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Volumn 253, Issue 1, 1998, Pages 49-56

Inactivation and destruction of conserved Trp159 of Fe-superoxide dismutase from Porphyromonas gingivalis by hydrogen peroxide

Author keywords

Cambialistic superoxide dismutase; Destruction of tryptophan residue; Fe superoxide dismutase; Hydrogen peroxide; Recombinant superoxide dismutase

Indexed keywords

HYDROGEN PEROXIDE; SUPEROXIDE DISMUTASE;

EID: 0032054583     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2530049.x     Document Type: Article
Times cited : (34)

References (46)
  • 2
    • 0002877219 scopus 로고
    • Superoxide dismutase: Protein chemistry and structure-function relationship
    • (Oberley, L. W., ed.) CRC Press, Boca Raton FL
    • Steinman, H. (1982) Superoxide dismutase: protein chemistry and structure-function relationship, in Superoxide dismutase (Oberley, L. W., ed.) vol. 1, pp. 11 - 69, CRC Press, Boca Raton FL.
    • (1982) Superoxide Dismutase , vol.1 , pp. 11-69
    • Steinman, H.1
  • 3
    • 0023463279 scopus 로고
    • Aspects of the structure, function, and applications of Superoxide dismutase
    • Bannister, J. V., Bannister, W. H. & Rotilio, G. (1987) Aspects of the structure, function, and applications of Superoxide dismutase, CRC Crit. Rev. Biochem. 22, 111 - 180.
    • (1987) CRC Crit. Rev. Biochem. , vol.22 , pp. 111-180
    • Bannister, J.V.1    Bannister, W.H.2    Rotilio, G.3
  • 4
    • 0029778889 scopus 로고    scopus 로고
    • A novel nickel-containing Superoxide dismutase from Streptomyces spp.
    • Youn, H.-D., Kim, E.-J., Roe, J.-H., Hah, Y. C. & Kang, S.-O. (1996) A novel nickel-containing Superoxide dismutase from Streptomyces spp., Biochem. J. 318, 889 - 896.
    • (1996) Biochem. J. , vol.318 , pp. 889-896
    • Youn, H.-D.1    Kim, E.-J.2    Roe, J.-H.3    Hah, Y.C.4    Kang, S.-O.5
  • 5
    • 0029849183 scopus 로고    scopus 로고
    • Differential expression of Superoxide dismutase containing Ni, and Fe/Zn in Streptomyces coelicolor
    • Kim, E.-J., Kim, H.-P., Hah, Y. C. & Roe, J.-H. (1996) Differential expression of Superoxide dismutase containing Ni, and Fe/Zn in Streptomyces coelicolor, Eur. J. Biochem. 241, 178 - 185.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 178-185
    • Kim, E.-J.1    Kim, H.-P.2    Hah, Y.C.3    Roe, J.-H.4
  • 7
    • 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
  • 8
    • 0022995840 scopus 로고
    • Inuctivution of Pseudomonas iron-superoxide dismutase by hydrogen peroxide
    • Yamakura F. & Suzuki, K. (1986) Inuctivution of Pseudomonas iron-superoxide dismutase by hydrogen peroxide, Biochem. Biophys. Acta 874, 23 - 29.
    • (1986) Biochem. Biophys. Acta , vol.874 , pp. 23-29
    • Yamakura, F.1    Suzuki, K.2
  • 9
    • 0023124274 scopus 로고
    • Effect of hydrogen peroxide on the iron-containing Superoxide dismutase of Escherichia coli
    • Beyer, W. F. & 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
  • 11
    • 0026325332 scopus 로고
    • Unique characteristics of Superoxide dismutase of a strictly anaerobic archaebacterium Methanobacterium thermoautotrophicum
    • Takao, M., Yasui, A. & 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
  • 13
    • 0017314966 scopus 로고
    • Superoxide dismutase, reversible removal of manganese and its substitution by cobalt, nickel, or zinc
    • Ose, D. E. & Fridovich, I. (1976) Superoxide dismutase, reversible removal of manganese and its substitution by cobalt, nickel, or zinc, J. Biol. Chem. 251, 1217 - 1218.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1217-1218
    • Ose, D.E.1    Fridovich, I.2
  • 14
    • 0017706064 scopus 로고
    • Superoxide dismutase from Bacillus stearothermophilus: Reversible removal of manganese and its replacement by other metals
    • Brock, C. J. & Harris, J. I. (1977) Superoxide dismutase from Bacillus stearothermophilus: reversible removal of manganese and its replacement by other metals. Biochem. Soc. Trans. 5, 1533 - 1539.
