84
Views
35
CrossRef citations to date
0
Altmetric
Original Article

Inactivation of Yeast Glutathione Reductase by Fenton Systems: Effect of Metal Chelators, Catecholamines and Thiol Compounds

&
Pages 543-555 | Received 17 Jan 1997, Published online: 07 Jul 2009

References

  • Williams C. H. J. Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase and mercuric reductase. A family of flavoenzyme transhydrogenase in Chemistry and biochemistry of flavoenzymes, Vol. 3, F. Müller. CRC Press, Boca Raton, FL 1992; 121–211
  • Rietveld P., Arscott L. D., Berry A., Scrutton N. S., Deonarain M. P., Perham R. N., Williams C. H. Reductive and oxidative half-reactions of glutathione reductase from Escherichia coli. Biochemistry 1994; 33: 13888–13895
  • Collinson L. P., Dawes I. W. Isolation, characterization and overexpression of the yeast gene, GRL1, encoding glutathione reductase. Gene 1995; 156: 123–127
  • Schirmer R. H., Müller J. G., Krauth-Siegel L. Disulfide-reductase inhibitors as chemotherapeutic agents: the design of drugs for trypanosomiasis and malaria. Angewandte Chemie-International Edition in English 1995; 34: 141–154
  • Krauth-Siegel R. L., Schoneck R. Trypanothione reductase and lipoamide dehydrogenase as targets for a structure-based drug design. Faseb Journal 1995; 9: 1138–1146
  • Gutierrez Correa J., Stoppani A. O. M. Inactivation of lipoamide dehydrogenase by cobalt(II) and iron(II) Fenton systems: effect of metal chelators, thiol compounds and adenine nucleotides. Free Radical Research Communications 1993; 19: 303–314
  • Gutierrez Correa J., Stoppani A. O. M. Inactivation of heart lipoamide dehydrogenase by copper Fenton systems. Effect of thiol compounds and metal chelators. Free Radical Research 1995; 22: 239–250
  • Gutierrez Correa J., Stoppani A. O. M. Catecholamines enhance dihydrolipoamide dehydrogenase inactivation by the copper Fenton system. Enzyme protection by copper chelators. Free Radical Research 1996; 25: 311–322
  • Grant C. M., Dawes I. W. Synthesis and role of glutathione in protection against oxidative stress in yeasts. Redox Report 1996; 2: 223–229
  • Sreider C. M., Grinblat L., Stoppani A. O. M. Catalysis of nitrofuran redox-cycling and superoxide anion production by heart lipoamide dehydrogenase. Biochemical Pharmacology 1990; 40: 1849–1857
  • Childs R. E., Bardsley W. G. The steady-state kinetics of peroxidase with 2, 2′-azino-di-(3-ethyl-ben-zthiazolined-sulphonic acid) as chromogen. Biochemical Journal 1975; 145: 93–103
  • Wolfenden B. S., Willson R. L. Radical cations as reference chromogens in kinetic studies of one-electron transfer reactions: pulse radiolysis studies of 2, 2′-azinobis-(3-ethylbenzthiazolie-6-sulphonate). Journal of Chemistry Society Perkin Transaction 1982; II: 805–812
  • Gutteridge J. M. C. Ferrous-salt-promoted damage to deoxyribose and benzoate. Biochemical Journal 1987; 243: 709–714
  • Holler T. P., Hopkins P. B. A qualitative fluorescence-based assay for tyrosyl radical scavenging activity: ovothiol A is an efficient scavenger. Analytical Biochemistry 1989; 180: 326–330
  • Moreaux V., Birlouez-Aragon I., Ducauze C. Copper chelation by tryptophan inhibits the copper-ascorbate oxidation of tryptophan. Redox Report 1996; 2: 191–197
  • Halliwell B., Gutteridge J. M. C. Free Radicals in Biology and Medicine 2nd. Clarendon Press, Oxford 1989
  • Stadtman E. R. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annual Review of Biochemistry 1993; 62: 797–821
  • Marx G., Chevion M. Site.specific modifications of albumin by free radicals. Reactions with copper(II) and ascorbate. Biochemical Journal 1985; 236: 397–400
  • Ozawa T., Ueda J., Hanaki A. Copper(II)-albumin complex can activate hydrogen peroxide in the presence of biological reductants; first ESR evidence for the formation of hydroxyl radical. Biochemical and Molecular Biology International 1993; 29: 247–253
  • Rowley D. A., Halliwell B. Formation of hydroxyl radicals from NADH and NADPH in the presence of copper salts. Journal of Inorganic Biochemistry 1985; 23: 103–108
  • Oikawa S., Kawanishi S. Site-specific DNA damage induced by NADH in the presence of copper(II): role of active oxygen species. Biochemistry 1996; 35: 4584–4590
  • Wardman P., von Sonntag C. Kinetic factors that control the fate of thiyl radicals in cells. Methods in Enzymology 1995; 251: 31–45
  • Wardman P. Reactions of thiyl radicals. Biothiols in health and disease, L. Packer, E. Cadenas. M. Dekker, Inc., New York 1995; 1–19
  • Davidson J. F., Whyte B., Bissinger P. H., Schiestl R. H. Oxidative stress is involved in heat-induced cell death in. Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences of the United States of America 1996; 93: 5116–5121
