Role of metal complexes in the formation-detoxication action of active oxygen species

doi:10.1016/0302-4598(87)85004-3

Bioelectrochemistry and Bioenergetics

Volume 18, Issues 1–3, December 1987, Pages 21-28

Bioelectrochemistry ...

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Abstract

A general mechanism for the action of metal compounds either in enhancing the biological damage induced by active oxygen species or in protecting the biological target against these species is proposed. The effect of several copper complexes and iron and copper bleomycin complexes on DNA cleavage is discussed in view of this mechanism.

References (51)

S.D. Aust et al.
J. Free Rad. Biol. Med.
(1985)
C.C. Winterbourn et al.
Arch. Biochem. Biophys.
(1984)
R.C. Lynch et al.
Biochim. Biophys. Acta
(1979)
K.L. Fong et al.
Chem. Biol. Inter.
(1976)
S. Goldstein et al.
J. Free Rad. Biol. Med.
(1985)
R. Brigelius et al.
FEBS Lett.
(1974)
M. Younes et al.
Biochem. Biophys. Res. Commun.
(1978)
E.A. Sausville et al.
Biochem. Biophys. Res. Commun.
(1976)
R.M. Burger et al.
J. Biol. Chem.
(1981)
J.M.C. Gutteridge et al.
Biochem. Inter.
(1985)

E.A. Sausville et al.

Biochemistry

(1978)

J.W. Lown et al.

Biochemistry

(1977)

J.R.F. Muidini et al.

FEBS Lett.

(1984)

R. Cone et al.

Can. J. Biochem.

(1976)

R. Kohen et al.

Free Rad. Res. Commun.

(1985)

A.C.M. Filho et al.

Biochem. J

(1984)

B.M. Babior

N. Engl. J. Med.

(1978)

B. Hammond et al.

Can. J. Physiol. Pharmacol.

(1985)

F. Haber et al.

Proc. R. Soc. London, Ser. A

(1934)

W.H. Koppenol et al.

Photochem. Photobiol.

(1978)

G. Czapski et al.

Photochem. Photobiol.

(1978)

E.W. Kellog et al.

J. Biol. Chem.

(1975)

J.J. Van Hemmen et al.

Biochim. Biophys. Acta

(1975)

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^☆: Presented at the Bioelectrochemical Society Meeting on “Formation and Reactions of Peroxides in Biological Systems”, Obernai, 22–24 October 1986.

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Role of metal complexes in the formation-detoxication action of active oxygen species☆

Abstract

J. Free Rad. Biol. Med.

Arch. Biochem. Biophys.

Biochim. Biophys. Acta

Chem. Biol. Inter.

J. Free Rad. Biol. Med.

FEBS Lett.

Biochem. Biophys. Res. Commun.

Biochem. Biophys. Res. Commun.

J. Biol. Chem.

Biochem. Inter.

Biochemistry

Biochemistry

FEBS Lett.

Can. J. Biochem.

Free Rad. Res. Commun.

Biochem. J

N. Engl. J. Med.

Can. J. Physiol. Pharmacol.

Proc. R. Soc. London, Ser. A

Photochem. Photobiol.

Photochem. Photobiol.

J. Biol. Chem.

Biochim. Biophys. Acta