User menu

Reactions of bovine liver catalase with superoxide radicals and hydrogen peroxide.

Bibliographic reference Lardinois, O M. Reactions of bovine liver catalase with superoxide radicals and hydrogen peroxide.. In: Free radical research, Vol. 22, no. 3, p. 251-74 (1995)
Permanent URL http://hdl.handle.net/2078.1/11915
  1. del Río Luis A., Sandalio Luisa M., Palma JoséM., Bueno Pablo, Corpas Francisco J., Metabolism of oxygen radicals in peroxisomes and cellular implications, 10.1016/0891-5849(92)90150-f
  2. Tolbert N. E., Microbodies: peroxisomes and glyoxysomes, 10.1083/jcb.91.3.271s
  3. Goldberg Iris, Hochman Ayala, Three different types of catalases in Klebsiella pneumoniae, 10.1016/0003-9861(89)90572-9
  4. Nadler Varda, Goldberg Iris, Hochman Ayala, Comparative study of bacterial catalases, 10.1016/0304-4165(86)90160-1
  5. Hochman A., The Journal of Biological Chemistry, 262, 6871 (1987)
  6. Deisseroth A, Physiological Reviews, 50, 319 (1970)
  7. Schonbaum G. R., The enzymes, 13, 363 (1976)
  8. Esaka M., Plant & Cell Physiology, 23, 315 (1982)
  9. Vainshtein B. K., Melik-Adamyan W. R., Barynin V. V., Vagin A. A., Grebenko A. I., Three-dimensional structure of the enzyme catalase, 10.1038/293411a0
  10. 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 catalase fromMicrococcus lysodeikticusat 1.5 Å resolution, 10.1016/0014-5793(92)80919-8
  11. Clayton Roderick K., Purified catalase from Rhodopseudomonas spheroides, 10.1016/0006-3002(59)90067-8
  12. Tanford Charles., Lovrien Rex., Dissociation of Catalase into Subunits, 10.1021/ja00869a025
  13. Sund H., Weber K., Molbert E., Dissoziation der Rinderleber-Katalase in ihre Untereinheiten, 10.1111/j.1432-1033.1967.tb00088.x
  14. Schroeder W.A., Shelton J.Roger, Shelton Joan Balog, Robberson Barbara, Apell Gerald, The amino acid sequence of bovine liver catalase: A preliminary report, 10.1016/0003-9861(69)90441-x
  15. Maeda Yutaka, Trautwein Alfred, Gonser Ulrich, Yoshida Koichi, Kikuchi-Torii Kyoko, Homma Takeshi, Ogura Yasuyuki, Mössbauer effect in bacterial catalase, 10.1016/0005-2795(73)90351-6
  16. Fita Ignacio, Rossmann Michael G., The active center of catalase, 10.1016/0022-2836(85)90180-9
  17. Sharma K. D., The Journal of Biological Chemistry, 264, 12772 (1989)
  18. Melik-Adamyan William R., Barynin Vladimir V., Vagin Alexey A., Borisov Vsevolod V., Vainshtein Boris K., Fita Ignacio, Murthy Mathur R.N., Rossmann Michael G., Comparison of beef liver and Penicillium vitale catalases, 10.1016/0022-2836(86)90480-8
  19. Reid T. J., Murthy M. R., Sicignano A., Tanaka N., Musick W. D., Rossmann M. G., Structure and heme environment of beef liver catalase at 2.5 A resolution., 10.1073/pnas.78.8.4767
  20. Murthy Mathur R.N., Reid Thomas J., Sicignano Andrew, Tanaka Nobuo, Rossmann Michael G., Structure of beef liver catalase, 10.1016/0022-2836(81)90254-0
  21. Davison A. J., The Journal of Biological Chemistry, 261, 1193 (1986)
  22. Chance B, The Journal of Biological Chemistry, 194, 471 (1952)
  23. Margoliash E., Novogrodsky A., Schejter A., Irreversible reaction of 3-amino-1:2:4-triazole and related inhibitors with the protein of catalase, 10.1042/bj0740339
  24. Jacob Gary S., Orme-Johnson W. H., Catalase of Neurospora crassa. 1. Induction, purification, and physical properties, 10.1021/bi00581a009
  25. Kono Y., The Journal of Biological Chemistry, 258, 6015 (1983)
  26. Clairborne A., The Journal of Biological Chemistry, 254, 11664 (1979)
  27. Poole R. K., Journal of General Microbiology, 132, 1525 (1986)
  28. Johnston M. A., Journal of Bacteriology, 90, 352 (1965)
