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Title: A mechanistic study of the copper(II)-peptide-catalyzed superoxide dismutation. A pulse radiolysis study

Abstract

The reactivity of O{sub 2}{sup {minus}} toward Cu(II)-peptides containing glycine and histidine for which E{degree}{sub Cu(III)/Cu(II)} {<=} 1.08 V was investigated by the pulse radiolysis technique. It has been found that the ability of the various complexes to catalyze O{sub 2}{sup {minus}} dismutation depends inversely on the redox potential of the couple Cu(III)/Cu(II). The Cu(II)-peptides containing histidine, which have higher redox potentials than that of the couple O{sub 2}{sup {minus}}/H{sub 2}O{sub 2}, do not catalyze the reaction at all. Although no direct evidence was found for the formation of Cu(III)-peptide, the results suggest that the mechanism of the catalysis of O{sub 2}{sup {minus}} dismutation proceeds via alternate oxidation and reduction of the metal by O{sub 2}{sup {minus}}. Furthermore, this mechanism is supported by indirect observations, which are discussed in detail.

Authors:
;  [1];  [2]
  1. Hebrew Univ. of Jerusalem (Israel)
  2. Ben-Gurion Univ. of the Negev, Beer-Sheva (Israel)
Publication Date:
OSTI Identifier:
5452106
Resource Type:
Journal Article
Journal Name:
Journal of the American Chemical Society; (United States)
Additional Journal Information:
Journal Volume: 112:18; Journal ID: ISSN 0002-7863
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; SUPEROXIDE RADICALS; CHEMICAL REACTIONS; COPPER COMPLEXES; METALLOPROTEINS; PEPTIDES; RADIOLYSIS; SENSITIVITY; SUPEROXIDE DISMUTASE; CHEMICAL RADIATION EFFECTS; COMPLEXES; DECOMPOSITION; ENZYMES; ORGANIC COMPOUNDS; OXIDOREDUCTASES; PROTEINS; RADIATION EFFECTS; RADICALS; TRANSITION ELEMENT COMPLEXES; 550200* - Biochemistry; 560120 - Radiation Effects on Biochemicals, Cells, & Tissue Culture

Citation Formats

Goldstein, S, Czapski, G, and Meyerstein, D. A mechanistic study of the copper(II)-peptide-catalyzed superoxide dismutation. A pulse radiolysis study. United States: N. p., 1990. Web. doi:10.1021/ja00174a006.
Goldstein, S, Czapski, G, & Meyerstein, D. A mechanistic study of the copper(II)-peptide-catalyzed superoxide dismutation. A pulse radiolysis study. United States. https://doi.org/10.1021/ja00174a006
Goldstein, S, Czapski, G, and Meyerstein, D. 1990. "A mechanistic study of the copper(II)-peptide-catalyzed superoxide dismutation. A pulse radiolysis study". United States. https://doi.org/10.1021/ja00174a006.
@article{osti_5452106,
title = {A mechanistic study of the copper(II)-peptide-catalyzed superoxide dismutation. A pulse radiolysis study},
author = {Goldstein, S and Czapski, G and Meyerstein, D},
abstractNote = {The reactivity of O{sub 2}{sup {minus}} toward Cu(II)-peptides containing glycine and histidine for which E{degree}{sub Cu(III)/Cu(II)} {<=} 1.08 V was investigated by the pulse radiolysis technique. It has been found that the ability of the various complexes to catalyze O{sub 2}{sup {minus}} dismutation depends inversely on the redox potential of the couple Cu(III)/Cu(II). The Cu(II)-peptides containing histidine, which have higher redox potentials than that of the couple O{sub 2}{sup {minus}}/H{sub 2}O{sub 2}, do not catalyze the reaction at all. Although no direct evidence was found for the formation of Cu(III)-peptide, the results suggest that the mechanism of the catalysis of O{sub 2}{sup {minus}} dismutation proceeds via alternate oxidation and reduction of the metal by O{sub 2}{sup {minus}}. Furthermore, this mechanism is supported by indirect observations, which are discussed in detail.},
doi = {10.1021/ja00174a006},
url = {https://www.osti.gov/biblio/5452106}, journal = {Journal of the American Chemical Society; (United States)},
issn = {0002-7863},
number = ,
volume = 112:18,
place = {United States},
year = {Wed Aug 29 00:00:00 EDT 1990},
month = {Wed Aug 29 00:00:00 EDT 1990}
}