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Volumn 125, Issue 1, 1999, Pages 186-193

An azide-insensitive superoxide dismutase from a hyperthermophilic archaeon, Sulfolobus solfataricus

Author keywords

Archaea; Azide; Hyperthermophile; Sulfolobus solfataricus; Superoxide dismutase

Indexed keywords

AZIDE; DIMER; FLUORIDE; GENE PRODUCT; IRON; MANGANESE; METAL; NITROGEN DERIVATIVE; PHENYLALANINE; SUPEROXIDE; SUPEROXIDE DISMUTASE; TYROSINE;

EID: 0032973502     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022258     Document Type: Article
Times cited : (35)

References (37)
  • 1
    • 0019015731 scopus 로고
    • Distinguishing between Mn-containing and Fe-containing superoxide dismutase in crude extracts of cells
    • Kirby, T.W., Blum, J., Kahane, I., and Fridovich, I. (1980) Distinguishing between Mn-containing and Fe-containing superoxide dismutase in crude extracts of cells. Arch. Biochem. Biophys. 201, 551-555
    • (1980) Arch. Biochem. Biophys. , vol.201 , pp. 551-555
    • Kirby, T.W.1    Blum, J.2    Kahane, I.3    Fridovich, I.4
  • 2
    • 0002554499 scopus 로고
    • Regulation and protective role of the microbial superoxide dismutases
    • (Scandalios, J.G., ed.) Cold Spring Harbor Laboratory Press, New York
    • Touati, D. (1992) Regulation and protective role of the microbial superoxide dismutases in Molecular Biology of Free Radical Scavenging Systems (Scandalios, J.G., ed.) pp. 231-261, Cold Spring Harbor Laboratory Press, New York
    • (1992) Molecular Biology of Free Radical Scavenging Systems , pp. 231-261
    • Touati, D.1
  • 3
    • 0000163923 scopus 로고
    • The lesson of archaebacteria
    • (Bengtson, S., ed.) Columbia University Press, New York
    • Stetter, K.O. (1994) The lesson of Archaebacteria in Early Life on Earth (Bengtson, S., ed.) pp. 143-151, Columbia University Press, New York
    • (1994) Early Life on Earth , pp. 143-151
    • Stetter, K.O.1
  • 4
    • 0031441862 scopus 로고    scopus 로고
    • Iron superoxide dismutase from the archaeon sulfolobus solfataricus: Average hydrophobicity and amino acid weight are involved in the adaptation of proteins to extreme environments
    • Russo, A.D., Rullo, R., Nitti, G., Masullo, M., and Bocchini, V. (1997) Iron superoxide dismutase from the archaeon Sulfolobus solfataricus: average hydrophobicity and amino acid weight are involved in the adaptation of proteins to extreme environments. Biochim. Biophys. Acta 1343, 23-30
    • (1997) Biochim. Biophys. Acta , vol.1343 , pp. 23-30
    • Russo, A.D.1    Rullo, R.2    Nitti, G.3    Masullo, M.4    Bocchini, V.5
  • 5
    • 0029984175 scopus 로고    scopus 로고
    • Isolation, characterization and crystallization of an iron-superoxide dismutase from the crenarchaeon sulfolobus acido-caldarius
    • Kardinahl, S., Schmidt, C.L., Petersen, A., and Schäfer, G. (1996) Isolation, characterization and crystallization of an iron-superoxide dismutase from the crenarchaeon Sulfolobus acido-caldarius. FEMS Microbiol. Lett. 138, 65-70
    • (1996) FEMS Microbiol. Lett. , vol.138 , pp. 65-70
    • Kardinahl, S.1    Schmidt, C.L.2    Petersen, A.3    Schäfer, G.4
  • 6
    • 0015275944 scopus 로고
    • Sulfolobus: A new genus of sulfur-oxidizing bacteria living at low pH and high temperature
    • Brock, T.D., Brock, K.M., Bellay, R.T., and Waiss, R.L. (1972) Sulfolobus: a new genus of sulfur-oxidizing bacteria living at low pH and high temperature. Arch. Microbiol. 84, 54-68
    • (1972) Arch. Microbiol. , vol.84 , pp. 54-68
    • Brock, T.D.1    Brock, K.M.2    Bellay, R.T.3    Waiss, R.L.4
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0014691242 scopus 로고
    • Superoxide dismutase: An enzymatic function for erythrocuprein (hemocuprein)
