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Bibliography on structural studies of Fe-superoxide dismutase

  1. Asada, K., Yoshikawa, K., Takahashi, M., Maeda, Y. and Enmanji, K. (1975) Superoxide dismutases from a blue­green alga, Plectonema boryanum. J. Biol. Chem. 250, 2801-2807.
  2. Barra, D., Schinina, M.E., Bossa, F., Puget, K., Durosay, P., Guissani, A. and Michelson, A.M. (1990) A tetrameric iron superoxide dismutase from the eucaryote Tetrahymena pyriformis. J. Biol. Chem. 265, 17680-17687.
  3. Beyer, W.F., Jr. and Fridovich, I. (1987) Effect of hydrogen peroxide on the iron­containing superoxide dismutase of Escherichia coli. Biochemistry 26, 1251-1257.
  4. Beyer, W.F., Jr. and Fridovich, I. (1991) In vivo competition between iron and manganese for occupancy of the active site region of the manganese-superoxide dismutase of Escherichia coli. J. Biol. Chem. 266, 303-308.
  5. Beyer, W.F., Jr., Reynolds, J.A. and Fridovich, I. (1989) Differences between the manganese­ and the iron­containing superoxide dismutases of Escherichia coli detected through sedimentation equilibrium, hydrodynamic, and spectroscopic studies. Biochemistry 28, 4403-4409.
  6. Bunting, K., Cooper, J.B., Badasso, M.O., Tickle, I.J., Newton, M., Wood, S.P., Zhang, Y. and Young, D. (1998) Engineering a change in metal­ion specificity of the iron­dependent superoxide dismutase from Mycobacterium tuberculosis - X­ray structure analysis of site­directed mutants. Eur. J. Biochem. 251, 795-803.
  7. Carlioz, A., Ludwig, M.L., Stallings, W.C., Fee, J.A., Steinman, H.M. and Touati, D. (1988) Iron superoxide dismutase. Nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structures. J. Biol. Chem. 263, 1555-1562.
  8. Cooper, J.B., McIntyre, K., Badasso, M.O., Wood, S.P., Zhang, Y., Garbe, T.R. and Young, D. (1995) X­ray structure analysis of the iron­dependent superoxide dismutase from Mycobacterium tuberculosis at 2.0 Å resolution reveals novel dimer-dimer interactions. J. Mol. Biol. 246, 531-544.
  9. Cooper, J.B., Saward, S., Erskine, P.T., Badasso, M.O., Wood, S.P., Zhang, Y. and Young, D. (1996) X­ray structure analysis of an engineered Fe-superoxide dismutase Gly->Ala mutant with significantly reduced stability to denaturant. FEBS Lett. 387, 105-108.
  10. Cseke, C., Horvath, L.L., Simon, P., Borbely, G., Keszthelyi, L. and Farkas, G.L. (1979) An iron­containing superoxide dismutase from Anacystis nidulans. J. Biochem. (Tokyo) 85, 1397-1404.
  11. Edwards, R.A., Whittaker, M.M., Whittaker, J.W., Jameson, G.B. and Baker, E.N. (1998) Distinct metal environment in Fe­substituted manganese superoxide dismutase provides a structural basis of metal specificity. J. Am. Chem. Soc. 120, 9684-9685.
  12. Gabbianelli, R., Battistoni, A., Capo, C., Polticelli, F., Rotilio, G., Meier, B. and Desideri, A. (1997a) Effect of Val73->Trp mutation on the reaction of "cambialistic" superoxide dismutase from Propionibacterium shermanii with hydrogen peroxide. Arch. Biochem. Biophys. 345, 156-159.
  13. Gabbianelli, R., Battistoni, A., Polticelli, F., Meier, B., Schmidt, M., Rotilio, G. and Desideri, A. (1997b) Effect of Lys175 mutation on structure function properties of Propionibacterium shermanii superoxide dismutase. Protein Engineering 10, 1067-1070. Computation
  14. Hunter, T., Ikebukuro, K., Bannister, W.H., Bannister, J.V. and Hunter, G.J. (1997) The conserved residue tyrosine 34 is essential for maximal activity of iron-superoxide dismutase from Escherichia coli. Biochemistry 36, 4925-4933.
