Specific Oxidation of Copper Binding Sites in Copper (II) -Oligopeptide Complexes

Alexander Levitzki; Arieh Berger

doi:10.1021/bi00777a010

Specific Oxidation of Copper Binding Sites in Copper (II) -Oligopeptide Complexes

Alexander Levitzki
, Arieh Berger

Alexander Silberman Institute of Life Sciences

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

The specific oxidation of the copper(II) binding sites by chloroiridate in two peptide-copper complexes is described. The octapeptide and the 20-peptide derived from the amino terminal of RNase were used to prepare the 1:1 copper complexes. In both cases the copper was found to bind to the a-amino end of the molecule, using the chloroiridate oxidation technique. The possibility of using this or similar reactions for locating copper binding sites in proteins is discussed.

Original language	English
Pages (from-to)	64-66
Number of pages	3
Journal	Biochemistry
Volume	10
Issue number	1
DOIs	https://doi.org/10.1021/bi00777a010
State	Published - 1 Jan 1971

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abstract = "The specific oxidation of the copper(II) binding sites by chloroiridate in two peptide-copper complexes is described. The octapeptide and the 20-peptide derived from the amino terminal of RNase were used to prepare the 1:1 copper complexes. In both cases the copper was found to bind to the a-amino end of the molecule, using the chloroiridate oxidation technique. The possibility of using this or similar reactions for locating copper binding sites in proteins is discussed.",

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N2 - The specific oxidation of the copper(II) binding sites by chloroiridate in two peptide-copper complexes is described. The octapeptide and the 20-peptide derived from the amino terminal of RNase were used to prepare the 1:1 copper complexes. In both cases the copper was found to bind to the a-amino end of the molecule, using the chloroiridate oxidation technique. The possibility of using this or similar reactions for locating copper binding sites in proteins is discussed.

AB - The specific oxidation of the copper(II) binding sites by chloroiridate in two peptide-copper complexes is described. The octapeptide and the 20-peptide derived from the amino terminal of RNase were used to prepare the 1:1 copper complexes. In both cases the copper was found to bind to the a-amino end of the molecule, using the chloroiridate oxidation technique. The possibility of using this or similar reactions for locating copper binding sites in proteins is discussed.

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Specific Oxidation of Copper Binding Sites in Copper (II) -Oligopeptide Complexes

Abstract

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