    • (1977) Biochem. Soc. Trans. , vol.5 , pp. 1533-1539
    • Brock, C.J.1    Harris, J.I.2
  • 15
    • 0008947897 scopus 로고
    • Superoxide dismutase from prokaryote and eucaryote bioluminescent organisms
    • (Michelson. A. M., McCord, J. M. & Fridovich, I., eds) Acadmic Press, London
    • Puget, K., Lavelle, F. & Michelson, A. M. (1977) Superoxide dismutase from prokaryote and eucaryote bioluminescent organisms, in Superoxide and Superoxide dismutase (Michelson. A. M., McCord, J. M. & Fridovich, I., eds) pp. 140-150, Acadmic Press, London.
    • (1977) Superoxide and Superoxide Dismutase , pp. 140-150
    • Puget, K.1    Lavelle, F.2    Michelson, A.M.3
  • 16
    • 0019035043 scopus 로고
    • Cadmium, chromium, and manganese replacement for iron in iron-superoxide dismutase from Pseudomonas ovalis
    • Yamakura, F. & Suzuki, K. (1980) Cadmium, chromium, and manganese replacement for iron in iron-superoxide dismutase from Pseudomonas ovalis. J. Biochem. (Tokyo) 88, 191 - 196.
    • (1980) J. Biochem. (Tokyo) , vol.88 , pp. 191-196
    • Yamakura, F.1    Suzuki, K.2
  • 17
    • 0020356135 scopus 로고
    • Synthesis of either Fe- or Mn-superoxide dismutase with an apparently identical protein moiety by an anaerobic bacterium dependent on the metal supplied
    • Meier, B., Barra, D., Bossa, F., Calabrese, L. & Rotilio, G. (1982) Synthesis of either Fe- or Mn-superoxide dismutase with an apparently identical protein moiety by an anaerobic bacterium dependent on the metal supplied. J. Biol. Chem. 257, 13 977 - 13 980.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13977-13980
    • Meier, B.1    Barra, D.2    Bossa, F.3    Calabrese, L.4    Rotilio, G.5
  • 18
    • 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
  • 19
    • 0022570126 scopus 로고
    • Isolation and reconstitution of iron- And manganese-containing Superoxide dismutase from Bucteroides thetaiotaomicron
    • Pennington, C. D. & Gregory, E. U. (1986) Isolation and reconstitution of iron- and manganese-containing Superoxide dismutase from Bucteroides thetaiotaomicron, J. Bacteriol. 166, 528 - 532.
    • (1986) J. Bacteriol. , vol.166 , pp. 528-532
    • Pennington, C.D.1    Gregory, E.U.2
  • 20
    • 0025219013 scopus 로고
    • Characterization of Superoxide dismutases purified from either anaerobically maintained or aerated Bacteroides gingivalis
    • Amano, A., Shizukuishi, S., Tamagawa, H., Iwakura, K., Tsunasawa, S. & Tsunemitsu, A. (1990) Characterization of Superoxide dismutases purified from either anaerobically maintained or aerated Bacteroides gingivalis. J. Bacteriol. 172, 1457 - 1463.
