Structure-Function Relationships in Iron and Manganese Superoxide Dismutases

References

• Stallings W. C., Powers T. B., Pattridge K. A., Fee J. A., Ludwig M. L. Iron superoxide dismutase from Escherichia coli at 3.I Å resolution. Proceedings of the National Academy of Sciences, USA. 1983; 80: 3884–3888
   PubMed Web of Science ®Google Scholar
• Ringe D., Petsko G. A., Yamakurd F., Suzuki K., Ohmori D. Struclure oriron superoxide dismutase from Pseudomonas ovalis at 2.9 Å resolution. Proceedings of the National Academy of Sciences USA 1983; 80: 3897–3883
   Google Scholar
• Stallings W. C., Pattridge K. A., Strong R. K., Ludwig M. L. The structure of manganese superoxide dismutase from Thermus thermophilus HB8 at 2.4 a resolution. Journal of Biological Chemistry 1985; 260: 16424–16432
   PubMed Web of Science ®Google Scholar
• Parker M. W., Blake C. F. Crystal structure of manganese superoxide dismutase from Bacillus stearothermophilus at 2.4 Å resolution. Journal of Moleculur Biology 1988; 199: 649–661
   PubMed Web of Science ®Google Scholar
• Carlioz A., Ludwig M. L., Stallings W. C., Fee J. A., Steinman H. M., Touati D. Iron superoxide dismutase. Nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structures. Journal of Biological Chemistry. 1988; 263: 1555–1562
   PubMedGoogle Scholar
• Sato S., Nakada Y., Nakasawa-Tomizawa K. Amino-acid sequence of a tetrameric manganese superoxide dismutase from. Thermus thermophilus HB. Biochimica et Biophysica Acta. 1987; 912: 178–184
   PubMedGoogle Scholar
• Ludwig M. L., Pattridge K. A., Stallings W. C. Manganese superoxide dismutase. Manganese in Metabolism and Enzyme Function, V. L. Schramm, F. C. Wedler. Academic Press. 1986; 405–430
   Google Scholar
• Hendrickson W. A. Stereochemically restrained refinement of macromolecular structures. Methods in Enzymology 1985; 115: 252–270
   PubMed Web of Science ®Google Scholar
• Brunger A. T., Karplus M., Petsko G. A. Crystallographic refinement by simulated annealing: application to crambin. Acta Crystallographica. 1989; A45: 50–61
   Google Scholar
• Richards F. M. Calculation of molecular volumes and areas for structures of known geometry. Merlrods in Enzymology 1985; 115: 440–464
   PubMedGoogle Scholar
• Sines J., Allison S., Wierzbicki A., McCammon J. A. Brownian dynamics simulation of the superoxide-superoxide dismutase reaction: Fe and Mn enzymes. Journal of Physical Chemistry, in press.
   Google Scholar
• Borders C. L., Jr., Horton P. J., Beyer W. F., Jr. Chemical modification of iron-and manganese-containing superoxide dismutases from. Escherichia coli. Archives of Biochemistry and Biophysics 1989; 268: 74–80
   PubMedGoogle Scholar
• Benkovic J., Tillman T., Cudd A., Fridovich I. Electrostatic facilitation of the reaction catalyzed by the manganese-containing and ironcontaining superoxide dismutases. Archives of Biochemistry and Biophysics. 1983; 221: 329–332
   PubMedGoogle Scholar
• Brock C. J., Walker J. E. Superoxide dismutase from Bacillus sterarothermophilus. Complete amino acid sequence of a manganese enzyme. Biochemstry. 1980; 19: 2873–2882
   PubMed Web of Science ®Google Scholar
• Steinman H. M. The amino acid sequence of manganese superoxide dismutase from. Escherichia coli B. Journal of Biological Chemistry. 1978; 253: 8108–8720
   Google Scholar
• Ditlow C., Johansen J. T., Martin B. M., Svendsen I. The complete amino acid sequence of manganese superoxide dismutase from. Saccharomyces cerevisiae. Carlsberg Research Communications. 1982; 47: 81–91
   Google Scholar
• Barra D., Schinina M. E., Simmaco M., Bannister J. V., Bannister W. H., Rotilio G., Bossa F. The primary structure of human liver manganese superoxide dismutase. Journal of Biological Chemistry 1984; 259: 12595–12601
   PubMed Web of Science ®Google Scholar
• Barra D., Schinina M. E., Bannister W. H., Bannister J. V., Bossa F. The primary structure of iron-superoxide dismutase from. Photobacterium leiognathi. Journal of Biological Chemistry. 1987; 262: 1001–1009
   PubMed Web of Science ®Google Scholar
• Fee J. A., McClune G. J., Lees A. C., Zidovetski R., Pecht I. The pH dependence of the spectral and anion binding properties of iron containing superoxide dismutase from E. coli B: an explanation for the azide inhibition of dismutase activity. Israel Journal of Chemistry. 1981; 21: 54–58
   Web of Science ®Google Scholar
• Bull C., Fee J. A. Steady-state kinetic studies of superoxide dismutases: properties of the iron containing protein from. Escherichia coli. Journal of the American Chemistry Society. 1985; 107: 3295–3304
   Web of Science ®Google Scholar
• Whittakerand J. W., Solomon E. I. Journal of the American Chemistry. Society. 1986; 108: 835–836, Spectroscopic studics on ferrous non-hcmc iron active sites: variable-temperature MCD probe of ground-and excited-state splittings in iron superoxide dismutase and lipoxygenase.
   Google Scholar
• Bertini I., Luchinat C., Monnanni R. Evidence of the breaking of the copper-imidazolate bridge in copper/cobalt-substituted superoxide dismutase upon reduction of the copper (II) centers. Journal of the American Chemistry Society. 1985; 107: 2178–2179
   Google Scholar
• Niederhoffer E. C., Fee J. A., Papaefthymiou V., Münck E. Magnetic resonance studies involving iron superoxide dismutase from. E. coli. Isotupe and Nuclear Chemistry Division. Annual Report. Los Alanios Natiorial Laboratory. 1987; 79–84
   Google Scholar
• Parker M. W., Schinina M. E., Bossa F., Bannister J. V. Chemical aspects of the structure, function, and evolution of superoxidc dismutascs. Inorganica Chimica Acta. 1984; 91: 307–317
   Web of Science ®Google Scholar