User menu

Characterization of hydrogen peroxide and superoxide degrading pathways of Aspergillus niger catalase: a steady-state analysis.

Bibliographic reference Lardinois, O M ; Rouxhet, Paul. Characterization of hydrogen peroxide and superoxide degrading pathways of Aspergillus niger catalase: a steady-state analysis.. In: Free radical research, Vol. 20, no. 1, p. 29-50 (1994)
Permanent URL http://hdl.handle.net/2078.1/11975
  1. Halliwell Barry, Reactive oxygen species in living systems: Source, biochemistry, and role in human disease, 10.1016/0002-9343(91)90279-7
  2. Halliwell B, Gutteridge J M C, Oxygen toxicity, oxygen radicals, transition metals and disease, 10.1042/bj2190001
  3. McCord J. M., Journal of Biological Chemistry, 244, 6049 (1969)
  4. Nicholls P., The enzymes, 8, 147 (1963)
  5. Dunford H, On the function and mechanism of action of peroxidases, 10.1016/s0010-8545(00)80316-1
  6. Deisseroth A., Physiological Reviews, 50, 319 (1970)
  7. 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, 10.1016/0003-9861(84)90234-0
  8. Dunford H. B, Peroxidases in Chemistry and Biology, 1 (1991)
  9. Chuang W. J., Journal of Biological Chemistry, 267, 13293 (1992)
  10. Erman James E., Vitello Lidia B., Mauro J. Matthew, Kraut Joseph, Detection of an oxyferryl porphyrin .pi.-cation-radical intermediate in the reaction between hydrogen peroxide and a mutant yeast cytochrome c peroxidase. Evidence for tryptophan-191 involvement in the radical site of compound I, 10.1021/bi00446a004
  11. Chuang W. J., Journal of Biological Chemistry, 264, 14209 (1989)
  12. Bielski B.H.J., Cabelli D.E., Highlights of Current Research Involving Superoxide and Perhydroxyl Radicals in Aqueous Solutions, 10.1080/09553009114550301
  13. Gębicka Lidia, Metodiewa Diana, Gębicki Jerzy L., Pulse Radiolysis of Catalase in Solution. I. Reactions of O−2with Catalase and Its Compound I, 10.1080/09553008914550051
  14. Shimizu N., The Journal of Biological Chemistry, 259, 4414 (1984)
  15. Bielski B. H., Biochimica et Biophysica Acta, 364, 233 (1974)
  16. Bielski Benon H.J., Comstock David A., Haber Arthur, Chan Phillip C., Study of peroxidase mechanisms by pulse radiolysis. II. Reaction of horseradish peroxidase Compound I with O2−, 10.1016/0005-2744(74)90208-3
  17. Rest Richard F., Spitznagel John K., Subcellular distribution of superoxide dismutases in human neutrophils. Influence of myeloperoxidase on the measurement of superoxide dismutase activity, 10.1042/bj1660145
  18. Cuperus Roelck A., Muijsers Anton O., Wever Ron, The superoxide dismutase activity of myeloperoxidase; formation of Compound III, 10.1016/0167-4838(86)90135-4
  19. Heinecke J. W., The Journal of Biological Chemistry, 265, 9241 (1990)
  20. Metodiewa Diana, Pickard Michael, Dunford H.Brian, The reactions of chloroperoxidase in the presence of xanthine/xanthine oxidase, 10.1016/0006-291x(89)92220-1
  21. Kono Y., The Journal of Biological Chemistry, 257, 5751 (1982)
  22. KIKUCHI-TORII Kyoko, HAYASHI Sueko, NAKAMOTO Hideko, NAKAMURA Satoshi, Properties of Aspergillus niger Catalase, 10.1093/oxfordjournals.jbchem.a134069
  23. del Río Luís A., Ortega M.Gómez, López A.Leal, Gorgé J.López, A more sensitive modification of the catalase assay with the Clark oxygen electrode, 10.1016/0003-2697(77)90662-5
  24. Scott D., Enzymologia, 22, 229 (1960)
  25. Kikuchi Kyoko, Kawamura-Konishi Yasuko, Suzuki Haruo, The reaction of Aspergillus niger catalase with methyl hydroperoxide, 10.1016/0003-9861(92)90548-b
  26. Chance B., The reactions of catalase in the presence of the notatin system, 10.1042/bj0460387
  27. Chance Britton, The spectra of the enzyme-substrate complexes of catalase and peroxidase, 10.1016/0003-9861(52)90469-4
  28. Gruft H., Ruck R., Traynor J., Properties of a unique catalase isolated fromAspergillus niger, 10.1139/o78-141
  29. Sharma K. D., The Journal of Biological Chemistry, 264, 12772 (1989)
  30. Vasudevan P. T., Weiland R. H., Deactivation of catalase by hydrogen peroxide, 10.1002/bit.260360805
  31. Chance B., Biochemical Journal, 46, 402 (1950)
  32. Wariishi H., The Journal of Biological Chemistry, 265, 2070 (1990)
  33. Rotilio G., Biochemical Journal, 145, 405 (1975)
  34. Chance B., Physiological Reviews, 59, 527 (1979)
  35. Chance Britton, Rosted Carl Olof, Sillén Lars Gunnar, Linnasalmi Annikki, Laukkanen Pentti, An Intermediate Compound in the Catalase-hydrogen peroxide Reaction., 10.3891/acta.chem.scand.01-0236
  36. Chance Britton, Greenstein D.S., Roughton F.J.W., The mechanism of catalase action. I. Steady-state analysis, 10.1016/0003-9861(52)90194-x
  37. Kirkman H. N., The Journal of Biological Chemistry, 262, 660 (1987)
  38. Shimizu Norihide, Kobayashi Kazuo, Hayashi Koichiro, Studies on the Equilibria and Kinetics of the Reactions of Ferrous Catalase with Ligands, 10.1093/oxfordjournals.jbchem.a122409
  39. Keilin D., Biochimica et Biophysica Acta, 29, 302 (1958)
  40. Sawada Y., Biochimica et Biophysica Acta, 327, 257 (1973)
  41. Mylrajan Muthusamy, Valli Khadar, Wariishi Hiroyuki, Gold Michael H., Loehr Thomas M., Resonance Raman spectroscopic characterization of compound III of lignin peroxidase, 10.1021/bi00493a016
  42. Kobayashi K., Superoxide and Superoxide Dismutase in Chemistry, Biology and Medicine, 228 (1986)
  43. Cai D., The Journal of Biological Chemistry, 267, 11149 (1992)
  44. Jenzer Herbert, Kohler Heinz, The role of superoxide radicals in lactoperoxidase-catalysed H2O2 — metabolism and in irreversible enzyme inactivation, 10.1016/s0006-291x(86)80117-6
  45. Mal Asoke, Nandi Anuradha, Chatterjee I B, Haemoglobin: A scavenger of superoxide radical, 10.1007/bf02720050
  46. Sutton H. C., Biochemical Journal, 155, 503 (1976)
  47. Nakajima R., The Journal of Biological Chemistry, 262, 2576 (1987)
  48. Keilin D., Nichols P., Reactions of catalase with hydrogen peroxide and hydrogen donors, 10.1016/0006-3002(58)90189-6