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Volumn 29, Issue 5-6, 2008, Pages 134-168

Second-sphere tuning of the metal ion reduction potentials in iron and manganese superoxide dismutases

Author keywords

Density functional theory; Magnetic circular dichroism spectroscopy; Metal ion redox tuning; Quantum mechanics molecularmechanics calculations; Superoxide dismutases

Indexed keywords


EID: 56849107475     PISSN: 02603594     EISSN: 15489574     Source Type: Journal    
DOI: 10.1080/02603590802429529     Document Type: Article
Times cited : (38)

References (91)
  • 1
    • 0021126946 scopus 로고
    • Manganese and iron superoxide dismutases are structural homologs
    • Stallings, W. C., K. A. Pattridge, R. K. Strong, and M. L. Ludwig, 1984. Manganese and iron superoxide dismutases are structural homologs. J. Biol. Chem., 259, 10695-10699.
    • (1984) J. Biol. Chem , vol.259 , pp. 10695-10699
    • Stallings, W.C.1    Pattridge, K.A.2    Strong, R.K.3    Ludwig, M.L.4
  • 2
    • 0028933323 scopus 로고
    • Structure-function in Escherichia-coli iron superoxide-dismutase-Comparisons with the manganese enzyme from Thermusthermophilus
    • Lah, M. S., M. M. Dixon, K. A. Partridge, W. C. Stallings, J. A. Fee, and M. L. Ludwig, 1995. Structure-function in Escherichia-coli iron superoxide-dismutase-Comparisons with the manganese enzyme from Thermusthermophilus. Biochem., 34, 1646-1660.
    • (1995) Biochem , vol.34 , pp. 1646-1660
    • Lah, M.S.1    Dixon, M.M.2    Partridge, K.A.3    Stallings, W.C.4    Fee, J.A.5    Ludwig, M.L.6
  • 4
    • 0029778889 scopus 로고    scopus 로고
    • A novel nickel-containing superoxide dismutase from Streptomyces spp
    • Youn, H., E. Kim, J. Roe, Y. C. Hah, and S. Kang, 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.1    Kim, E.2    Roe, J.3    Hah, Y.C.4    Kang, S.5
  • 5
    • 2942556712 scopus 로고    scopus 로고
    • Crystal structure of nickel-containing superoxide dismutase reveals another type of active site
    • Wuerges, J., J.-W. Lee, Y.-I. Yim, H.-S. Yim, S.-O. Kang, and K. D. Carugo, 2004. Crystal structure of nickel-containing superoxide dismutase reveals another type of active site. Proc. Natl. Acad. Sci. U.S.A., 101, 8569-8574.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 8569-8574
    • Wuerges, J.1    Lee, J.-W.2    Yim, Y.-I.3    Yim, H.-S.4    Kang, S.-O.5    Carugo, K.D.6
  • 7
    • 33746932518 scopus 로고    scopus 로고
    • Activation of superoxide dismutases: Putting the metal to the pedal
    • Culotta, V. C., M. Yang, and T. V. O'Halleron, 2006. Activation of superoxide dismutases: Putting the metal to the pedal. Biochim. Biophys. Acta., 1763, 747-758.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 747-758
    • Culotta, V.C.1    Yang, M.2    O'Halleron, T.V.3
  • 8
    • 0034306267 scopus 로고    scopus 로고
    • Mitochondria, oxygen free radicals, disease and ageing
    • Raha, S. and B. H. Robinson, 2000. Mitochondria, oxygen free radicals, disease and ageing. Trends Biochem. Sci., 25, 502-508.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 502-508
    • Raha, S.1    Robinson, B.H.2
  • 10
    • 0021270566 scopus 로고
    • Isolation of the Escherichia coli iron superoxide dismutase gene: Evidence that intracellular superoxide concentration does not regulate oxygen-dependent synthesis of the manganese superoxide dismutase
    • Nettleton, C. J., C. Bull, C. Baldwin, and J. A. Fee, 1984. Isolation of the Escherichia coli iron superoxide dismutase gene: Evidence that intracellular superoxide concentration does not regulate oxygen-dependent synthesis of the manganese superoxide dismutase. Proc. Natl. Acad. Sci. U.S.A., 81, 4970-4973.
