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Very little is known of the metabolism of copper on a molecular level. For example, there is no evidence of an oxidative breakdown of Cu(I)-thionein leading to Cu(II). Thus it was of interest to use L- and D-amino-acid oxidases, amino oxidase and galactose oxidase to control the oxidation of Cu(I)-thionein by enzymically generated H2O2. In the presence of these enzymes Cu(II) was generated in each case. In a more detailed study the Cu(I)-thiolate chromophores of Cu-thionein were oxidized in the presence of xanthine oxidase as deduced from spectrometrical measurements using EPR and circular dichroism. Unlike Cu2Zn2-superoxide dismutase catalase inhibited the oxidative cleavage, suggesting peroxide as the actual oxidizing agent. Possibly there is an enzymic oxidative pathway for the generation of biologically important Cu(II).
H J Hartmann, and
A Gärtner, and
U Weser
January 1985,
Journal of free radicals in biology & medicine,
H J Hartmann, and
A Gärtner, and
U Weser
October 1996,
Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine,
H J Hartmann, and
A Gärtner, and
U Weser
October 1977,
The Journal of biological chemistry,
H J Hartmann, and
A Gärtner, and
U Weser
June 1979,
Biochimica et biophysica acta,
H J Hartmann, and
A Gärtner, and
U Weser
April 1978,
Biochemical and biophysical research communications,
H J Hartmann, and
A Gärtner, and
U Weser
January 1989,
Biology of metals,
H J Hartmann, and
A Gärtner, and
U Weser
March 1986,
FEBS letters,
H J Hartmann, and
A Gärtner, and
U Weser
November 1986,
The Biochemical journal,
H J Hartmann, and
A Gärtner, and
U Weser
May 1996,
Journal of inorganic biochemistry,
H J Hartmann, and
A Gärtner, and
U Weser
January 1998,
Advances in experimental medicine and biology,