  • Van Steveninck J., Van der Zee J., Dubbelman T. M. A. R. Site-specific and bulk-phase generation of hydroxyl radicals in the presence of cupric ions and thiol compounds. Biochemical Journal 1985; 232: 309–311
  • Gunther M. R., Hanna P. M., Mason R. P., Cohen M. S. Hydroxyl radical formation from cuprous ion and hydrogen peroxide: a spin-trapping study. Archives of Biochemistry and Biophysics 1995; 316: 515–522
  • Hanna P. M., Mason R. P. Direct evidence for inhibition of free radical formation from Cu(I) and hydrogen peroxide by glutathione and other potential ligands using the EPR spin-trapping technique. Archives of Biochemistry and Biophysics 1992; 295: 205–213
  • Shinar E., Navok T., Chevion M. The analogous mechanisms of enzymatic inactivation induced by ascorbate and superoxide in the presence of copper. Journal of Biological Chemistry 1983; 258: 14778–14783
  • Kanazawa H., Fujimoto S., Ohara A. Inactivation of cholinesterase by ascorbic acid in the presence of cupric ions: a possible mechanism for the inactivation of an enzyme by the metal-catalyzed oxidation system. Biology and Pharmacology Bulletin 1995; 18: 1179–1183
  • Halliwell B. Vitamin C: antioxidant or prooxidant in vivo?. Free Radical Research 1996; 25: 439–454
  • Ueda J.-I., Shimazu Y., Ozawa T. Reactions of copper(II)-oligopeptide complexes with hydrogen peroxide: effects of biological reductants. Free Radical Biology and Medicine 1995; 18: 929–933
  • Goldstein S., Czapski G. The role and mechanism of metal ions and their complexes in enhancing damage in biological systems or in protecting these systems from the toxicity of O2. Free Radical Biology and Medicine 1986; 2: 3–11
  • Shi X., Dalal N. S. NADPH-dependent flavoenzymes catalyze one electron reduction of metal ions and molecular oxygen, and generate hydroxyl radicals. FEBS Letters 1990; 276: 189–191
  • Arscott L. D., Thorpe C., Williams C. H., Jr. Glutathione reductase from yeast. Differential reactivity of the nascent thiols in two electron reduced enzyme and properties of a monoalkylated derivative. Biochemistry 1981; 20: 1513–1524
  • Dean R. T., Wolff S. P., McElligott M. A. Histidine and proline are important sites of free radical damage to proteins. Free Radical Research Communications 1989; 7: 97–103
  • Mattevi A., Schierbeek C. H., Hol W. G. J. Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 resolution. A comparison with the structure of glutathione reductase. Journal of Molecular Biology 1991; 220: 975–995
  • O'Brien J. P. Radical formation during the peroxidase catalyzed metabolism of carcinogens and xenobiotics: the reactivity of these radicals with GSH, DNA and unsaturated lipids. Free Radical Biology and Medicine 1988; 4: 169–183
  • Yamakura F. Destruction of tryptophan residues by hydrogen proxide in iron-superoxide dismutase. Biochemical and Biophysical Research Communications 1984; 122: 635–641
  • Milne L., Nicotera P., Orrenius S., Burkitt M. J. Effects of glutathione and chelating agents on copper-mediated DNA oxidation: pro-oxidant and antioxidant pl'operties of glutathione. Archives of Biochemistry and Biophysics 1993; 304: 102–109
  • Spear N., Aust S. D. Hydroxylation of deoxyguanosine in DNA by copper and thiols. Archives of Biochemistry and Biophysics 1995; 317: 142–148
  • Kamidate T., Kinkou T., Watanabe H. Role of amino tluols in luminol chemiluminescence coupled with copper(II)-catalyzed oxidation of cysteine and glutathione. Journal of Bioluminescence and Chemihminescence 1996; 11: 123–129
  • Presta A., Stillman M. J. Chiral copper(I)-thiolate clusters in metallothionein and glutathione. Chirality 1994; 6: 521–530
  • Corazza A., Harvey I., Sadler P. J. 1H, 13-NMR and X-ray absorption studies of copper(I) glutathione complexes. European Journal of Biochemistry 1996; 236: 697–705
  • Wefers H., Sies H. Oxidation of glutathione by the superoxide radical to the disulfide and the sulfonate yielding singlet oxygen. European Journal of Biochemistry 1983; 137: 29–36
  • Dikalov S., Khramtsov V., Zimmer G. Determination of rate constants of the reactions of thiols with superoxide radical by electron paramagnetic resonance: critical remarks on spectrophotometric approaches. Archives of Biochemistry and Biophysics 1996; 326: 207–218
  • Reguli J., Misik V. Superoxide scavenging by thiol/copper complex of Captopril-An EPR spectroscopic study. Free Radical Research 1995; 22: 123–130
  • Packer L., Witt E. H., Tritschler H. J. Alphalipoic acid as a biological antioxidant. Free Radical Biology and Medicine 1995; 19: 227–250
  • Baker W. L. Disulfide inhibition of copper-catalyzed oxidation of ascorbic acid: spectrophotometric evidence for accumulation of a stable complex. Archives of Biochemistry and Biophysics 1987; 252: 451–457

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.