    • (1984) Proc. Natl. Acad. Sci. U.S.A , vol.81 , pp. 4970-4973
    • Nettleton, C.J.1    Bull, C.2    Baldwin, C.3    Fee, J.A.4
  • 11
    • 0021924999 scopus 로고
    • Induction of superoxide dismutases in Escherichia coli B by metal chelators
    • Pugh, S. Y. R. and I. Fridovich, 1985. Induction of superoxide dismutases in Escherichia coli B by metal chelators. Journal of Bacteriology, 162, 196-202.
    • (1985) Journal of Bacteriology , vol.162 , pp. 196-202
    • Pugh, S.Y.R.1    Fridovich, I.2
  • 12
    • 0015903497 scopus 로고
    • An iron-containing superoxide dismutase from Escherichia coli
    • Yost, F. J. and I. Fridovich, 1973. An iron-containing superoxide dismutase from Escherichia coli. J. Biol. Chem., 248, 4905-4908.
    • (1973) J. Biol. Chem , vol.248 , pp. 4905-4908
    • Yost, F.J.1    Fridovich, I.2
  • 13
  • 15
    • 0000755267 scopus 로고
    • Kinetic-studies of superoxide dismutases - Properties of the manganese-containing protein from Thermus-thermophilus
    • Bull, C., E. C. Niederhoffer, T. Yoshida, and J. A. Fee, 1991. Kinetic-studies of superoxide dismutases - Properties of the manganese-containing protein from Thermus-thermophilus. J. Am. Chem. Soc., 113, 4069-4076.
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 4069-4076
    • Bull, C.1    Niederhoffer, E.C.2    Yoshida, T.3    Fee, J.A.4
  • 16
    • 0000348087 scopus 로고
    • Steady-state kinetic studies of superoxide dismutases: Properties of the iron containing protein from Escherichia coli
    • Bull, C. and J. A. Fee, 1985. Steady-state kinetic studies of superoxide dismutases: Properties of the iron containing protein from Escherichia coli. J. Am. Chem. Soc., 107, 3295-3304.
    • (1985) J. Am. Chem. Soc , vol.107 , pp. 3295-3304
    • Bull, C.1    Fee, J.A.2
  • 17
    • 0037185044 scopus 로고    scopus 로고
    • Coupled redox potentials in manganese and iron superoxide dismutases from reaction kinetics and density functional/electrostatics calculations
    • Han, W. G., T. Lovell, and L. Noodleman, 2002. Coupled redox potentials in manganese and iron superoxide dismutases from reaction kinetics and density functional/electrostatics calculations. Inorg. Chem., 41, 205-218.
    • (2002) Inorg. Chem , vol.41 , pp. 205-218
    • Han, W.G.1    Lovell, T.2    Noodleman, L.3
  • 18
    • 0000192330 scopus 로고    scopus 로고
    • Density functional and electrostatic calculations of manganese superoxide dismutase active site complexes in protein environments
    • Li, J., C. L. Fisher, R. Konecny, D. Bashford, and L. Noodleman, 1999. Density functional and electrostatic calculations of manganese superoxide dismutase active site complexes in protein environments. Inorg. Chem. 38, 929-939.
    • (1999) Inorg. Chem , vol.38 , pp. 929-939
    • Li, J.1    Fisher, C.L.2    Konecny, R.3    Bashford, D.4    Noodleman, L.5
  • 19
    • 33747201345 scopus 로고    scopus 로고
    • The reaction mechanism of iron and manganese superoxide dismutases studied by theoretical calculations
    • Rulíšek, L., K. P. Jensen, K. Lundgren, and U. Ryde, 2006. The reaction mechanism of iron and manganese superoxide dismutases studied by theoretical calculations. J. Comput. Chem., 27, 1398-1410.
