The Superoxide Dismutase-Like Activity of Some Copper (II) Complexes Derived from Tridentate Schiff Bases

References

• McCord J. M., Day E. D., Jr. Superoxide-dependent production of hydroxyl radical catalyzed by iron-EDTA complex. FEBS Letters. 1978; 86: 139–142
   PubMed Web of Science ®Google Scholar
• Sies H. biochemistry of oxidative stress. Angewandte Chemie. 1986; 25: 1058–1071
   Google Scholar
• McCord J. M., Fridovich I. Superoxide dismutase: An enzymic functin for erythrocuprein (hemocuprein). Journal of Biological Chemistry. 1969; 244: 6049–6055
   PubMed Web of Science ®Google Scholar
• Fee J. A., Valentine J. S. Chemical and physical properties of superoxide. Superoxde and Superoxide Dismutases, A. M. Michelson, J. M. McCord, I. Fridovich. Academic Press, New York 1977; 19–60
   Google Scholar
• Fridovich I. Biological effects of the superoxide radical. Archives of Biochemistry and Biophysics. USA 1986; 247: 1–11
   PubMed Web of Science ®Google Scholar
• Haber F., Weiss J. the catalytic decomposition of hydrogen peroxide by iron salts. Proceedings of the Royal Society of Medicine (London), Ser. A 1934; 147: 332–351
   Google Scholar
• Fenton H. J. H. Oxidation of tartaric acid in presence of iron. Journal of Chemical Society. 1894; 6: 899–910
   Google Scholar
• Southorn P. A., Powis G. Free radicals in medicine I. Chemical nature and biologic reactions. Mayo Clinic Proceedings. 1988; 63: 381–388
   PubMed Web of Science ®Google Scholar
• Michelson A. M. Clinical use of superoxide dismutase and possible pharmacological approaches. Pathology of Oxygen, A. P. Autor. Academic Press, New York 1982; 277–302
   Google Scholar
• Archibald F. S., Fridovich I. Manganese and defense against oxygen toxicity in Lactobacil-lus plantarum. Journal of Bacteriology. 1981; 145: 442–451
   PubMed Web of Science ®Google Scholar
• Soldanova J., Kritsmar-Smogrovif J., Pavelfik F., Seressova V., Zcaron;emlička M. (1987) Structure and properties of Diaqua(N-salicylidene-L-glutamato)copr(II) monohydrate. Proceedings of the 11th Conference on Coordination Chemistry. 1987. Smolenice. ČSSR., 365–370
   Google Scholar
• Sivý J., Pavelčik F., Kratsmar-Šmogrovif J., Zcaron;emlička M. The crystal and molecular structure and properties of potassium (isothiocyanato)-(N-salicylidene-D, L-phenylalaninato) cuprate. Proceedings of the 12th Conference on Coordination Chemistry. Smolencie. ČSSR 1989; 343–348
   Google Scholar
• Younes M., Langfelder W., Zienoan S., Weser U. Radiolytically generated superoxide and Cu(II)-salicylates. Biochemical and Biophysical Reserch Commimications. 1978; 81: 576–580
   PubMed Web of Science ®Google Scholar
• Amar C., Vilkas E., Foos J. Catalytic activity studies of some copper(II)-histidine-containing dipeptide complexes on aqueous superoxide ion dismutation. Journal of Inorganic Biochemistry. 1982; 17: 313–323
   Web of Science ®Google Scholar
• Sorenson J. R. J. Copper complexes a physiological approach to treatment of chronic disease. Comprehensive Therapy 1985; 11: 49–64
   PubMedGoogle Scholar
• Jouini M., Lapluye G., Huet J., Julien R., Ferrddini C. Catalytic activity of a copper (II)-oxidized glutathione complex on aqueous superoxide ion dismutation. Journal of Inorganic Biochemistry. 1986; 26: 269–280
   PubMed Web of Science ®Google Scholar
• Auclair C., Gautero H., Boivin P. Effects of salicylate copper complex on the metabolic activation in hagocytizing granulocytes. Biochemical Pharmacology 1980; 29: 3105–3109
   PubMed Web of Science ®Google Scholar
• Kritsmar-Šmogrovič J., Bergendi L., Šuračková Z., Scaron;vajlenova O., Seressová V. Method of influencing of the SOD activity of the Cu(II) by its chelating with Schiff base anions. Czechoslovak Applied 1988; 04947–88
   Google Scholar
• Krätsmár-Smogrovič J., Scaron;vajlenová O., Varkonda S., Konečny V. Coordination compounds of the (N-salicylidene-3-alaninato)-thiocyanatocuprate type and the method of their preparing. Czechoslovak applied 04272–88. 1988
   Google Scholar
• Bøyum A. Isolation of lymphocytes, granulocytes and macrophages. Scandinavian Journal of Immunology. Suppl. 1976; 5: 9–15
   Google Scholar
• Bergendi L., Ďuračková Z. Superoxide anion production after phagocytosis by pig leukocytes. Bioldgia (Bratislava) 1980; 35: 435–444
   Web of Science ®Google Scholar
• Babior B. M., Kipnes R. S., Curnutte J. T. Biological defense mechanisms. The production by leukocytes of superoxide a potential bactericidal agent. Journal of Cloinical Investigtion. 1973; 52: 741–744
   PubMed Web of Science ®Google Scholar
• Karnovsky M. L. Biochemical aspects of the functions of polyrnorphonuclearand mononuclear leukocytes. The Phagocytic Cell in Host Resistance, J. A. Bellanti, D. H. Dayton. Raven Press, New York 1975; 25–43
   Google Scholar
• Tainer J. A., Getzoff E. D., Beem K. M., Richardson J. S., Richardson D. C. Determination and analysis of the 2 A structure of copper, zinc superoxide dismutase. Journal of Molecular Biology. 1982; 160: 181–217
   PubMed Web of Science ®Google Scholar
• Minotti G., Aust S. D. Superoxide-dependent redox cycling of citrdte-Fe3+: Evidence for a superoxide disrnutaselike activity. Archives of Biochemistry and Biophysics. 1987; 253: 257–267
   PubMed Web of Science ®Google Scholar
• Salin M. L., McCord J. M. Free radicals and inflammation. Protection of phagocytosing leukocytes by silperoxide dismutase. Journal of clinical Investigation. 1975; 56: 1319–1323
   PubMed Web of Science ®Google Scholar
• Babior B. M., Kipnes R. S., Curnutte J. T. Biologicdl defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent. Journal of Clinical Investigation. 1973; 2: 741–744
   Google Scholar
• Sawyer D. T., Valentine J. S. How super is superoxid?. Accounts of chemical Research. 1981; 14: 393–400
   Web of Science ®Google Scholar
• Joester K. E., Jung G., Weber U., War U. Superoxide dismutase activity of Cu2+ amino acid chelates. FEBS Letters 1972; 25: 25–28
   PubMed Web of Science ®Google Scholar
• Robertson P., Fridovich I. Does copper-D-penicillamine catalyze the dismutation of O2-?. Archives of Biochemistry and Biophysics 1980; 203: 830–831
   PubMed Web of Science ®Google Scholar
• Kubota S., Yang J. T. Bis[Cyclo(histidylhistidine)] copper(II) complex that mimicks the active center of superoxide dismutase has its catalytic activity. Proceedings of the National Academy of Sciences. USA 1984; 81: 3283–3286
   PubMed Web of Science ®Google Scholar
• Czapski G., Goldstein S. When do metal complexes protect the biological system from superoxide toxicity and when do they enhance it?. Free Rodicol Reseurch Communications. 1986; 1: 157–161
   PubMedGoogle Scholar