    • McCord, J.M. and Fridovich, I. (1969) Superoxide dismutase: an enzymatic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244, 6049-6055
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 9
    • 0026573580 scopus 로고
    • A general and fast method to generate multiple site directed mutations
    • Mikaelian, I. and Sergeant, A. (1992) A general and fast method to generate multiple site directed mutations. Nucleic Acids Res. 20, 376
    • (1992) Nucleic Acids Res. , vol.20 , pp. 376
    • Mikaelian, I.1    Sergeant, A.2
  • 11
    • 0024978426 scopus 로고
    • Evolution and regulation of the gene encoding superoxide dismutase from the archaebacterium Halobacterium cutirubrum
    • May, B.P. and Dennis, P.P. (1989) Evolution and regulation of the gene encoding superoxide dismutase from the archaebacterium Halobacterium cutirubrum. J. Biol. Chem. 264, 12253-12258
    • (1989) J. Biol. Chem. , vol.264 , pp. 12253-12258
    • May, B.P.1    Dennis, P.P.2
  • 12
    • 0027181280 scopus 로고
    • Nucleotide sequence, transcription and phylogeny of the gene encoding the superoxide dismutase of Sulfolobus acidocaldarius
    • Klenk, H.P., Schleper, C., Schwass, V., and Brudler, R. (1993) Nucleotide sequence, transcription and phylogeny of the gene encoding the superoxide dismutase of Sulfolobus acidocaldarius. Biochim. Biophys. Acta 1174, 95-98
    • (1993) Biochim. Biophys. Acta , vol.1174 , pp. 95-98
    • Klenk, H.P.1    Schleper, C.2    Schwass, V.3    Brudler, R.4
  • 13
    • 0017170525 scopus 로고
    • Physical and chemical studies on bacterial superoxide dismutases
    • Slykhouse, T.O. and Fee, J.A. (1976) Physical and chemical studies on bacterial superoxide dismutases. J. Biol. Chem. 251, 5472-5477
    • (1976) J. Biol. Chem. , vol.251 , pp. 5472-5477
    • Slykhouse, T.O.1    Fee, J.A.2
  • 14
    • 0018928663 scopus 로고
    • The Sulfolobus-"Caldariella" Group: Taxonomy on the basis of the structure of DNA-dependent RNA polymerases
    • Zillig, W., Stetter, K.O., Wunderl, S., Schulz, W., Priess, H., and Scholz, I. (1980) The Sulfolobus-"Caldariella" Group: Taxonomy on the basis of the structure of DNA-dependent RNA polymerases. Arch. Microbiol. 125, 259-269
    • (1980) Arch. Microbiol. , vol.125 , pp. 259-269
    • Zillig, W.1    Stetter, K.O.2    Wunderl, S.3    Schulz, W.4    Priess, H.5    Scholz, I.6
  • 15
    • 0030914069 scopus 로고    scopus 로고
    • Cloning and expression of superoxide dismutase from Aquifex pyrophilus, a hyperthermophilic bacterium
    • Lim, J.-H., Yu, Y.-G., Choi, I.-G., Ryu, J.-R., Ahn, B.-Y., Kim, S.-H., and Han, Y.-S. (1997) Cloning and expression of superoxide dismutase from Aquifex pyrophilus, a hyperthermophilic bacterium. FEBS Lett. 406, 142-146
    • (1997) FEBS Lett. , vol.406 , pp. 142-146
    • Lim, J.-H.1    Yu, Y.-G.2    Choi, I.-G.3    Ryu, J.-R.4    Ahn, B.-Y.5    Kim, S.-H.6    Han, Y.-S.7
  • 16
    • 0017849697 scopus 로고
    • Inhibition of superoxide dismutase by azide
    • Misra, H.P. and Fridovich, I. (1978) Inhibition of superoxide dismutase by azide. Arch. Biochem. Biophys. 189, 317-322
    • (1978) Arch. Biochem. Biophys. , vol.189 , pp. 317-322
    • Misra, H.P.1    Fridovich, I.2
  • 17
    • 0016861525 scopus 로고
    • Superoxide dismutases from a blue-green alga, Plectonema boryanum
    • Asada, K., Yoshikawa, K., Takahashi, M., Maeda, Y., and Enmanji, K. (1975) Superoxide dismutases from a blue-green alga, Plectonema boryanum. J. Biol. Chem. 250, 2801-2807
    • (1975) J. Biol. Chem. , vol.250 , pp. 2801-2807
    • Asada, K.1    Yoshikawa, K.2    Takahashi, M.3    Maeda, Y.4    Enmanji, K.5
  • 18
    • 0023945399 scopus 로고
    • Iron- and manganese-containing superoxide dismutase can be distinguished by analysis of their primary structures