    • (2006) J. Comput. Chem , vol.27 , pp. 1398-1410
    • Rulíšek, L.1    Jensen, K.P.2    Lundgren, K.3    Ryde, U.4
  • 21
    • 0020714518 scopus 로고
    • Potentiometrie titrations and oxidation-reduction potentials of several iron superoxide dismutases
    • Barrette, W. C., Jr., D. T. Sawyer, J. A. Fee, and K. Asada, 1983. Potentiometrie titrations and oxidation-reduction potentials of several iron superoxide dismutases. Biochem., 22, 624-627.
    • (1983) Biochem , vol.22 , pp. 624-627
    • Barrette Jr., W.C.1    Sawyer, D.T.2    Fee, J.A.3    Asada, K.4
  • 22
    • 0018786876 scopus 로고
    • Potentiometric titrations and oxidation-reduction potentials of manganese and copper-zinc superoxide dismutases
    • Lawrence, G. D. and D. T. Sawyer, 1979. Potentiometric titrations and oxidation-reduction potentials of manganese and copper-zinc superoxide dismutases. Biochem., 18, 3045-3050.
    • (1979) Biochem , vol.18 , pp. 3045-3050
    • Lawrence, G.D.1    Sawyer, D.T.2
  • 24
    • 0017374830 scopus 로고
    • A pulse-radiolysis study of the manganese-containing superoxide dismutase from Bacillus stearothermophilus
    • McAdam, M. E., R. A. Fox, F. Lavelle, and E. M. Fielden, 1977. A pulse-radiolysis study of the manganese-containing superoxide dismutase from Bacillus stearothermophilus. Biochem. J., 165, 81-87.
    • (1977) Biochem. J , vol.165 , pp. 81-87
    • McAdam, M.E.1    Fox, R.A.2    Lavelle, F.3    Fielden, E.M.4
  • 25
    • 0033609790 scopus 로고    scopus 로고
    • Characterization of the product inhibited complex in catalysis by human manganese superoxide dismutase
    • Hearn, A. S., C. K. Tu, H. S. Nick, and D. N. Silverman, 1999. Characterization of the product inhibited complex in catalysis by human manganese superoxide dismutase. J. Biol. Chem., 274, 24457-24460.
    • (1999) J. Biol. Chem , vol.274 , pp. 24457-24460
    • Hearn, A.S.1    Tu, C.K.2    Nick, H.S.3    Silverman, D.N.4
  • 26
    • 39749091799 scopus 로고    scopus 로고
    • The kinetic mechanism of manganese-containing superoxide dismutase from Deinococcus radiodurans: A specialized enzyme for the elimination of high superoxide concentrations
    • Abreu, I. A., A. S. Hearn, H. An, H. S. Nick, D. N. Silverman, and D. E. Cabelli, 2008. The kinetic mechanism of manganese-containing superoxide dismutase from Deinococcus radiodurans: A specialized enzyme for the elimination of high superoxide concentrations. Biochem., 47, 2350-2356.
    • (2008) Biochem , vol.47 , pp. 2350-2356
    • Abreu, I.A.1    Hearn, A.S.2    An, H.3    Nick, H.S.4    Silverman, D.N.5    Cabelli, D.E.6
  • 27
    • 13444257644 scopus 로고    scopus 로고
    • Probing the geometric and electronic structures of the low-temperature azide adduct and the product-inhibited form of the oxidized manganese superoxide dismutase
    • Jackson, T. A., A. Karapetian, A.-F. Miller, and T. C. Brunold, 2005. Probing the geometric and electronic structures of the low-temperature azide adduct and the product-inhibited form of the oxidized manganese superoxide dismutase. Biochem., 44, 1504-1520.
    • (2005) Biochem , vol.44 , pp. 1504-1520
    • Jackson, T.A.1    Karapetian, A.2    Miller, A.-F.3    Brunold, T.C.4
  • 28
    • 0028938504 scopus 로고
    • X-Ray-absorption spectroscopy of the iron site in Escherichia-coli Fe(III) superoxide-dismutase
    • Tierney, D. L., J. A. Fee, M. L. Ludwig, and J. E. Penner-Hahn, 1995. X-Ray-absorption spectroscopy of the iron site in Escherichia-coli Fe(III) superoxide-dismutase. Biochem., 34, 1661-1668.