    • (1990) J. Bacteriol. , vol.172 , pp. 1457-1463
    • Amano, A.1    Shizukuishi, S.2    Tamagawa, H.3    Iwakura, K.4    Tsunasawa, S.5    Tsunemitsu, A.6
  • 21
    • 0023030627 scopus 로고
    • A Streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor
    • Martin, M. E., Byers, B. R., Olson, M. O. J., Salin, M. L., Arec-Neaux, E. L. & Tolbert, C. (1986) A Streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor. J. Biol. Chem. 261, 9361 - 9367.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9361-9367
    • Martin, M.E.1    Byers, B.R.2    Olson, M.O.J.3    Salin, M.L.4    Arec-Neaux, E.L.5    Tolbert, C.6
  • 22
    • 0025853830 scopus 로고
    • Iron- and manganese-containing Superoxide dismutase from Methylomonas J: Identity of the protein moiety and amino acid sequence
    • Matsumoto, T., Terauchi, T., Isobe, T., Matsuoka, K. & Yamakura, F. (1991) Iron- and manganese-containing Superoxide dismutase from Methylomonas J: identity of the protein moiety and amino acid sequence, Biochemistry, 30, 3210 - 3215.
    • (1991) Biochemistry , vol.30 , pp. 3210-3215
    • Matsumoto, T.1    Terauchi, T.2    Isobe, T.3    Matsuoka, K.4    Yamakura, F.5
  • 23
    • 0028093084 scopus 로고
    • Reactions of hydrogen peroxide with sueproxide dismutase from Propionibacterium shermanii - An enzyme which is equally active with iron or manganese-are independent of the prosthetic metal
    • Meier, B., Sehan, A. P., Michel, C. & Saran, M. (1994) Reactions of hydrogen peroxide with sueproxide 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    Sehan, A.P.2    Michel, C.3    Saran, M.4
  • 24
    • 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. & 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
  • 25
    • 0025155014 scopus 로고
    • The primary structure of Superoxide dismutase purified from anaerobically maintained Bacteroides gingivalis
    • Amano, A., Shizukuishi, S., Tsunemitsu, A., Maekawa, K. & Tsunemitsu, S. (1990) The primary structure of Superoxide dismutase purified from anaerobically maintained Bacteroides gingivalis, FEBS Lett. 272, 217 - 220.
    • (1990) FEBS Lett. , vol.272 , pp. 217-220
    • Amano, A.1    Shizukuishi, S.2    Tsunemitsu, A.3    Maekawa, K.4    Tsunemitsu, S.5
  • 26
    • 0025696672 scopus 로고
    • The Superoxide dismutase-encoding gene of the obligately anaerobic bacterium Bacteroides gingivalis
    • Nakayama, K. (1990) The Superoxide dismutase-encoding gene of the obligately anaerobic bacterium Bacteroides gingivalis, Gene (Amst.) 96, 149 - 150.
    • (1990) Gene (Amst.) , vol.96 , pp. 149-150
    • Nakayama, K.1
  • 27
    • 0022683672 scopus 로고
    • Isolation of superoxide dismutase mutants in Escherichia coli: Is superoxide dismutase necessary for aerobic life?
    • Carlioz, A. & Touati, D. (1986) Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? EMBO J. 5, 623 - 630.
    • (1986) EMBO J. , vol.5 , pp. 623-630
    • Carlioz, A.1    Touati, D.2
  • 28
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymatic function for erythrocuprein (hemocuprein)
    • McCord, J. M. & 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
  • 30
    • 0017289045 scopus 로고
    • Purification, crystallization, and properties of iron-containing Superoxide dismutase from Pseudomonas ovalis
    • Yamakura, F. (1976) Purification, crystallization, and properties of iron-containing Superoxide dismutase from Pseudomonas ovalis, Biochim. Biophys. Acta 422, 280 - 294.
    • (1976) Biochim. Biophys. Acta , vol.422 , pp. 280-294
    • Yamakura, F.1
  • 31
    • 78651153791 scopus 로고
    • Disc electrophoresis-II. Method and application to human serum proteins
    • Davis, B. J. (1964) Disc electrophoresis-II. Method and application to human serum proteins, Ann. NY Acad. Sci. 121, 404 - 427.
