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Volumn 5, Issue 2, 1996, Pages 248-253

Identification of the residues responsible for the alkaline inhibition of Cu,Zn superoxide dismutase: A site-directed mutagenesis approach

Author keywords

alkaline inhibition; Brownian dynamics; electrostatics; pulse radiolysis; site directed mutagenesis

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE;

EID: 0030062699     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050208     Document Type: Article
Times cited : (17)

References (33)
  • 1
    • 0023194022 scopus 로고
    • Electrostatic control of the rate determining step of the copper,zinc superoxide dismutase catalytic reaction
    • Argese E, Viglino P, Rotilio G, Scarpa M, Rigo A. 1987. Electrostatic control of the rate determining step of the copper,zinc superoxide dismutase catalytic reaction. Biochemistry 26:3224-3228.
    • (1987) Biochemistry , vol.26 , pp. 3224-3228
    • Argese, E.1    Viglino, P.2    Rotilio, G.3    Scarpa, M.4    Rigo, A.5
  • 2
    • 0023463279 scopus 로고
    • Aspects of the structure, function and application of superoxide dismutase
    • Bannister JV, Bannister WH, Rotilio G. 1987. Aspects of the structure, function and application of superoxide dismutase. CRC Biochem 22:111-180.
    • (1987) CRC Biochem , vol.22 , pp. 111-180
    • Bannister, J.V.1    Bannister, W.H.2    Rotilio, G.3
  • 3
    • 0026975772 scopus 로고
    • Temperature-dependent protein folding in vivo-Lower growth temperature increases yield of two genetic variants of Xenopus laevis Cu,Zn superoxide dismutase in E. coli
    • Battistoni A, Carri MT, Mazzetti AP, Rotilio G. 1992. Temperature-dependent protein folding in vivo-Lower growth temperature increases yield of two genetic variants of Xenopus laevis Cu,Zn superoxide dismutase in E. coli. Biochem Biophys Res Commun 186:1339-1344.
    • (1992) Biochem Biophys Res Commun , vol.186 , pp. 1339-1344
    • Battistoni, A.1    Carri, M.T.2    Mazzetti, A.P.3    Rotilio, G.4
  • 4
    • 0025984707 scopus 로고
    • Involvement of the copper in the inhibition of Cu,Zn superoxide dismutase at high pH
    • Calabrese L, Polticelli F, Capo C, Musci G. 1994. Involvement of the copper in the inhibition of Cu,Zn superoxide dismutase at high pH. Free Rads Res Comms 12-13:305-312.
    • (1994) Free Rads Res Comms , vol.12-13 , pp. 305-312
    • Calabrese, L.1    Polticelli, F.2    Capo, C.3    Musci, G.4
  • 5
    • 0024412646 scopus 로고
    • Substitution of arginine for lysine 134 alters electrostatic parameters of the active site in shark Cu,Zn superoxide dismutase
    • Calabrese L, Polticelli F, O'Neill P, Galtieri A, Barra D, Schininà E, Bossa F. 1989. Substitution of arginine for lysine 134 alters electrostatic parameters of the active site in shark Cu,Zn superoxide dismutase. FEBS Lett 250:49-52.
    • (1989) FEBS Lett , vol.250 , pp. 49-52
    • Calabrese, L.1    Polticelli, F.2    O'Neill, P.3    Galtieri, A.4    Barra, D.5    Schininà, E.6    Bossa, F.7
  • 6
    • 0020492513 scopus 로고
    • Carbamoylation of Cu,Zn superoxide dismutase by cyanate. Role of lysmes in enzyme action
    • Cocco D, Rossi L, Barra D, Bossa F, Rotilio G. 1982. Carbamoylation of Cu,Zn superoxide dismutase by cyanate. Role of lysmes in enzyme action. FEBS Lett 150:303-306.
    • (1982) FEBS Lett , vol.150 , pp. 303-306
    • Cocco, D.1    Rossi, L.2    Barra, D.3    Bossa, F.4    Rotilio, G.5
  • 7
    • 0021107965 scopus 로고
    • Solvent accessible surfaces of proteins and nucleic acids
    • Connolly ML. 1983. Solvent accessible surfaces of proteins and nucleic acids. Science 221:709.
    • (1983) Science , vol.221 , pp. 709
    • Connolly, M.L.1
  • 8
    • 0020357311 scopus 로고
    • Electrostatic interactions in the reaction mechanism of bovine erythrocyte superoxide dismutase
