Reactions of Bovine Liver Catalase with Superoxide Radicals and Hydrogen Peroxide

References

• del Rio L. A., Sandalio L. M., Palma J. M., Bueno P., Corpas F. J. Metabolism of oxygen radicals in peroxisomes and cellular implications. Free Radical Biology & Medicine 1992; 13: 557–580
   PubMed Web of Science ®Google Scholar
• Tolbert N. E., Essner E. Microbodies: peroxisomes and glyoxysomes. Journal of Cell Biology 1981; 91: 271s–283s
   PubMed Web of Science ®Google Scholar
• Goldberg I., Hochman A. Three different types of catalases in Klebsiella pneumoniae. Archives of Biochemistry and Biophysics 1989; 268: 124–128
   PubMed Web of Science ®Google Scholar
• Nadler V., Goldberg I., Hochman A. Comparative study of bacterial catalases. Biochimica el Biophysica Acta 1986; 882: 234–241
   Google Scholar
• Hochman A., Shemesh A. Purification and characterization of a catalase-peroxidase from the photosynthetic bacterium Rhodopseudomonas capsulata. The Journal of Biological Chemistry 1987; 262: 6871–6876
   PubMed Web of Science ®Google Scholar
• Deisseroth A, Dounce A. L. Catalase: physical and chemical properties, mechanism of catalysis, and physiological role. Physiological Reviews 1970; 50: 319–375
   PubMed Web of Science ®Google Scholar
• Schonbaum G. R., Chance B. Catalase. The enzymes, P. D. Boyer. Academic Press, New York 1976; Vol. 13: 363–408
   Google Scholar
• Esaka M., Asahi T. Purification and properties of catalase from sweet potato root microbodies. Plant & Cell Physiology 1982; 23: 315–322
   Google Scholar
• Vainshtein B. K., Melik-Adamyan W. R., Barynin V. V., Vagin A. A., Grebenko A. I. Three-dimensional structure of the enzyme catalase. Nature 1981; 293: 411–412
   PubMed Web of Science ®Google Scholar
• Murshudov G. N., Melik-Adamyan W. R., Grebenko A. I., Barynin V. V., Vagin A. A., Vainshtein B. K., Dauter Z., Wilson K. S. Three-dimensional structure of the catalase from Micrococcus lysodeikticus at 1.5 A resolution. FEBS Letters 1992; 312: 127–131
   PubMed Web of Science ®Google Scholar
• Clayton R. K. Purified catalase from Rhodopseudomonas spheroides. Biochimica et Biophysica Acta 1959; 36: 40–47
   PubMedGoogle Scholar
• Tanford C., Lovrien R. Dissociation of catalase into subunits. Journal of the American Chemical Society 1962; 84: 1892–1896
   Google Scholar
• Sund H., Weber K., Molbert E. Dissoziation der rinderleber-katalase in ihre untereinheiten. European Journal of Biochemistry 1967; 1: 400–410
   PubMedGoogle Scholar
• Schroeder W. A., Shelton J. R., Shelton J. B., Robberson B., Appell G. The amino acid sequence of bovine liver catalase: a preliminary report. Archives of Biochemistry and Biophysics 1969; 131: 653–655
   PubMedGoogle Scholar
• Maeda Y., Trautwein A., Gonser U., Yoshida K., Kikuchi-Torii K., Homma T., Ogura Y. Mossbauer effect in bacterial catalase. Biochimica et Biophysica Acta 1973; 303: 230–236
   PubMedGoogle Scholar
• Fita I., Rossmann M. G. The active-center of catalase. Journal of Molecular Biology 1985; 185: 21–37
   PubMed Web of Science ®Google Scholar
• Sharma K. D., Anderson L. A., Loehr T. M., Terner J., Goff H. M. Comparative spectral analysis of mammalian, fungal, and bacterial catalases. Resonance Raman evidence for iron-tyrosinate coordination. The Journal of Biological Chemistry 1989; 264: 12772–12779
   PubMed Web of Science ®Google Scholar
• Melik-Adamyan W. R., Barynin V. V., Vagin A. A., Borisov V. V., Vainshtein B. K., Fita I., Murthy M. R.N., Rossmann M. G. Comparison of beef liver and Penicillium vitale catalases. Journal of Molecular Biology 1986; 188: 63–72
   PubMed Web of Science ®Google Scholar
• Reid T. J., Murthy M. R.N., Sicignano A., Tanaka N., Musick W. D.L., Rossmann M. G. Structure and heme environment of beef liver catalase at 2.5 A resolution. Proceedings of the National Academy of Sciences of the United States of America 1981; 78: 4767–4771
   PubMed Web of Science ®Google Scholar
• Murthy M. R.N., Reid T. J., Sicignano A., Tanaka N., Rossmann M. G. Structure of beef liver catalase. Journal of Molecular Biology 1981; 152: 465–499
   PubMed Web of Science ®Google Scholar