    • Parker, M.W. and Blake, C.C.F. (1988) Iron- and manganese-containing superoxide dismutase can be distinguished by analysis of their primary structures. FEBS Lett. 229, 377-382
    • (1988) FEBS Lett. , vol.229 , pp. 377-382
    • Parker, M.W.1    Blake, C.C.F.2
  • 19
    • 0345093132 scopus 로고
    • Dependence of the activity of manganese enzymes on manganese: A study on manganese superoxide dismutase
    • Yamakura, F. (1995) Dependence of the activity of manganese enzymes on manganese: a study on manganese superoxide dismutase. Kagaku Sosetsu 24, 124-131
    • (1995) Kagaku Sosetsu , vol.24 , pp. 124-131
    • Yamakura, F.1
  • 20
    • 0026325332 scopus 로고
    • Unique characteristics of superoxide dismutase of a strictly anaerobic archaebacterium Methanobacterium thermoautotrophicum
    • Takao, M., Yasui, A., and Oikawa, A. (1991) Unique characteristics of superoxide dismutase of a strictly anaerobic archaebacterium Methanobacterium thermoautotrophicum. J. Biol. Chem. 266, 14151-14154
    • (1991) J. Biol. Chem. , vol.266 , pp. 14151-14154
    • Takao, M.1    Yasui, A.2    Oikawa, A.3
  • 21
    • 0019834273 scopus 로고
    • Isolation and characterization of the iron-containing superoxide dismutase Methanobacterium bryantii
    • Kirby, T.W., Lancaster, J.R., and Fridovich, I. (1981) Isolation and characterization of the iron-containing superoxide dismutase Methanobacterium bryantii. Arch. Biochem. Biophys. 210, 140-148
    • (1981) Arch. Biochem. Biophys. , vol.210 , pp. 140-148
    • Kirby, T.W.1    Lancaster, J.R.2    Fridovich, I.3
  • 22
    • 0028933323 scopus 로고
    • Structure-function in Escherichia coli iron superoxide dismutase: Comparisons with the manganese enzyme from Thermus thermophilus
    • Lau, M.S., Dixon, M.M., Partridge, 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
    • (1995) Biochemistry , vol.34 , pp. 1646-1660
    • Lau, M.S.1    Dixon, M.M.2    Partridge, K.A.3    Stallings, W.C.4    Fee, J.A.5    Ludwig, M.L.6
  • 23
    • 0021774481 scopus 로고
    • Destruction of tryptophan residues by hydrogen peroxide in iron-superoxide dismutase
    • Yamakura, F. (1984) Destruction of tryptophan residues by hydrogen peroxide in iron-superoxide dismutase. Biochem. Biophys. Res. Commun. 122, 635-641
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 635-641
    • Yamakura, F.1
  • 24
    • 0023124274 scopus 로고
    • Effect of hydrogen peroxide on the iron-containing superoxide dismutase of Escherichia coli
    • Beyer, W.F. and Fridovich, I. (1987) Effect of hydrogen peroxide on the iron-containing superoxide dismutase of Escherichia coli. Biochemistry 26, 1251-1257
    • (1987) Biochemistry , vol.26 , pp. 1251-1257
    • Beyer, W.F.1    Fridovich, I.2
  • 25
    • 0028093084 scopus 로고
    • Reaction 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
    • Meier, B., Sehn, A.P., Michel, C., and Saran, M. (1994) Reaction 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
    • (1994) Arch. Biochem. Biophys. , vol.313 , pp. 296-303
    • Meier, B.1    Sehn, A.P.2    Michel, C.3    Saran, M.4
  • 26
    • 0031238606 scopus 로고    scopus 로고
    • Effect of val 73→trp mutation on the reaction of "cambialistic" superoxide dismutase from Propionibacterium shermanii with hydrogen peroxide
    • Gabbianelli, R., Battistoni, A., Capo, C., Polticelli, F., Rotilio, G., Meier, B., and Desideri, A. (1997) Effect of Val 73→Trp mutation on the reaction of "cambialistic" superoxide dismutase from Propionibacterium shermanii with hydrogen peroxide. Arch. Biochem. Biophys. 345, 156-159
    • (1997) Arch. Biochem. Biophys. , vol.345 , pp. 156-159
    • Gabbianelli, R.1    Battistoni, A.2    Capo, C.3    Polticelli, F.4    Rotilio, G.5    Meier, B.6    Desideri, A.7
  • 28
    • 0028994307 scopus 로고