    • (1995) Biochem , vol.34 , pp. 1661-1668
    • Tierney, D.L.1    Fee, J.A.2    Ludwig, M.L.3    Penner-Hahn, J.E.4
  • 29
    • 0037051651 scopus 로고    scopus 로고
    • Second-sphere contributions to substrate-analogue binding in iron(III) superoxide dismutase
    • Xie, J., E. Yikilmaz, A.-F. Miller, and T. C. Brunold, 2002. Second-sphere contributions to substrate-analogue binding in iron(III) superoxide dismutase. J. Am. Chem. Soc., 124, 3769-3774.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 3769-3774
    • Xie, J.1    Yikilmaz, E.2    Miller, A.-F.3    Brunold, T.C.4
  • 30
    • 0037063508 scopus 로고    scopus 로고
    • Spectroscopic and computational studies on iron and manganese superoxide dismutases: Nature of the chemical events associated with active-site pKs
    • Jackson, T. A., J. Xie, E. Yikilmaz, A.-F. Miller, and T. C. Brunold, 2002. Spectroscopic and computational studies on iron and manganese superoxide dismutases: Nature of the chemical events associated with active-site pKs. J. Am. Chem. Soc., 124, 10833-10845.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 10833-10845
    • Jackson, T.A.1    Xie, J.2    Yikilmaz, E.3    Miller, A.-F.4    Brunold, T.C.5
  • 31
    • 0038682379 scopus 로고    scopus 로고
    • 7 system: Exploring the geometric and electronic structures of the nitrosyl adduct of iron superoxide dismutase
    • 7 system: exploring the geometric and electronic structures of the nitrosyl adduct of iron superoxide dismutase. J. Am. Chem. Soc., 125, 8348-8363.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 8348-8363
    • Jackson, T.A.1    Yikilmaz, E.2    Miller, A.-F.3    Brunold, T.C.4
  • 32
    • 0021774481 scopus 로고
    • Destruction of tryptophan residues by hydrogen peroxide in iron-containing superoxide dismutase
    • Yamakura, F. 1984. Destruction of tryptophan residues by hydrogen peroxide in iron-containing superoxide dismutase. Biochem. Biophys. Res. Commun., 122, 635-641.
    • (1984) Biochem. Biophys. Res. Commun , vol.122 , pp. 635-641
    • Yamakura, F.1
  • 33
    • 0023124274 scopus 로고
    • Effect of hydrogen peroxide on the iron-containing superoxide dismutase of Escherichia coli
    • Beyer, W. F. and I. Fridovich, 1987. Effect of hydrogen peroxide on the iron-containing superoxide dismutase of Escherichia coli. Biochem., 26, 1251-1257.
    • (1987) Biochem , vol.26 , pp. 1251-1257
    • Beyer, W.F.1    Fridovich, I.2
  • 34
    • 0030773529 scopus 로고    scopus 로고
    • A "thermophilic shift" in ligand interactions for Thermus thermophilus manganese superoxide dismutase
    • Whittaker, M. M. and J. W. Whittaker, 1997. A "thermophilic shift" in ligand interactions for Thermus thermophilus manganese superoxide dismutase. J. Biol. Inorg. Chem., 2, 667-671.
    • (1997) J. Biol. Inorg. Chem , vol.2 , pp. 667-671
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 35
    • 0029944136 scopus 로고    scopus 로고
    • Low-temperature thermochromism marks a change in coordination for the metal ion in manganese superoxide dismutase
    • Whittaker, M. M. and J. W. Whittaker, 1996. Low-temperature thermochromism marks a change in coordination for the metal ion in manganese superoxide dismutase. Biochem., 35, 6762-6770.
