TSRI's main web site PROMISE mirror at TSRI Metalloprotein DB site Created: 12 November 1996
Last modified: 31 March 1999

Bibliography on structural studies of catalases

  1. Adrian, M., Dubochet, J., Fuller, S.D. and Harris, J.R. (1998) Cryo­negative staining. Micron 29, 145-160.
  2. Akey, C.W. and Edelstein, S.J. (1983) Equivalence of the projected structure of thin catalase crystals preserved for electron microscopy by negative stain, glucose or embedding in the presence of tannic acid. J. Mol. Biol. 163, 575-612.
  3. Akey, C.W., Szalay, M. and Edelstein, S.J. (1984) Trigonal catalase crystals: A new molecular packing assignment obtained from sections preserved with tannic acid. Ultramicroscopy 13, 103-111.
  4. Aoyama, K., Ogawa, K., Kimura, Y. and Fujiyoshi, Y. (1995) A method for 2D crystallization of soluble proteins at liquid-liquid interface. Ultramicroscopy 57, 345-354.
  5. Benecky, M.J., Frew, J.E., Scowen, N., Jones, P. and Hoffman, B.M. (1993) EPR and ENDOR detection of compound I from Micrococcus lysodeikticus catalase. Biochemistry 32, 11929-11933.
  6. Berthet, S., Nykyri, L.M., Bravo, J., Mate, M.J., Berthet­Colominas, C., Alzari, P.M., Koller, F. and Fita, I. (1997) Crystallization and preliminary structural analysis of catalase A from Saccharomyces cerevisiae. Protein Science 6, 481-483.
  7. Bravo, J., Verdaguer, N., Tormo, J., Betzel, C., Switala, J., Loewen, P.C. and Fita, I. (1995) Crystal structure of catalase HPII from Escherichia coli. Structure 3, 491-502.
  8. Bravo, J., Fita, I., Ferrer, J.C., Ens, W., Hillar, A., Switala, J. and Loewen, P.C. (1997) Identification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli. Protein Science 6, 1016-1023.
  9. Bravo, J., Mate, M.J., Schneider, T., Switala, J., Wilson, K., Loewen, P.C. and Fita, I. (1999) Structure of catalase HPII from Escherichia coli at 1.9 Å resolution. Proteins 34, 155-166.
  10. Browett, W.R. and Stillman, M.J. (1979) Magnetic circular dichroism studies of bovine liver catalase. Biochim. Biophys. Acta 577, 291-306.
  11. Browett, W.R. and Stillman, M.J. (1980) Magnetic circular dichroism studies on the electronic configuration of catalase compounds I and II. Biochim. Biophys. Acta 623, 21-31.
  12. Browett, W.R. and Stillman, M.J. (1981) Evidence for heme pi cation radical species in compound I of horseradish peroxidase and catalase. Biochim. Biophys. Acta 660, 1-7.
  13. Chuang, W.J. and van Wart, H.E. (1992) Resonance Raman spectra of horseradish peroxidase and bovine liver catalase compound I species. Evidence for predominant 2A2u pi­cation radical ground state configurations. J. Biol. Chem. 267, 13293-13301.
  14. Chuang, W.J., Heldt, J. and van Wart, H.E. (1989) Resonance Raman spectra of bovine liver catalase compound II. Similarity of the heme environment to horseradish peroxidase compound II. J. Biol. Chem. 264, 14209-14215.
  15. Craven, P.A., DeRubertis, F.R. and Pratt, D.W. (1979) Electron spin resonance study of the role of NO·catalase in the activation of guanylate cyclase by NaN3 and NH2OH. Modulation of enzyme responses by heme proteins and their nitrosyl derivatives. J. Biol. Chem. 254, 8213-8222.
  16. Dawson, J.H., Bracete, A.M., Huff, A.M., Kadkhodayan, S., Zeitler, C.M., Sono, M., Chang, C.K. and Loewen, P.C. (1991) The active site structure of E. coli HPII catalase. Evidence favoring coordination of a tyrosinate proximal ligand to the chlorin iron. FEBS Lett. 295, 123-126.