  29. Clairborne A., The Journal of Biological Chemistry, 254, 4245 (1979)
  30. Chance B., Physiological Reviews, 59, 527 (1979)
  31. Chuang W. J., The Journal of Biological Chemistry, 267, 13293 (1992)
  32. Keilin D., Hartree E. F., Properties of catalase. Catalysis of coupled oxidation of alcohols, 10.1042/bj0390293
  33. Keilin D., Hartree E. F., Catalase, peroxidase and metmyoglobin as catalysts of coupled peroxidatic reactions, 10.1042/bj0600310
  34. Chance B., The reactions of catalase in the presence of the notatin system, 10.1042/bj0460387
  35. Chuang W. J., The Journal of Biological Chemistry, 264, 14209 (1989)
  36. Oshino Nozomu, Chance Britton, Sies Helmut, The properties of the secondary catalase—peroxide complex (Compound II) in the hemoglobin-free perfused rat liver, 10.1016/0003-9861(73)90510-9
  37. Keilin D., Nichols P., Reactions of catalase with hydrogen peroxide and hydrogen donors, 10.1016/0006-3002(58)90189-6
  38. 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
  39. Shimizu N., The Journal of Biochemistry, 104, 136 (1988)
  40. 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, 10.1080/09553009214552461
  41. Keilin D., Hartree E. F., Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobin, 10.1042/bj0490088
  42. Chance Britton, The spectra of the enzyme-substrate complexes of catalase and peroxidase, 10.1016/0003-9861(52)90469-4
  43. Shimizu N., The Journal of Biological Chemistry, 259, 4414 (1984)
  44. 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
  45. Dhaunsi G. S., The Journal of Biological Chemistry, 267, 6870 (1992)
  46. del Río Luis A., Lyon Diana S., Olah Imre, Glick Bruce, Salin Marvin L., Immunocytochemical evidence for a peroxisomal localization of manganese superoxide dismutase in leaf protoplasts from a higher plant, 10.1007/bf01075257
  47. Kono Y., The Journal of Biological Chemistry, 257, 5751 (1982)
  48. Samejima N., The Journal of Biological Chemistry, 238, 3256 (1963)
  49. 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
  50. Lardinois Olivier M., Rouxhet Paul G., Characterization of Hydrogen Peroxide and Superoxide Degrading Pathways ofAspergillus NigerCatalase: A Steady-State Analysis, 10.3109/10715769409145624
  51. McCord J. M., The Journal of Biological Chemistry, 244, 6049 (1969)
  52. Metodiewa Diana, Brian Dunford H., 3-aminotriazole is a substrate for lactoperoxidase but not for catalase, 10.1016/s0006-291x(05)81105-2
  53. Wariishi H., The Journal of Biological Chemistry, 265, 2070 (1990)
  54. Rotilio G, Falcioni G, Fioretti E, Brunoir M, Decay of oxyperoxidase and oxygen radicals; a possible role for myeloperoxidase, 10.1042/bj1450405
  55. Dunford H, On the function and mechanism of action of peroxidases, 10.1016/s0010-8545(00)80316-1
  56. KOHLER H, JENZER H, Interaction of lactoperoxidase with hydrogen peroxideFormation of enzyme intermediates and generation of free radicals, 10.1016/0891-5849(89)90059-2
  57. HUWILER Martin, JENZER Herbert, KOHLER Heinz, The role of compound III in reversible and irreversible inactivation of lactoperoxidase, 10.1111/j.1432-1033.1986.tb09798.x
  58. Nicholls P., The enzymes, 8, 147 (1963)
  59. Kirkman H. N., The Journal of Biological Chemistry, 262, 660 (1987)
  60. Jenzer H., The Journal of Biological Chemistry, 261, 15550 (1986)
  61. Cai Danying, Tien Ming, On the reactions of lignin peroxidase Compound III (isozyme H8), 10.1016/0006-291x(89)92020-2
  62. Jenzer Herbert, Kohler Heinz, Broger Clemens, The role of hydroxyl radicals in irreversible inactivation of lactoperoxidase by excess H2O2, 10.1016/0003-9861(87)90359-6
  63. Brill A. S, Comprehensive Biochemistry, 14, 447 (1966)