  15. Jackson, S.M. and Cooper, J.B. (1998) An analysis of structural similarity in the iron and manganese superoxide dismutases based on known structures and sequences. Biometals 11, 159-173.
  16. Kardinahl, S., Schmidt, C.L., Petersen, A. and Schäfer, G. (1996) Isolation, characterization and crystallization of an iron-superoxide dismutase from the crenarchaeon Sulfolobus acidocaldarius. FEMS Microbiol. Lett. 138, 65-70.
  17. Knapp, S., Kardinahl, S., Hellgren, N., Tibbelin, G., Schäfer, G. and Ladenstein, L. (1999) Refined crystal structure of a superoxide dismutase from the hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2 Å resolution. J. Mol. Biol. 285, 689-702.
  18. Lah, M.S., Dixon, M.M., Pattridge, K.A., Stallings, W.C., Fee, J.A. and Ludwig, M.L. (1995) Structure-function in Escherichia coli iron superoxide dismutase: Comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry 34, 1646-1660.
  19. Lavelle, F., McAdam, M.E., Fielden, E.M. and Roberts, P.B. (1977) A pulse­radiolysis study of the catalytic mechanism of the iron­containing superoxide dismutase from Photobacterium leiognathi. Biochem. J. 161, 3-11.
  20. Lim, J.­H., Yu, Y.G., Han, Y.S., Cho, S., Ahn, B.­Y., Kim, S.­H. and Cho, Y. (1997) The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 Å resolution: Structural basis for thermostability. J. Mol. Biol. 270, 259-274.
  21. Lumsden, J. and Hall, D.O. (1974) Soluble and membrane­bound superoxide dismutases in a blue­green algae (Spirulina) and spinach. Biochem. Biophys. Res. Commun. 58, 35-41.
  22. Lumsden, J., Cammack, R. and Hall, D.O. (1976) Purification and physicochemical properties of superoxide dismutase from two photosynthetic microorganisms. Biochim. Biophys. Acta 438, 380-392.
  23. Meier, B. (1991) Comparative studies on a superoxide dismutase exhibiting enzymatic activity with iron and manganese as active cofactor. Free Radic. Res. Commun. 12-13, 211-214.
  24. Meier, B., Sehn, A.P., Schinina, M.E. and Barra, D. (1994a) In vivo incorporation of copper into the iron­exchangeable and manganese­exchangeable superoxide dismutase from Propionibacterium shermanii. Amino acid sequence and identity of the protein moieties. Eur. J. Biochem. 219, 463-468.
  25. Meier, B., Sehn, A.P., Sette, M., Paci, M., Desideri, A. and Rotilio, G. (1994b) In vivo incorporation of cobalt into Propionibacterium shermanii superoxide dismutase. FEBS Lett. 348, 283-286.
  26. Meier, B., Sehn, A.P., Michel, C. and Saran, M. (1994c) Reactions of hydrogen peroxide with superoxide dismutase from Propionibacterium shermanii - an enzyme which is equally active with iron or manganese - are independent of the prosthetic metal. Arch. Biochem. Biophys. 313, 296-303.
  27. Meier, B., Michel, C., Saran, M., Huttermann, J., Parak, F. and Rotilio, G. (1995) Kinetic and spectroscopic studies on a superoxide dismutase from Propionibacterium shermanii that is active with iron or manganese: pH­dependence. Biochem. J. 310, 945-950.
  28. Meier, B., Parak, F., Desideri, A. and Rotilio, G. (1997) Comparative stability studies on the iron and manganese forms of the cambialistic superoxide dismutase from Propionibacterium shermanii. FEBS Lett. 414, 122-124.