    • (1996) Biochem , vol.35 , pp. 6762-6770
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 36
    • 4644220652 scopus 로고    scopus 로고
    • Spectroscopic and computational studies of the azide-adduct of manganese superoxide dismutase: Definitive assignment of the ligand responsible for the low-temperature thermochromism
    • Jackson, T. A., A. Karapetian, A.-F. Miller, and T. C. Brunold, 2004. Spectroscopic and computational studies of the azide-adduct of manganese superoxide dismutase: Definitive assignment of the ligand responsible for the low-temperature thermochromism. J. Am. Chem. Soc., 126, 12477-12491.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 12477-12491
    • Jackson, T.A.1    Karapetian, A.2    Miller, A.-F.3    Brunold, T.C.4
  • 37
    • 32344438011 scopus 로고    scopus 로고
    • Effects of substrate analogues and pH on manganese superoxide dismutase
    • Tabares, L. C., N. Cortez, B. Y. Hiraoka, F. Yamakura, and S. Un, 2006. Effects of substrate analogues and pH on manganese superoxide dismutase. Biochem., 45, 1919-1929.
    • (2006) Biochem , vol.45 , pp. 1919-1929
    • Tabares, L.C.1    Cortez, N.2    Hiraoka, B.Y.3    Yamakura, F.4    Un, S.5
  • 38
    • 34547905430 scopus 로고    scopus 로고
    • Role of tyrosine-34 in the anion binding equilibria in manganese(II) superoxide dismutases
    • Tabares, L. C., N. Cortez, and S. Un, 2007. Role of tyrosine-34 in the anion binding equilibria in manganese(II) superoxide dismutases. Biochem., 46, 9320-9327.
    • (2007) Biochem , vol.46 , pp. 9320-9327
    • Tabares, L.C.1    Cortez, N.2    Un, S.3
  • 39
    • 0026067789 scopus 로고
    • In vivo competition between iron and manganese for occupancy of the active site region of the manganese-superoxide dismutase of Escherichia coli
    • Beyer, W. F. and I. Fridovich, 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.
    • (1991) J. Biol. Chem , vol.266 , pp. 303-308
    • Beyer, W.F.1    Fridovich, I.2
  • 40
    • 0017314966 scopus 로고
    • Superoxide dismutase: Reversible removal of manganese and its substitution by cobalt, nickel, or zinc
    • Ose, D. E. and I. Fridovich, 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
  • 41
    • 56849118117 scopus 로고    scopus 로고
    • NMR studies of proton donation and metal ion specificity in superoxide dismutase
    • Sorkin, D. L., C. K. Vance, and A.-F. Miller, 1996. NMR studies of proton donation and metal ion specificity in superoxide dismutase. Biophys. J., 70, MP365-MP365.
    • (1996) Biophys. J , vol.70
    • Sorkin, D.L.1    Vance, C.K.2    Miller, A.-F.3
  • 42
    • 0030860007 scopus 로고    scopus 로고
    • Mutagenesis of a proton link-age pathway in Escherichia coli manganese superoxide dismutase
    • Whittaker, M. M. and J. W. Whittaker, 1997. Mutagenesis of a proton link-age pathway in Escherichia coli manganese superoxide dismutase. Biochem., 36, 8923-8931.
    • (1997) Biochem , vol.36 , pp. 8923-8931
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 43
    • 43649098548 scopus 로고    scopus 로고
    • Redox tuning over almost 1V in a structurally conserved active site: Lessons from Fe-containing superoxide dismutase
    • Miller, A.-F. 2008. Redox tuning over almost 1V in a structurally conserved active site: Lessons from Fe-containing superoxide dismutase. Acc. Chem. Res., 41, 501-510.
    • (2008) Acc. Chem. Res , vol.41 , pp. 501-510
    • Miller, A.-F.1
  • 44
    • 0032573845 scopus 로고    scopus 로고
    • A simple proposal that can explain the inactivity of metal-substituted superoxide dismutases
    • Vance, C. K. and A.-F. Miller, 1998. A simple proposal that can explain the inactivity of metal-substituted superoxide dismutases. J. Am. Chem. Soc., 120, 461-467.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 461-467
    • Vance, C.K.1    Miller, A.-F.2
  • 45
    • 0034233378 scopus 로고    scopus 로고
    • Mutational and spectroscopic studies of the significance of the active site Gln to metal ion specificity in superoxide dismutase
    • Schwartz, A. L., E. Yikilmaz, C. K. Vance, S. Vathyam, and A.-F. Miller, 2000. Mutational and spectroscopic studies of the significance of the active site Gln to metal ion specificity in superoxide dismutase. J. Inorg. Biochem., 80, 247-256.
