28
Views
17
CrossRef citations to date
0
Altmetric
Original Article

Characterization of Hydrogen Peroxide and Superoxide Degrading Pathways of Aspergillus Niger Catalase: A Steady-State Analysis

&
Pages 29-50 | Received 02 Aug 1993, Published online: 07 Jul 2009

References

  • Halliwell B. Reactive oxygen species in living systems: source, biochemistry, and role in human disease. The American journal of Medicine. 1991; 91: 14S–22S
  • Halliwell B., Gutteridge J. M. G. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochemical Journal 1984; 219: 1–14
  • McCord J. M., Fridovich I. Superoxide dismutase. An enzymatic function for erythrocuprein (hemocuprein). Journal of Biological Chemistry 1969; 244: 6049–6055
  • Nicholls P., Schonbaum G. R. Catalases. The enzymes, P. D. Boyer, H. Lardy, K. Myrback. Academic Press, Orlando, FL. 1963; vol. 8: 147–225
  • Dunford H. B., Stillman J. S. On the function and mechanism of action of peroxidases. Coordination Chemistry Reviews 1976; 19: 187–251
  • Deisseroth A., Dounce A. L. Catalase: physical and chemical properties, mechanism of catalysis, and physiological role. Physiological Reviews 1970; 50: 319–375
  • Chance B., Powers L., Ching Y., Poulos T., Paul K. G. X-Ray absorption studies of intermediates in peroxidase activity. Archives of Biochemistry and Biophysics 1984; 235: 596–611
  • Dunford H. B. Horseradish peroxidase: structure and kinetic properties. Peroxidases in Chemistry and Biology, J. Everse, K. E. Everse, M. B. Grisham. CRC Press, Boca RatonUSA 1991; 1–24
  • Chuang W. J., Van Wart H. E. Resonance Raman spectra of horseradish peroxidase and bovine liver catalase Compound I species. Evidence for predominent 2A2u α-cation radical ground state configurations. Journal of Biological Chemistry 1992; 267: 13293–13301
  • Erman J. E., Vitello L. B., Mauro J. M., Kraut J. Detection of an oxyferryl porphyrin T-cation radical intermediate in the reaction between hydrogen peroxide and a mutant cytochrome c peroxidase. Evidence for Tryptophan-191 involvement in the radical site of Compound I. Biochemistry 1989; 28: 7992–7995
  • Chuang W. J., Heldt J., Wart E. W. Resonance Raman spectra of bovine liver catalase Compound II. Similarity of the heme environment to horseradish peroxidase Compound II. Journal of Biological Chemistry 1989; 264: 14209–14215
  • Bielski B. H., Cabelli D. E. Highlights of current research involving superoxide and perhydroxyl radicals in aqueous solutions. International Journal of Radiation Biology 1991; 59: 291–319
  • Gebicka L., Metodiewa D., Gebicki J. L. Pulse radiolysis of catalase in solution. I. Reactions of O2− with catalase and its Compound I. International Journal of Radiation Biology 1989; 55: 45–50
  • Shimizu N., Kobayashi K., Hayashi K. The reaction of superoxide radical with catalase. Mechanism of the inhibition of catalase by superoxide radical. The Journal of Biological Chemistry 1984; 259: 4414–4418
  • Bielski B. H., Gebicki J. M. Study of peroxidase mechanisms by pulse radiolysis III. The rate of reaction of O2− and HO2 radicals with horseradish peroxidase Compound I. Biochimica et Biophysica Acta 1974; 364: 233–235
  • Bielski B. H. J., Comstock D. A., Haber A., Chan P. C. Study of peroxidase mechanisms by pulse radiolysis. II. Reaction of horseradish peroxidase Compound I with O2−. Biochimica et Biophysica Acta 1974; 350: 113–120
  • Rest R. F., Spitznagel J. K. Subcellular distribution of superoxide dismutase in human neutrophils. Influence of myeloperoxidase on the measurement of superoxide dismutase activity. Biochemical Journal 1977; 166: 145–153
  • Cuperus R. A., Muijsers A. O., Wever R. The superoxide dismutase activity of myeloperoxidase; formation of Compound III. Biochimica et Biophysica Acta 1986; 871: 78–84
  • Heinecke J. W., Shapiro B. M. Superoxide peroxidase activity of ovoperoxidase, the cross-linking enzyme of fertilization. The Journal of Biological Chemistry 1990; 265: 9241–9246
  • Metodiewa D., Pickard M., Dunford H. B. The reactions of chloroperoxidase in the presence of xanthine/xanthine oxidase. Biochemical and Biophysical Research Communications 1989; 159: 1086–1092
  • Kono Y., Fridovich I. Superoxide radical inhibits catalase. The Journal of Biological Chemistry 1982; 257: 5751–5754
  • Kikuchi-Torii K., Hayashi S., Nakamoto H., Nakamura S. Properties of Aspergillus niger catalase. The Journal of Biochemistry 1982; 92: 1449–1456