  17. Dickinson, L.C., Chien, J.C., Marie, A.L. and Parak, F. (1982) Electron paramagnetic resonance crystallography of bacterial catalase: g­Contour mapping method of analysis. Proc. Natl. Acad. Sci. USA 79, 7278-7282.
  18. Eglinton, D.G., Gadsby, P.M., Sievers, G., Peterson, J. and Thomson, A.J. (1983) A comparative study of the low­temperature magnetic circular dichroism spectra of horse heart metmyoglobin and bovine liver catalase derivatives. Biochim. Biophys. Acta 742, 648-658.
  19. Eventoff, W. and Gurskaya, G.U. (1975) The molecular symmetry of bovine liver catalase. J. Mol. Biol. 93, 55-62.
  20. Eventoff, W., Tanaka, N. and Rossmann, M.G. (1976) Crystalline bovine liver catalase. J. Mol. Biol. 103, 799-801.
  21. Fita, I. and Rossmann, M.G. (1985a) The NADPH binding site on beef liver catalase. Proc. Natl. Acad. Sci. USA 82, 1604-1608.
  22. Fita, I. and Rossmann, M.G. (1985b) The active center of catalase. J. Mol. Biol. 185, 21-37.
  23. Fita, I., Silva, A.M., Murthy, M.R.N. and Rossmann, M.G. (1986) The refined structure of beef liver catalase at 2.5 Å resolution. Acta Crystallogr. B42, 497-515.
  24. Gouet, P., Jouve, H.­M. and Dideberg, O. (1995) Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH. J. Mol. Biol. 249, 933-954.
  25. Gouet, P., Jouve, H.­M., Williams, P.A., Andersson, I., Andreoletti, P., Nussaume, L. and Hajdu, J. (1996) Ferryl intermediates of catalase captured by time­resolved Weissenberg crystallography and UV­VIS spectroscopy. Nature Struct. Biol. 3, 951-956.
  26. Harris, J.R. and Holzenburg, A. (1995) Human erythrocyte catalase: 2­D crystal nucleation and production of multiple crystal forms. J. Struct. Biol. 115, 102-112.
  27. Harris, J.R., Engelhardt, H., Volker, S. and Holzenburg, A. (1993) Electron microscopy of human erythrocyte catalase: new two­dimensional crystal forms. J. Struct. Biol. 111, 22-33.
  28. Hershberg, R.D. and Chance, B. (1975) Optical and magnetic resonance studies of formate binding to horse liver catalase and sperm whale myoglobin. Biochemistry 14, 3885-3891.
  29. Hu, S. and Kincaid, J.R. (1992) Resonance Raman studies of the carbonmonoxy form of catalase. Evidence for and effects of phenolate ligation. FEBS Lett. 314, 293-296.
  30. Ivancich, A., Jouve, H.M., Sartor, B. and Gaillard, J. (1997) EPR investigation of compound I in Proteus mirabilis and bovine liver catalases: Formation of porphyrin and tyrosyl radical intermediates. Biochemistry 36, 9356-9364.
  31. Jouve, H.­M., Gouet, P., Boudjada, N., Buisson, G., Kahn, R. and Duée, E. (1991) Crystallization and crystal packing of Proteus mirabilis PR catalase. J. Mol. Biol. 221, 1075-1077.
  32. Kobayashi, C., Suga, Y., Yamamoto, K., Yomo, T., Ogasahara, K., Yutani, K. and Urabe, I. (1997) Thermal conversion from low­ to high­activity forms of catalase I from Bacillus stearothermophilus. J. Biol. Chem. 272, 23011-23016.
  33. Labaw, L.W. (1967) Ox liver catalase crystal structure by electron microscopy. J. Ultrastruct. Res. 17, 327-341.
  34. Lardinois, O.M., Mestdagh, M.M. and Rouxhet, P.G. (1996) Reversible inhibition and irreversible inactivation of catalase in presence of hydrogen peroxide. Biochim. Biophys. Acta 1295, 222-238.
  35. Longley, W. (1967) The crystal structure of bovine liver catalase: a combined study by x­ray diffraction and electron microscopy. J. Mol. Biol. 30, 323-327.
  36. Luftig, R.B. (1967) An accurate measurement of the catalase crystal period and its use as an internal marker for electron microscopy. J. Ultrastruct. Res. 20, 91-102.