    • (2000) J. Inorg. Biochem , vol.80 , pp. 247-256
    • Schwartz, A.L.1    Yikilmaz, E.2    Vance, C.K.3    Vathyam, S.4    Miller, A.-F.5
  • 46
    • 0032560945 scopus 로고    scopus 로고
    • Distinct metal environment in Fe-substituted manganese superoxide dismutase provides a structural basis of metal specificity
    • Edwards, R. A., M. M. Whittaker, J. W. Whittaker, G. B. Jameson, and E. N. Baker, 1998. Distinct metal environment in Fe-substituted manganese superoxide dismutase provides a structural basis of metal specificity. J. Am. Chem. Soc., 120, 9684-9685.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 9684-9685
    • Edwards, R.A.1    Whittaker, M.M.2    Whittaker, J.W.3    Jameson, G.B.4    Baker, E.N.5
  • 47
    • 0037051599 scopus 로고    scopus 로고
    • Hydrogen-bond-mediated tuning of the redox potential of the non-heme Fe site of superoxide dismutase
    • Yikilmaz, E., J. Xie, T. C. Brunold, and A.-F. Miller, 2002. Hydrogen-bond-mediated tuning of the redox potential of the non-heme Fe site of superoxide dismutase. J. Am. Chem. Soc., 124, 3482-3483.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 3482-3483
    • Yikilmaz, E.1    Xie, J.2    Brunold, T.C.3    Miller, A.-F.4
  • 48
    • 0040186069 scopus 로고    scopus 로고
    • Multiple replacements of glutamine 143 in human manganese superoxide dismutase: Effects on structure, stability, and catalysis
    • Leveque, V. J. P., M. E. Stroupe, J. R. Lepock, D. E. Cabelli, J. A. Tainer, H. S. Nick, and D. N. Silverman, 2000. Multiple replacements of glutamine 143 in human manganese superoxide dismutase: Effects on structure, stability, and catalysis. Biochem., 39, 7131-7137.
    • (2000) Biochem , vol.39 , pp. 7131-7137
    • Leveque, V.J.P.1    Stroupe, M.E.2    Lepock, J.R.3    Cabelli, D.E.4    Tainer, J.A.5    Nick, H.S.6    Silverman, D.N.7
  • 51
    • 0035830385 scopus 로고    scopus 로고
    • Outer sphere mutations perturb metal reactivity in manganese superoxide dismutase
    • Edwards, R. A., M. M. Whittaker, J. W. Whittaker, E. N. Baker, and G. B. Jameson, 2001. Outer sphere mutations perturb metal reactivity in manganese superoxide dismutase. Biochem., 40, 15-27.
    • (2001) Biochem , vol.40 , pp. 15-27
    • Edwards, R.A.1    Whittaker, M.M.2    Whittaker, J.W.3    Baker, E.N.4    Jameson, G.B.5
  • 52
    • 0036428548 scopus 로고    scopus 로고
    • Thermostability of manganese- and iron-superoxide dismutases from Escherichia coli is determined by the characteristic position of a glutamine residue
    • Hunter, T., J. V. Bannister, and G. J. Hunter, 2002. Thermostability of manganese- and iron-superoxide dismutases from Escherichia coli is determined by the characteristic position of a glutamine residue. Eur. J. Biochem., 269, 5137-5148.
    • (2002) Eur. J. Biochem , vol.269 , pp. 5137-5148
    • Hunter, T.1    Bannister, J.V.2    Hunter, G.J.3
  • 53
    • 0034650220 scopus 로고    scopus 로고
    • A change of the metal-specific activity of a cambialistic superoxide dismutase from Porphyromonas gingivalis by a double mutation of Gln-70 to Gly and Ala-142 to Gln
    • Hiraoka, B. Y., F. Yamakura, S. Sugo, and K. Nakayama, 2000. A change of the metal-specific activity of a cambialistic superoxide dismutase from Porphyromonas gingivalis by a double mutation of Gln-70 to Gly and Ala-142 to Gln. Biochem. J., 345, 345-350.