    • Cudd A, Fridovich I. 1982. Electrostatic interactions in the reaction mechanism of bovine erythrocyte superoxide dismutase. J Biol Chem 257: 11443-11447.
    • (1982) J Biol Chem , vol.257 , pp. 11443-11447
    • Cudd, A.1    Fridovich, I.2
  • 9
    • 0026586029 scopus 로고
    • Evolutionary conservativeness of electric field in the Cu,Zn superoxide dismutase active site. Evidence for co-ordinated mutation of charged ammo acid residues
    • Desiden A, Falcoru M, Polticelli F, Bolognesi M, Djïnovic K, Rotilio G. 1992. Evolutionary conservativeness of electric field in the Cu,Zn superoxide dismutase active site. Evidence for co-ordinated mutation of charged ammo acid residues. J Mol Biol 225:337-342.
    • (1992) J Mol Biol , vol.225 , pp. 337-342
    • Desiden, A.1    Falcoru, M.2    Polticelli, F.3    Bolognesi, M.4    Djïnovic, K.5    Rotilio, G.6
  • 13
    • 0028300739 scopus 로고
    • The role of arginine 143 in the electrostatics and mechanism of Cu,Zn superoxide dismutase: Computational and experimental evaluation by mutational analysis
    • Fisher CL, Cabelli DE, Tainer JA, Hallewell RA, Getzoff ED. 1994. The role of arginine 143 in the electrostatics and mechanism of Cu,Zn superoxide dismutase: Computational and experimental evaluation by mutational analysis. Proteins Struct Fund Genet 19:24-34.
    • (1994) Proteins Struct Fund Genet , vol.19 , pp. 24-34
    • Fisher, C.L.1    Cabelli, D.E.2    Tainer, J.A.3    Hallewell, R.A.4    Getzoff, E.D.5
  • 16
    • 0022816745 scopus 로고
    • The dielectric constant of a folded protein
    • Gilson MK, Honig BH. 1986. The dielectric constant of a folded protein. Biopolymers 25:2097-2119.
    • (1986) Biopolymers , vol.25 , pp. 2097-2119
    • Gilson, M.K.1    Honig, B.H.2
  • 17
    • 84988087911 scopus 로고
    • Calculating the electrostatic potential of molecules in solution
    • Gilson MK, Sharp KA, Honig BH. 1987. Calculating the electrostatic potential of molecules in solution. J Comp Chem 9:327-335.
    • (1987) J Comp Chem , vol.9 , pp. 327-335
    • Gilson, M.K.1    Sharp, K.A.2    Honig, B.H.3
  • 18
    • 0022964504 scopus 로고
    • Focusing of electric fields in the active site of Cu-Zn superoxide dismutase: Effects of ionic strength and amino-acid modification
    • Klappert I, Hagstrom R, Fine R, Sharp K, Honig B. 1986. Focusing of electric fields in the active site of Cu-Zn superoxide dismutase: Effects of ionic strength and amino-acid modification. Proteins Struct Funet Genet 1:47-59.
    • (1986) Proteins Struct Funet Genet , vol.1 , pp. 47-59
    • Klappert, I.1    Hagstrom, R.2    Fine, R.3    Sharp, K.4    Honig, B.5
  • 19
    • 0025888264 scopus 로고
    • Efficient site-directed mutagenesis using uracil-corttaining DNA
    • Kunkel TA, Bebenek K, McClary J. 1990. Efficient site-directed mutagenesis using uracil-corttaining DNA. Methods Enzymol 204:125-139.
    • (1990) Methods Enzymol , vol.204 , pp. 125-139
    • Kunkel, T.A.1    Bebenek, K.2    McClary, J.3
  • 20
    • 0018801592 scopus 로고
    • Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase
    • Malinowski DP, Fridovich I. 1979. Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase. Biochemistry 18:5909-5916.
    • (1979) Biochemistry , vol.18 , pp. 5909-5916
    • Malinowski, D.P.1    Fridovich, I.2
  • 21
    • 0002111298 scopus 로고
    • Eukaryotic polypeptides expressed in E. coli
    • Glover DM, ed. Oxford, UK: IRL Press
    • Marston FAO. 1987. Eukaryotic polypeptides expressed in E. coli. In: Glover DM, ed. DNA cloning. A practical approach, vol III. Oxford, UK: IRL Press, pp 59-88.
    • (1987) DNA Cloning. A Practical Approach , vol.3 , pp. 59-88
    • Marston, F.A.O.1
  • 22
    • 0021966422 scopus 로고
    • Potential repair of free radical adduct of dGMP and dG by a series of reductants. A pulse radiolytic study