    • 2.0 Å structure of indol-3-glycerol phosphate synthase from the hyperthermophile sulfolobus solfataricus: Possible determinants of protein stability
    • Henning, M., Darimont, B., Sterner, R., Kirschner, K., and Jansonius, J.N. (1995) 2.0 Å structure of indol-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. Structure 3, 1295-1306
    • (1995) Structure , vol.3 , pp. 1295-1306
    • Henning, M.1    Darimont, B.2    Sterner, R.3    Kirschner, K.4    Jansonius, J.N.5
  • 29
    • 0002399828 scopus 로고
    • Phylogenic distribution of three types of superoxide dismutase in organisms and in cell organelles
    • (Bannister, J.V. and Hill, H.A.O., eds.) Elsevier Science, Amsterdam
    • Asada, K., Kanematsu, S., Okada, S., and Hayakawa, T. (1980) Phylogenic distribution of three types of superoxide dismutase in organisms and in cell organelles in Chemical and Biochemical Aspects of Superoxide and Superoxide Dismutase (Bannister, J.V. and Hill, H.A.O., eds.) pp. 136-153, Elsevier Science, Amsterdam
    • (1980) Chemical and Biochemical Aspects of Superoxide and Superoxide Dismutase , pp. 136-153
    • Asada, K.1    Kanematsu, S.2    Okada, S.3    Hayakawa, T.4
  • 30
    • 0020652683 scopus 로고
    • Isolation of iron-containing superoxide dismutase from bacteroides fragilis: Reconstitution as a Mn-containing enzyme
    • Gregory, E.M. and Dapper, C.H. (1983) Isolation of iron-containing superoxide dismutase from Bacteroides fragilis: reconstitution as a Mn-containing enzyme. Arch. Biochem. Biophys. 220, 293-300
    • (1983) Arch. Biochem. Biophys. , vol.220 , pp. 293-300
    • Gregory, E.M.1    Dapper, C.H.2
  • 31
    • 0022273807 scopus 로고
    • 2-induced manganese-containing superoxide dismutase from Bacteroides fragilis
    • 2-induced manganese-containing superoxide dismutase from Bacteroides fragilis. Arch. Biochem. Biophys. 238, 83-89
    • (1985) Arch. Biochem. Biophys. , vol.238 , pp. 83-89
    • Gregory, E.M.1
  • 32
    • 0017343504 scopus 로고
    • Enzymatic defenses against the toxicity of oxygen and of streptonigrin in Escherichia coli
    • Hassan, H.M. and Fridovich, I. (1977) Enzymatic defenses against the toxicity of oxygen and of streptonigrin in Escherichia coli. J. Bacteriol. 129, 1574-1583
    • (1977) J. Bacteriol. , vol.129 , pp. 1574-1583
    • Hassan, H.M.1    Fridovich, I.2
  • 33
    • 0018666716 scopus 로고
    • Intracellular production of superoxide radical and of hydrogen peroxide by redox active compounds
    • Hassan, H.M. and Fridovich, I. (1979) Intracellular production of superoxide radical and of hydrogen peroxide by redox active compounds. Arch. Biochem. Biophys. 196, 385-395
    • (1979) Arch. Biochem. Biophys. , vol.196 , pp. 385-395
    • Hassan, H.M.1    Fridovich, I.2
  • 34
    • 72849125772 scopus 로고
    • The oceans: A possible source of iron in iron-formations
    • Holland, H.D. (1973) The oceans: A possible source of iron in iron-formations. Economic Geol. 68, 1169-1172
    • (1973) Economic Geol. , vol.68 , pp. 1169-1172
    • Holland, H.D.1
  • 35
    • 0016736918 scopus 로고
    • Origin and early evolution of transition element enzymes
    • Egami, F. (1975) Origin and early evolution of transition element enzymes. J. Biochem. 77, 1165-1169
    • (1975) J. Biochem. , vol.77 , pp. 1165-1169
    • Egami, F.1
  • 36
    • 0026052699 scopus 로고
    • Evolution of the ferric enterobactin receptor in gram-negative bacteria
    • Rutz, J.M., Abdullah, T., Singh, S.P., Kalve, V.I., and Klebba, P.E. (1991) Evolution of the ferric enterobactin receptor in gram-negative bacteria. J. Bacteriol. 173, 5964-5974
    • (1991) J. Bacteriol. , vol.173 , pp. 5964-5974
    • Rutz, J.M.1    Abdullah, T.2    Singh, S.P.3    Kalve, V.I.4    Klebba, P.E.5
  • 37
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


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