  • Del Rio L. A., Ortega M. G., Lopez A. L., George J. L. A more sensitive modification of the catalase assay with the Clark oxygen electrode. Analytical Biochemistry 1977; 80: 409–415
  • Hammer F. E. (1960) Purification and characterization of catalase from Aspergillus niger. Proceedings of the Annual Meeting. 1960, I7C–18C, The American Chemical Society
  • Scott D., Hammer F. Properties of Aspergillus catalase. Enzymologia 1960; 22: 229–237
  • Kikuchi K., Kawamura-Konishi Y., Suzuki H. The reaction of Aspergillus niger catalase with methyl hydroperoxide. Archives of Biochemistry and Biophysics 1992; 296: 88–94
  • Chance B. The reactions of catalase in the presence of the notatin system. Biochemical Journal 1950; 46: 387–402
  • Chance B. The spectra of the enzyme-substrate complexes of catalase and peroxidase. Archives of Biochemistry and Biophysics 1952; 41: 404–415
  • Gruft H., Ruck R., Traynor J. Properties of a unique catalase isolate from. Aspergillus niger. Canadian Journal of Biochemistry 1978; 56: 916–919
  • Sharma K. D., Andersson L. A., Loehr T. M., Terner J., Goff H. M. Comparative spectral analysis of mammalian, fungal, and bacterial catalases. Resonance Raman evidence for irontyrosinate coordination. The Journal of Biological Chemistry 1989; 264: 12772–12779
  • Vasudevan P. T., Weiland R. H. Deactivation of catalase by hydrogen peroxide. Biotechnology and Bioengineering 1990; 36: 783–789
  • Chance B., Herbert D. The enzyme-substrate Compounds of bacterial catalase and peroxides. Biochemical Journal 1950; 46: 402–414
  • Wariishi H., Gold M. H. Lignin peroxidase Compound III. Mechanism of formation and decomposition. The Journal of Biological Chemistry 1990; 265: 2070–2077
  • Rotilio G., Falcioni G., Fioretti E., Brunori M. Decay of oxyperoxidase and oxygen radicals: a possible role for Myeloperoxidase. Biochemical Journal 1975; 145: 405–407
  • Chance B., Sies H., Boveris A. Hydroperoxide metabolism in mammalian organs. Physiological Reviews 1979; 59: 527–605
  • Chance B. An intermediate Compound in the catalase-hydrogen peroxide reaction. Acta Chemica Scandinavica 1947; 1: 236–267
  • Chance B., Greenstein D. S., Roughton F. J. W. The mechanism of catalase action. I. Steady-state analysis. Archives of Biochemistry and Biophysics 1952; 37: 301–321
  • Kirkman H. N., Galiano S., Gaetani G. F. The function of catalase-bound NADPH. The Journal of Biological Chemistry 1987; 262: 660–666
  • Shimizu N., Kobayashi K., Hayashi K. Studies on the equilibria and kinetics of the reactions of ferrous catalase with ligands. The Journal of Biochemistry 1988; 104: 136–140
  • Keilin D., Nicholls P. Reactions of catalase with hydrogen peroxide with hydrogen peroxide and hydrogen donors. Biochimica et Biophysica Acta 1958; 29: 302–307
  • Sawada Y., Yamazaki I. One-electron transfer reactions in biochemical systems. VIII. Kinetic study of superoxide dismutase. Biochimica et Biophysica Acta 1973; 327: 257–265
  • Mylrajan M., Valli K., Wariishi H., Gold M. H., Loehr T. M. Resonance Raman spectroscopic characterization of Compound III of lignin peroxidase. Biochemistry 1990; 29: 9617–9623
  • Kobayashi K., Shimizu N., Hayashi K. The reactions of superoxide radical with catalase. Superoxide and Superoxide Dismutase in Chemistry, Biology and Medicine, G. Rotilio. Elsevier Science Publishers B. V., Amsterdam 1986; 228–230
  • Cai D., Tien M. Kinetic studies on the formation and decomposition of Compounds II and III. The Journal of Biological Chemistry 1992; 267: 11149–11155
  • Jenzer H., Kohler H. The role of superoxide radicals in lactoperoxidase-catalysed H2O2-metabolism and in irreversible enzyme inactivation. Biochemical and Biophysical Research communications 1986; 139: 327–332
  • Mai A., Nandi A., Chatterjee I. B. Haemoglobin: a scavenger of superoxide radical. Journal of Biosciences 1991; 16: 43–53
  • Sutton H. C., Roberts P. B., Winterbourn C. C. The rate of reaction of superoxide radical ion with oxyhaemoglobin and methaemoglobin. Biochemical Journal 1976; 155: 503–510
  • Nakajima R., Yamazaki I. The mechanism of oxyperoxidase formation from ferryl peroxidase and hydrogen peroxide. The Journal of Biological Chemistry 1987; 262: 2576–2581
  • Keilin D., Nicholls P. Reactions of catalase with hydrogen peroxide and hydrogen donors. Biochimica et Biophysica Acta 1958; 29: 302–307

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.