  29. Meier, B., Scherk, C., Schmidt, M. and Parak, F. (1998) pH­dependent inhibition by azide and fluoride of the iron superoxide dismutase from Propionibacterium shermanii. Biochem J. 331, 403-407.
  30. Misra, H.P. and Keele, B.B., Jr. (1975) The purification and properties of superoxide dismutase from a blue­green alga. Biochim. Biophys. Acta 379, 418-425.
  31. Pagani, S., Colnaghi, R., Palagi, A. and Negri, A. (1995) Purification and characterization of an iron superoxide dismutase from the nitrogen­fixing Azotobacter vinelandii. FEBS Lett. 357, 79-82.
  32. Pennington, C.D. and Gregory, E.M. (1986) Isolation and reconstitution of iron­ and manganese­containing superoxide dismutases from Bacteroides thetaiotaomicron. J. Bacteriol. 166, 528-532.
  33. Renault, J.P., Morgenstern­Badarau, I. and Piccioli, M. (1999) Thermochromic conformational change of Methanobacterium thermoautotrophicum iron superoxide dismutase. Inorg. Chem. 38, 614-615.
  34. Ringe, D., Petsko, G.A., Yamakura, F., Suzuki, K. and Ohmori, D. (1983a) Structure of iron superoxide dismutase from Pseudomonas ovalis at 2.9­Å resolution. Proc. Natl. Acad. Sci. USA 80, 3879-3883.
  35. Ringe, D., Petsko, G.A., Yamakura, F., Suzuki, K. and Ohmori, D. (1983b) The iron content of iron superoxide dismutase: determination by anomalous scattering. Proc. R. Soc. Lond. B218, 119-126.
  36. Scherk, C., Schmidt, M., Nolting, H.F., Meier, B. and Parak, F. (1996) EXAFS investigation of the active site of iron superoxide dismutase of Escherichia coli and Propionibacterium shermanii. Eur. Biophys. J. 24, 243-250.
  37. Schmidt, M., Meier, B. and Parak, F. (1996) X­ray structure of the cambialistic superoxide dismutase from Propionibacterium shermanii active with Fe or Mn. J. Biol. Inorg. Chem. 1, 532-541.
  38. Searcy, K.B. and Searcy, D.G. (1981) Superoxide dismutase from the Archaebacterium Thermoplasma acidophilum. Biochim. Biophys. Acta 670, 39-46.
  39. Slykhouse, T.O. and Fee, J.A. (1976) Physical and chemical studies on bacterial superoxide dismutases. Purification and some anion binding properties of the iron­containing protein of Escherichia coli B. J. Biol. Chem. 251, 5472-5477.
  40. Sorkin, D.L. and Miller, A.­F. (1997) Spectroscopic measurement of a long­predicted active site pK in iron-superoxide dismutase from Escherichia coli. Biochemistry 36, 4916-4924.
  41. Sorkin, D.L., Duong, D.K. and Miller, A.­F. (1997) Mutation of tyrosine 34 to phenylalanine eliminates the active site pK of reduced iron­containing superoxide dismutase. Biochemistry 36, 8202-8208.
  42. Stallings, W.C., Powers, T.B., Pattridge, K.A., Fee, J.A. and Ludwig, M.L. (1983) Iron superoxide dismutase from Escherichia coli at 3.1­Å resolution: A structure unlike that of copper/zinc protein at both monomer and dimer levels. Proc. Natl. Acad. Sci. USA 80, 3884-3888.
  43. Stallings, W.C., Metzger, A.L., Pattridge, K.A., Fee, J.A. and Ludwig, M.L. (1991) Structure-function relationships in iron and manganese superoxide dismutases. Free Radic. Res. Commun. 12-13, 259-268.
  44. Stoddard, B.L., Howell, P.L., Ringe, D. and Petsko, G.A. (1990a) The 2.1­Å resolution structure of iron superoxide dismutase from Pseudomonas ovalis. Biochemistry 29, 8885-8893.