  37. McPherson, A. and Rich, A. (1973) Crystallographic study of beef liver catalase. Arch. Biochem. Biophys. 157, 23-27.
  38. Maj, M., Loewen, P. and Nicholls, P. (1998) E. coli HPII catalase interaction with high spin ligands: formate and fluoride as active site probes. Biochim. Biophys. Acta 1384, 209-222.
  39. Matricardi, V.R., Moretz, R.C. and Parsons, D.F. (1972) Electron diffraction of wet proteins: catalase. Science 177, 268-270.
  40. Melik­Adamyan, W.R., Barynin, V.V., Vagin, A.A., Borisov, V.V., Vainshtein, B.K., Fita, I., Murthy, M.R.N. and Rossmann, M.G. (1986) Comparison of beef liver and Penicillium vitale catalases. J. Mol. Biol. 188, 63-72.
  41. Murshudov, G.N., Melik­Adamyan, W.R., Grebenko, A.I., Barynin, V.V., Vagin, A.A., Vainshtein, B.K., Dauter, Z. and Wilson, K.S. (1992) Three­dimensional structure of catalase from Micrococcus lysodeikticus at 1.5 Å resolution. FEBS Lett. 312, 127-131.
  42. Murthy, M.R.N., Reid, T.J., Sicignano, A., Tanaka, N. and Rossmann, M.G. (1981) Structure of beef liver catalase. J. Mol. Biol. 152, 465-499.
  43. Prajapati, S., Bhakuni, V., Babu, K.R. and Jain, S.K. (1998) Alkaline unfolding and salt­induced folding of bovine liver catalase at high pH. Eur. J. Biochem. 255, 178-184.
  44. Reid, T.J., Murthy, M.R.N., Sicignano, A., Tanaka, N., Musick, W.D.L. and Rossmann, M.G. (1981) Structure and heme environment of beef liver catalase at 2.5 Å resolution. Proc. Natl. Acad. Sci. USA 78, 4767-4771.
  45. Sato, A., Furuno, T., Toyoshima, C. and Sasabe, H. (1993) Two­dimensional crystallization of catalase on a monolayer film of poly(1­benzyl­L­histidine) spread at the air/water interface. Biochim. Biophys. Acta 1062, 54-60.
  46. Sevinc, M.S., Maté, M.J., Switala, J., Fita, I. and Loewen, P.C. (1999) Role of the lateral channel in catalase HPII of Escherichia coli. Protein Science 8, 490-498.
  47. Sharma, K.D., Andersson, L.A., Loehr, T.M., Terner, J. and Goff, H.M. (1989) Comparative spectral analysis of mammalian, fungal, and bacterial catalases. Resonance Raman evidence for iron-tyrosinate coordination. J. Biol. Chem. 264, 12772-12779.
  48. Switala, J., O'Neil, J.O. and Loewen, P.C. (1999) Catalase HPII from Escherichia coli exhibits enhanced resistance to denaturation. Biochemistry 38, 3895-3901.
  49. Tormo, J., Fita, I., Switala, J. and Loewen, P.C. (1990) Crystallization and preliminary X­ray diffraction analysis of catalase HPII from Escherichia coli. J. Mol. Biol. 213, 219-220.
  50. Unwin, P.N. (1975) Beef liver catalase structure: interpretation of electron micrographs. J. Mol. Biol. 98, 235-242.
  51. Vainshtein, B.K., Melik­Adamyan, W.R., Barynin, V.V., Vagin, A.A. and Grebenko, A.I. (1981) Three­dimensional structure of the enzyme catalase. Nature 293, 411-412.
  52. Vainshtein, B.K., Melik­Adamyan, W.R., Barynin, V.V., Vagin, A.A., Grebenko, A.I., Borisov, V.V., Bartels, K.S., Fita, I. and Rossmann, M.G. (1986) Three­dimensional structure of catalase from Penicillium vitale at 2.0 Å resolution. J. Mol. Biol. 188, 49-61.
  53. Zhang, J., Chi, Q., Zhang, B., Dong, S. and Wang, W. (1998) Molecular characterization of beef liver catalase by scanning tunneling microscopy. Electroanalysis 10, 738-746.
Reviews on catalases