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

Journal Article · · Journal of the American Chemical Society; (United States)
DOI:https://doi.org/10.1021/ja00174a006· OSTI ID:5452106
;  [1];  [2]
  1. Hebrew Univ. of Jerusalem (Israel)
  2. Ben-Gurion Univ. of the Negev, Beer-Sheva (Israel)

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.

OSTI ID:
5452106
Journal Information:
Journal of the American Chemical Society; (United States), Vol. 112:18; ISSN 0002-7863
Country of Publication:
United States
Language:
English