  45. Stoddard, B.L., Ringe, D. and Petsko, G.A. (1990b) The structure of iron superoxide dismutase from Pseudomonas ovalis complexed with the inhibitor azide. Protein Engineering 4, 113-119.
  46. Tierney, D.L., Fee, J.A., Ludwig, M.L. and Penner­Hahn, J.E. (1995) X­ray absorption spectroscopy of the iron site in Escherichia coli Fe(III) superoxide dismutase. Biochemistry 34, 1661-1668.
  47. Ursby, T., Adinolfi, B.S., Al­Karadaghi, S., De Vendittis, E. and Bocchini, V. (1999) Iron superoxide dismutase from the archaeon Sulfolobus solfataricus: Analysis of structure and thermostability. J. Mol. Biol. 286, 189-205. Crystallography
  48. Vance, C.K. and Miller, A.­F. (1998) Spectroscopic comparisons of the pH dependencies of Fe­substituted (Mn)superoxide dismutase and Fe-superoxide dismutase. Biochemistry 37, 5518-5527.
  49. Vance, C.K., Kang, Y.M. and Miller, A.­F. (1997) Selective 15N labeling and direct observation by NMR of the active­site glutamine of Fe­containing superoxide dismutase. J. Biomol. NMR 9, 201-206.
  50. Verhagen, M.F., Meussen, E.T. and Hagen, W.R. (1995) On the reduction potentials of Fe and Cu-Zn containing superoxide dismutases. Biochim. Biophys. Acta 1244, 99-103.
  51. Villafranca, J.J., Yost, F.J., Jr. and Fridovich, I. (1974) Magnetic resonance studies of manganese(3) and iron(3) superoxide dismutases. Temperature and frequency dependence of proton relaxation rates of water. J. Biol. Chem. 249, 3532-3536.
  52. Yamakura, F. (1976) Purification, crystallization and properties of iron­containing superoxide dismutase from Pseudomonas ovalis. Biochim. Biophys. Acta 422, 280-294.
  53. Yamakura, F. (1978) A study on the reconstitution of iron-superoxide dismutase from Pseudomonas ovalis. J. Biochem. (Tokyo) 83, 849-857.
  54. Yamakura, F. and Suzuki, K. (1976) Reconstitution of iron-superoxide dismutase. Biochem. Biophys. Res. Commun. 72, 1108-1115.
  55. Yamakura, F. and Suzuki, K. (1980) Cadmium, chromium, and manganese replacement for iron in iron-superoxide dismutase from Pseudomonas ovalis. J. Biochem. (Tokyo) 88, 191-196.
  56. Yamakura, F. and Suzuki, K. (1986) Inactivation of Pseudomonas iron-superoxide dismutase by hydrogen peroxide. Biochim. Biophys. Acta 874, 23-29.
  57. Yamakura, F., Kobayashi, K., Ue, H. and Konno, M. (1995a) The pH­dependent changes of the enzymic activity and spectroscopic properties of iron­substituted manganese superoxide dismutase. A study on the metal­specific activity of Mn­containing superoxide dismutase. Eur. J. Biochem. 227, 700-706.
  58. Yamakura, F., Kobayashi, K., Tagawa, S., Morita, A., Imai, T., Ohmori, D. and Matsumoto, T. (1995b) pH­dependent activity change of superoxide dismutase from Mycobacterium smegmatis. Biochem. Mol. Biol. Int. 36, 233-240.
  59. Yost, F.J., Jr. and Fridovich, I. (1974) An iron­containing superoxide dismutase from Escherichia coli. J. Biol. Chem. 248, 4905-4908.
  60. Youn, H.D., Youn, H., Lee, J.W., Yim, Y.I., Lee, J.K., Hah, Y.C. and Kang, S.O. (1996) Unique isozymes of superoxide dismutase in Streptomyces griseus. Arch. Biochem. Biophys. 334, 341-348.
Bibliography on structural studies Mn-superoxide dismutase
Reviews on superoxide dismutases