• Davison A. J., Kettle A. J., Fatur D. J. Mechanism of the inhibition of catalase by ascorbate. Roles of active oxygen species, copper and semidehydroascorbate. The Journal of Biological Chemistry 1986; 261: 1193–1200
   PubMedGoogle Scholar
• Chance B. Effect of pH upon the reaction kinetics of the enzyme-substrate Compounds of catalase. The Journal of Biological Chemistry 1952; 194: 471–481
   PubMed Web of Science ®Google Scholar
• Margoliash E., Novogrodsky A., Schejter A. Irreversible reaction of 3-Amino-1:2:4-triazole and related inhibitors with the protein of catalase. Biochemical Journal 1960; 74: 339–350
   PubMed Web of Science ®Google Scholar
• Jacob G. S., Orme-Johnson W. H. Catalase of Neurospora crassa. 1. Induction, purification, and physical properties. Biochemistry 1979; 18: 2967–2975
   PubMedGoogle Scholar
• Kono Y., Fridovich I. Isolation and characterization of the pseudocatalase of Lactobacillus plantarium. A new manganese-containing enzyme. The Journal of Biological Chemistry 1983; 258: 6015–6019
   PubMed Web of Science ®Google Scholar
• Clairborne A., Malinowski D. P., Fridovich I. Purification and characterization of hydroperoxidase II of Escherichia coli B. The Journal of Biological Chemistry 1979; 254: 11664–11667
   PubMedGoogle Scholar
• Poole R. K., Baines B. S., Appleby C. A. Haemoprotein b-590 (Escherichia coli), a reductive catalase and peroxidase: evidence for its close relationship to hydroperoxidase I and a “Cytochrome alb” preparation. Journal of General Microbiology 1986; 132: 1525–1539
   PubMedGoogle Scholar
• Johnston M. A., Delwiche E. A. Isolation and characterization of the Cyanide-resistant and Azide-resistant catalase of Lactobacillus plantar urn. Journal of Bacteriology 1965; 90: 352–356
   PubMedGoogle Scholar
• Clairborne A., Fridovich I. Purification of the o-dianisidine peroxidase from Escherichia coli B. Physicochemical characterization and analysis of its dual catalatic and peroxidatic activities. The Journal of Biological Chemistry 1979; 254: 4245–4252
   PubMedGoogle Scholar
• Chance B., Sies H., Boveris A. Hydroperoxide metabolism in mammalian organs. Physiological Reviews 1979; 59: 527–605
   PubMed Web of Science ®Google Scholar
• Chuang W. J., Van Wart H. E. Resonance Raman spectra of horseradish peroxidase and bovine liver catalase Compound I species. Evidence for predominant 2A2u β-cation radical ground state configurations. The Journal of Biological Chemistry 1992; 267: 13293–13301
   PubMed Web of Science ®Google Scholar
• Keilin D., Hartree E. F. Properties of catalase. Catalysis of coupled oxidation of alcohols. Biochemical Journal 1945; 39: 293–301
   Web of Science ®Google Scholar
• Keilin D., Hartree E. F. Catalase, peroxidase and metmyoglobin as catalysts of coupled peroxidatic reactions. Biochemical Journal 1955; 60: 310–325
   PubMed Web of Science ®Google Scholar
• Chance B. The reactions of catalase in the presence of the notatin system. Biochemical Journal 1950; 46: 387–402
   PubMed Web of Science ®Google Scholar
• 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. The Journal of Biological Chemistry 1989; 264: 14209–14215
   PubMed Web of Science ®Google Scholar
• Oshino N., Chance B., Sies H. The properties of the secondary catalase-peroxide complex (Compound II) in the hemoglobin-free perfused rat liver. Archives of Biochemistry and Biophysics 1973; 159: 704–711
   Web of Science ®Google Scholar
• Keilin D., Nicholls P. Reactions of catalase with hydrogen peroxide and hydrogen donors. Biochimica et Biophysica Acta 1958; 29: 302–307
   PubMed Web of Science ®Google Scholar
• Chance B., Powers L., Ching Y., Poulos T., Schonbaum G. R., Yamazaki I., Paul K. G. X-Ray absorption studies of intermediates in peroxidase activity. Archives of Biochemistry and Biophysics 1984; 235: 596–611
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Metodiewa D., Dunford H. B. Spectral studies of intermediate species formed in one-electron reactions of bovine liver catalase at room and low temperatures. A comparison with peroxidase reactions. International Journal of Radiation Biology 1992; 62: 543–553
   PubMed Web of Science ®Google Scholar