    • (1964) Ann. NY Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 32
    • 0019795076 scopus 로고
    • Resolution of 52 ninhydrin-positive compounds with a high-speed amino acid analysis
    • Murayama, K. & Sugawara, T. (1981) Resolution of 52 ninhydrin-positive compounds with a high-speed amino acid analysis, J. Chromatogr. 224, 315 - 321.
    • (1981) J. Chromatogr. , vol.224 , pp. 315-321
    • Murayama, K.1    Sugawara, T.2
  • 33
    • 0023945399 scopus 로고
    • Iron- and manganese-containing Superoxide dismutase can be distinguished by analysis of their primary structures
    • Parker, M. W. & Blake, C. C. F. (1986) Iron- and manganese-containing Superoxide dismutase can be distinguished by analysis of their primary structures, FEBS Lett. 229, 377 - 382.
    • (1986) FEBS Lett. , vol.229 , pp. 377-382
    • Parker, M.W.1    Blake, C.C.F.2
  • 34
    • 0028933323 scopus 로고
    • Structure-function in Escherichia coli iron Superoxide dismutase: Comparisons with the manganese enzyme from Thermus thermophilus
    • Lah, M. S., Dixon, M. M. Pattridge, K. A., Stallings, W. C., Fee, J. A. & 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
    • Lah, M.S.1    Dixon, M.M.2    Pattridge, K.A.3    Stallings, W.C.4    Fee, J.A.5    Ludwig, M.L.6
  • 35
    • 0025196784 scopus 로고
    • The 2.1 Å resolution structure of iron Superoxide dismutase from Pseudomonas ovalis
    • Stoddard, B. L., Howell, P. L., Ringe, D. & Petsko, G. A. (1990) The 2.1 Å resolution structure of iron Superoxide dismutase from Pseudomonas ovalis, Biochemistry 29, 8885 - 8893.
    • (1990) Biochemistry , vol.29 , pp. 8885-8893
    • Stoddard, B.L.1    Howell, P.L.2    Ringe, D.3    Petsko, G.A.4
  • 36
    • 0024292275 scopus 로고
    • Crystal structure of manganese Superoxide dismutase from Bacillus stearothermophilus at 2.4 A resolution
    • Parker, M. W. & Blake, C. C. F (1988) Crystal structure of manganese Superoxide dismutase from Bacillus stearothermophilus at 2.4 A resolution. J. Mol. Biol. 199, 649 - 661.
    • (1988) J. Mol. Biol. , vol.199 , pp. 649-661
    • Parker, M.W.1    Blake, C.C.F.2
  • 37
    • 0026688441 scopus 로고
    • The structure of human mitochondria manganese superoxide dismutase reveals a novel tetrameric interface of two 4 Helix bundles
    • Borgstahl, G. E. O., Parge, H. E., Hichey, M. J., Beyer, W. F., Hallewell, R. A. & Tainer, J. A. (1992) The structure of human mitochondria manganese superoxide dismutase reveals a novel tetrameric interface of two 4 Helix bundles, Cell 71, 107 - 118.
    • (1992) Cell , vol.71 , pp. 107-118
    • Borgstahl, G.E.O.1    Parge, H.E.2    Hichey, M.J.3    Beyer, W.F.4    Hallewell, R.A.5    Tainer, J.A.6
  • 38
    • 0027481686 scopus 로고
    • Comparison of the crystal structures of genetically engineered human manganese superioxide dismutase and manganese Superoxide dismutase from Thermus thermophilus: Differences in dimer-dimer interaction
    • Wagner, U. G., Pattridge, K. A., Ludwig, M. L., Stalling, W. C., Werber, M. M., Oefner, C., Frolow, F. & Sussman, J. L. (1993) Comparison of the crystal structures of genetically engineered human manganese superioxide dismutase and manganese Superoxide dismutase from Thermus thermophilus: differences in dimer-dimer interaction. Protein Sci. 2, 814 - 825.