    • (2000) Biochem. J , vol.345 , pp. 345-350
    • Hiraoka, B.Y.1    Yamakura, F.2    Sugo, S.3    Nakayama, K.4
  • 54
    • 0042820012 scopus 로고    scopus 로고
    • Pronounced conversion of the metal-specific activity of superoxide dismutase from Porphyromonas gingivalis by the mutation of a single amino acid (Gly155Thr) located apart from the active site
    • Yamakura, F., S. Sugio, B. Y. Hiraoka, D. Ohmori, and T. Yokota, 2003. Pronounced conversion of the metal-specific activity of superoxide dismutase from Porphyromonas gingivalis by the mutation of a single amino acid (Gly155Thr) located apart from the active site. Biochem., 42, 10790-10799.
    • (2003) Biochem , vol.42 , pp. 10790-10799
    • Yamakura, F.1    Sugio, S.2    Hiraoka, B.Y.3    Ohmori, D.4    Yokota, T.5
  • 57
    • 0023030627 scopus 로고
    • A Streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor
    • Martin, M. E., B. R. Byers, M. O. J. Olson, M. L. Salin, J. E. L. Aruneaux, and C. Tolbert, 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    Aruneaux, J.E.L.5    Tolbert, C.6
  • 58
    • 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., D. Barra, F. Bossa, L. Calabrese, and G. Rotilio, 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, 13977-13980.
    • (1982) J. Biol. Chem , vol.257 , pp. 13977-13980
    • Meier, B.1    Barra, D.2    Bossa, F.3    Calabrese, L.4    Rotilio, G.5
  • 59
    • 0025219013 scopus 로고
    • Characterization of superoxide dismutases purified from either anaerobically maintained or aerated Bacteroides gingivalis
    • Amano, A. S. S., H. Tamagawa, K. Iwakura, S. Tsunasawa, and A. Tsunemitsu, 1990. Characterization of superoxide dismutases purified from either anaerobically maintained or aerated Bacteroides gingivalis. J. Bacter., 172, 1457-1463.
    • (1990) J. Bacter , vol.172 , pp. 1457-1463
    • Amano, A.S.S.1    Tamagawa, H.2    Iwakura, K.3    Tsunasawa, S.4    Tsunemitsu, A.5
  • 60
    • 0033920250 scopus 로고    scopus 로고
    • Crystal structure of cambialistic superoxide dismutase from Porphyromonas gingivalis
    • Sugio, S., B. Y. Hiraoka, and F. Yamakura, 2000. Crystal structure of cambialistic superoxide dismutase from Porphyromonas gingivalis. Eur. J. Biochem., 267, 3487-3495.
    • (2000) Eur. J. Biochem , vol.267 , pp. 3487-3495
    • Sugio, S.1    Hiraoka, B.Y.2    Yamakura, F.3
  • 61
    • 0001122503 scopus 로고    scopus 로고
    • X-ray structure of the cambialistic superoxide dismutase from Propionibacterium shermanii active with Fe or Mn
    • Schmidt, M., B. Meier, and F. Parak, 1996. X-ray structure of the cambialistic superoxide dismutase from Propionibacterium shermanii active with Fe or 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
  • 62
    • 0028932184 scopus 로고
    • X-ray structure-analysis of the iron-dependent superoxide-dismutase from Mycobacterium-tuberculosis at 2.0 Åresolution reveals novel dimer-dimer interactions
    • Cooper, J. B., K. McIntyre, M. O. Badasso, S. P. Wood, Y. Zhang, T. R. Garbe, and D. Young, 1995. X-ray structure-analysis of the iron-dependent superoxide-dismutase from Mycobacterium-tuberculosis at 2.0 Åresolution reveals novel dimer-dimer interactions. J. Mol. Biol., 246, 531-544.
    • (1995) J. Mol. Biol , vol.246 , pp. 531-544
    • Cooper, J.B.1    McIntyre, K.2    Badasso, M.O.3    Wood, S.P.4    Zhang, Y.5    Garbe, T.R.6    Young, D.7
  • 63
    • 0033555252 scopus 로고    scopus 로고
    • Refined crystal structure of a superoxide dismutase from the hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2 Åresolution
    • Knapp, S., S. Kardinahl, N. Hellgren, G. Tibbelin, G. Schäfer, and R. Ladenstein. 1999. Refined crystal structure of a superoxide dismutase from the hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2 Åresolution. J. Mol. Biol., 285, 689-702.
