus, the present, an earlier, and accompanying manuscripts [Maret, W., Larsen, K. S. & Vallee, B. L. (1997) Proc. Natl. Acad. Sci. USA 94, 2233-2237; Jiang, L.-J., Maret, W. & Vallee, B. L. (1998) Proc. Natl. Acad. Sci. USA 95, 3483-3488; and Jacob, C., Maret, W. & Vallee, B. L. (1998) Proc. Natl. Acad. Sci. USA 95, 3489-3494] demonstrate that the interactive network featuring multiple zinc/sulfur bonds as found in the clusters of metallothionein (MT) constitutes a coordination unit critical for the concurrent oxidation of cysteine ligands and the ensuing release of zinc. The low position of MT (
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.95.7.3478