    • (1993) Protein Sci. , vol.2 , pp. 814-825
    • Wagner, U.G.1    Pattridge, K.A.2    Ludwig, M.L.3    Stalling, W.C.4    Werber, M.M.5    Oefner, C.6    Frolow, F.7    Sussman, J.L.8
  • 39
    • 0001122503 scopus 로고    scopus 로고
    • X-ray structure of the cambialistic Superoxide dismutase from Propionibacterium shermanii active with Fe and Mn
    • Schmidt, M. Meier, B. & Parak, F. (1996) X-ray structure of the cambialistic Superoxide dismutase from Propionibacterium shermanii active with Fe and Mn, J. Biol. Inorg. Chem. 1, 532 - 541.
    • (1996) J. Biol. Inorg. Chem. , vol.1 , pp. 532-541
    • Schmidt, M.1    Meier, B.2    Parak, F.3
  • 40
    • 0027954501 scopus 로고
    • Regulation of an in vivo metal-exchangeable superoxide dismutase from Propionibacterium shermanii exhibiting activity with different metal cofactors
    • Meier, B., Sehn, A., Schinina, M. E. & Barra, D. (1994) Regulation of an in vivo metal-exchangeable superoxide dismutase from Propionibacterium shermanii exhibiting activity with different metal cofactors, Eur. J. Biol. 219, 463 - 468.
    • (1994) Eur. J. Biol. , vol.219 , pp. 463-468
    • Meier, B.1    Sehn, A.2    Schinina, M.E.3    Barra, D.4
  • 41
    • 0023659711 scopus 로고
    • Amino acid sequence of iron-superoxide dismutase from Pseudomonas ovalis
    • Isobe, T., Fang, Y.-I., Muno, D., Okuyama, T., Ohmori, D. & Yamakura, F. (1987) Amino acid sequence of iron-superoxide dismutase from Pseudomonas ovalis. FEBS Lett. 223, 92 - 96.
    • (1987) FEBS Lett. , vol.223 , pp. 92-96
    • Isobe, T.1    Fang, Y.-I.2    Muno, D.3    Okuyama, T.4    Ohmori, D.5    Yamakura, F.6
  • 42
    • 0023109533 scopus 로고
    • The primary structure of iron-superoxide dismutase from Photobacterium leiognathi
    • Barra, D., Schinina, M. E. Bannister, W. H., Bannister, J. V. & Bossa, F. (1987) The primary structure of iron-superoxide dismutase from Photobacterium leiognathi, J. Biol. Chem. 262, 1001 - 1009.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1001-1009
    • Barra, D.1    Schinina, M.E.2    Bannister, W.H.3    Bannister, J.V.4    Bossa, F.5
  • 43
  • 44
    • 0018241823 scopus 로고
    • The amino acid sequence of manganese Superoxide dismutase from Escherichia coli B
    • Steinman, H. M. (1978) The amino acid sequence of manganese Superoxide dismutase from Escherichia coli B, J. Biol. Chem. 253, 8708 - 8720.
    • (1978) J. Biol. Chem. , vol.253 , pp. 8708-8720
    • Steinman, H.M.1
  • 45
    • 0025043659 scopus 로고
    • Characterization of a superoxide dismutase gene from the archebacterium Methano-bacterium thermoautotrophicum
    • Takao, M., Oikawa, A. & Yasui, A. (1990) Characterization of a superoxide dismutase gene from the archebacterium Methano-bacterium thermoautotrophicum. Arch. Biochem. Biophys. 238, 210 - 216.
    • (1990) Arch. Biochem. Biophys. , vol.238 , pp. 210-216
    • Takao, M.1    Oikawa, A.2    Yasui, A.3
  • 46
    • 0023902809 scopus 로고
    • Isolation and characterization of complementary DNAs encoding human manganese-containing superoxide dismutase
    • Ho, Y-S. & Crapo, J. D. (1988) Isolation and characterization of complementary DNAs encoding human manganese-containing superoxide dismutase, FEBS Lett. 229, 256 - 260.
    • (1988) FEBS Lett. , vol.229 , pp. 256-260
    • Ho, Y.-S.1    Crapo, J.D.2


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