• Keilin D., Hartree E. F. Purification of horse-radish peroxidase and comparison of its properties with those of catalase and met haemoglobin. Biochemical Journal 1951; 49: 88–104
   PubMed Web of Science ®Google Scholar
• Chance B. The spectra of the enzyme-substrate complexes of catalase and peroxidase. Archives of Biochemistry and Biophysics 1952; 41: 404–415
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Dhaunsi G. S., Gulati S., Singh A. K., Orak J. K., Asayama K., Singh I. Demonstration of Cu-Zn superoxide dismutase in rat liver peroxisomes. Biochemical and immunochemical evidence. The Journal of Biological Chemistry 1992; 267: 6870–6873
   PubMed Web of Science ®Google Scholar
• del Rio L. A., Lyon D. S., Olah I., Glick B., Marvin L. S. Immunocytochemical evidence for a peroxisomal localization of manganese superoxide dismutase in leaf protoplasts from a higher plant. Planta 1983; 158: 216–224
   PubMed Web of Science ®Google Scholar
• Kono Y., Fridovich I. Superoxide radical inhibits catalase. The Journal of Biological Chemistry 1982; 257: 5751–5754
   PubMed Web of Science ®Google Scholar
• Samejima N., Yang J. Reconstitution of acid-denatured catalase. The Journal of Biological Chemistry 1963; 238: 3256–3261
   PubMed Web of Science ®Google Scholar
• del Rio L. A., Gomez Ortega M., Leal Lopez A., Lopez Gorge J. A more sensitive modification of the catalase assay with the Clark oxygen electrode. Analytical Biochemistry 1977; 80: 409–415
   PubMed Web of Science ®Google Scholar
• Lardinois O. M., Rouxhet P. G. Characterization of hydrogen peroxide and superoxide degrading pathways of Aspergillus niger catalase: a steady-state analysis. Free Radical Research 1994; 20: 29–50
   PubMed Web of Science ®Google Scholar
• McCord J. M., Fridovich I. Superoxide dismutase. An enzymatic function for erythrocuprein (hemocuprein). The Journal of Biological Chemistry 1969; 244: 6049–6055
   PubMed Web of Science ®Google Scholar
• Metodiewa D., Dunford H. B. 3-Aminotriazole is a substrate for lactoperoxidase but not for catalase. Biochemical and Biophysical Research Communications 1991; 180: 585–590
   PubMed Web of Science ®Google Scholar
• Wariishi H., Gold M. H. Lignin peroxidase Compound III. Mechanism of formation and decomposition. The Journal of Biological Chemistry 1990; 265: 2070–2077
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Dunford H. B., Stillman J. S. On the function and mechanism of action of peroxidases. Coordination Chemisrtry Reviews 1976; 19: 187–251
   Web of Science ®Google Scholar
• Kohler H., Jenzer H. Interaction of lactoperoxidase with hydrogen peroxide. Formation of enzyme intermediates and generation of free radicals. Free Radical Biology and Medicine 1989; 6: 323–339
   PubMed Web of Science ®Google Scholar
• Huwiler M., Jenzer H., Kohler H. The role of Compound III in reversible and irreversible inactivation of lactoperoxidase. European Journal of Biochemistry 1986; 158: 609–614
   PubMedGoogle Scholar
• Nicholls P., Schonbaum G. R. Catalases. The enzymes, P. D. Boyer, L. Lardy, K. Myrback. Academic Press, Orlando, FL 1963; Vol.8: 147–225
   Google Scholar
• Kirkman H. N., Galiano S., Gaetani G. F. The function of catalase-bound NADPH. The Journal of Biological Chemistry 1987; 262: 660–666
   PubMed Web of Science ®Google Scholar
• Jenzer H., Jones W., Kohler H. On the molecular mechanism of lactoperoxidase-catalyzed H2O2 metabolism and irreversible enzyme inactivation. The Journal of Biological Chemistry 1986; 261: 15550–15556
   PubMedGoogle Scholar
• Cai D., Tien M. On the reactions of lignin peroxidase Compound III (Isozyme H8). Biochemical and Biophysical Research Communications 1989; 162: 464–469
   PubMedGoogle Scholar
• Jenzer H., Kohler H., Broger C. The role of hydroxyl radicals in irreversible inactivation of lactoperoxidase by excess H2O2. A spin-trapping/ESR and absorption spectroscopy study. Archives of Biochemistry and Biophysics 1987; 258: 381–390
   PubMedGoogle Scholar
• Brill A. S. Peroxidases and Catalase. Comprehensive Biochemistry, M. Florkin, E. H. Stotz. Elsevier Publishing Company, Amsterdam. London, New York 1966; Vol. 14: 447–479
   Google Scholar