    • O'Neill P, Chapman PW. 1985. Potential repair of free radical adduct of dGMP and dG by a series of reductants. A pulse radiolytic study. Int J Radiai Biol 47:71-80.
    • (1985) Int J Radiai Biol , vol.47 , pp. 71-80
    • O'Neill, P.1    Chapman, P.W.2
  • 26
    • 0029114835 scopus 로고
    • Identification of the residues responsible for the alkaline inhibition of the activity of Cu,Zn superoxide dismutase. A study of native and chemically modified enzymes
    • Polticelli F, O'Neill P, Costanzo S, Lania A, Rotilio G, Desideri A. 1995b. Identification of the residues responsible for the alkaline inhibition of the activity of Cu,Zn superoxide dismutase. A study of native and chemically modified enzymes. Arch Biochem Biophys 321:123-126.
    • (1995) Arch Biochem Biophys , vol.321 , pp. 123-126
    • Polticelli, F.1    O'Neill, P.2    Costanzo, S.3    Lania, A.4    Rotilio, G.5    Desideri, A.6
  • 27
    • 0015520583 scopus 로고
    • Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase
    • Rotilio G, Calabrese L, Bossa F, Barra D, Finazzi Agro' A, Mondovi B. 1972. Properties of the apoprotein and role of copper and zinc in protein conformation and enzyme activity of bovine superoxide dismutase. Biochemistry 11:2182-2187.
    • (1972) Biochemistry , vol.11 , pp. 2182-2187
    • Rotilio, G.1    Calabrese, L.2    Bossa, F.3    Barra, D.4    Finazzi Agro', A.5    Mondovi, B.6
  • 29
    • 33751158844 scopus 로고
    • Simulation of superoxide-superoxide dismutase association rate for six natural variants. Comparison with the experimental catalytic rate
    • Sergi A, Ferrario M, Poiticelli F, O'Neill P, Desideri A. 1994. Simulation of superoxide-superoxide dismutase association rate for six natural variants. Comparison with the experimental catalytic rate. J Phys Chem 98:10554-10557.
    • (1994) J Phys Chem , vol.98 , pp. 10554-10557
    • Sergi, A.1    Ferrario, M.2    Poiticelli, F.3    O'Neill, P.4    Desideri, A.5
  • 30
    • 0023364022 scopus 로고
    • Computer simulations of the diffusion of a substrate to an active site of an enzyme
    • Sharp K, Fine R, Honig B. 1987. Computer simulations of the diffusion of a substrate to an active site of an enzyme. Science 230:1460-1463.
    • (1987) Science , vol.230 , pp. 1460-1463
    • Sharp, K.1    Fine, R.2    Honig, B.3
  • 31
    • 0025110479 scopus 로고
    • Point charge distributions and electrostatic steering in enzyme/substrate encounter: Brownian dynamics of modified copper/zinc superoxide dismutases
    • Sines JJ, Allison SA, McCammon JA. 1990. Point charge distributions and electrostatic steering in enzyme/substrate encounter: Brownian dynamics of modified copper/zinc superoxide dismutases. Biochemistry 29:9403-9412.
    • (1990) Biochemistry , vol.29 , pp. 9403-9412
    • Sines, J.J.1    Allison, S.A.2    McCammon, J.A.3
  • 32
    • 0002291052 scopus 로고
    • Kinetics effects of multiple charge modifications in enzyme-substrate reactions: Brownian dynamics simulations of Cu,Zn superoxide dismutase
    • Sines JJ, McCammon JA, Allison SA. 1992. Kinetics effects of multiple charge modifications in enzyme-substrate reactions: Brownian dynamics simulations of Cu,Zn superoxide dismutase. J Comput Chem 13:66-69.
    • (1992) J Comput Chem , vol.13 , pp. 66-69
    • Sines, J.J.1    McCammon, J.A.2    Allison, S.A.3
  • 33
    • 0020374498 scopus 로고
    • Determination and analysis of the 2 A structure of bovine copper, zinc superoxide dismutase
    • Tainer JA, Getzoff ED, Beem KM, Richardson JS, Richardson DC. 1982. Determination and analysis of the 2 A structure of bovine copper, zinc superoxide dismutase. J Mol Biol 160:181-217.
    • (1982) J Mol Biol , vol.160 , pp. 181-217
    • Tainer, J.A.1    Getzoff, E.D.2    Beem, K.M.3    Richardson, J.S.4    Richardson, D.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.