    • (1999) J. Mol. Biol , vol.285 , pp. 689-702
    • Knapp, S.1    Kardinahl, S.2    Hellgren, N.3    Tibbelin, G.4    Schäfer, G.5    Ladenstein, R.6
  • 67
    • 0001479052 scopus 로고    scopus 로고
    • MCD C-term signs, saturation behavior, and determination of band polarizations in randomly oriented systems with spin S ≥ 1/2. Application to S = 1/2 and S = 5/2
    • Neese, F. and E. I. Solomon, 1999. MCD C-term signs, saturation behavior, and determination of band polarizations in randomly oriented systems with spin S ≥ 1/2. Application to S = 1/2 and S = 5/2. Inorg. Chem., 38, 1847-1865.
    • (1999) Inorg. Chem , vol.38 , pp. 1847-1865
    • Neese, F.1    Solomon, E.I.2
  • 69
    • 0344791553 scopus 로고
    • Approximate density functional theory as a practical tool in molecular energetics and dynamics
    • Ziegler, T. 1991. Approximate density functional theory as a practical tool in molecular energetics and dynamics. Chem. Rev., 91, 651-667.
    • (1991) Chem. Rev , vol.91 , pp. 651-667
    • Ziegler, T.1
  • 70
    • 0034314630 scopus 로고    scopus 로고
    • Theoretical methods for the description of the solvent effect in biomolecular systems
    • Orozco, M. and F. J. Luque, 2000. Theoretical methods for the description of the solvent effect in biomolecular systems. Chem. Rev., 100, 4187-4225.
    • (2000) Chem. Rev , vol.100 , pp. 4187-4225
    • Orozco, M.1    Luque, F.J.2
  • 71
    • 84986527758 scopus 로고
    • IMOMM: A new integrated ab initio + molecular mechanics geometry optimization scheme of equilibrium structures and ransition states
    • Maseras, R and K. Morokuma, 1995. IMOMM: A new integrated ab initio + molecular mechanics geometry optimization scheme of equilibrium structures and ransition states. J. Comput. Chem., 16, 1170-1179.
    • (1995) J. Comput. Chem , vol.16 , pp. 1170-1179
    • Maseras, R.1    Morokuma, K.2
  • 72
    • 0032509281 scopus 로고    scopus 로고
    • Implementation of the IMOMM methodology for performing combined QM/MM molecular dynamics simulations and frequency calculations
    • Woo, T. K., L. Cavallo, and T. Ziegler, 1998. Implementation of the IMOMM methodology for performing combined QM/MM molecular dynamics simulations and frequency calculations. Theor. Chem. Acc., 100, 307-313.
    • (1998) Theor. Chem. Acc , vol.100 , pp. 307-313
    • Woo, T.K.1    Cavallo, L.2    Ziegler, T.3
  • 74
    • 0041784950 scopus 로고    scopus 로고
    • MacKerell, A. D., D. Bashford, M. Bellott, R. L. Dunbrack, J. D. Evanseck, M. J. Field, S. Fischer, J. Gao, H. Guo, S. Ha, D. Joseph-McCarthy, L. Kuchnir, K. Kuczera, F. T. K. Lau, C. Mattos, S. Michnick, T. Ngo, D. T. Nguyen, B. Prodhom, W. E. Reiher, B. Roux, M. Schlenkrich, J. C. Smith, R. Stote, J. Straub, M. Watanabe, J. Wiorkiewicz-Kuczera, D. Yin, and M. Karplus, 1998. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B., 102, 3586-3616.
    • MacKerell, A. D., D. Bashford, M. Bellott, R. L. Dunbrack, J. D. Evanseck, M. J. Field, S. Fischer, J. Gao, H. Guo, S. Ha, D. Joseph-McCarthy, L. Kuchnir, K. Kuczera, F. T. K. Lau, C. Mattos, S. Michnick, T. Ngo, D. T. Nguyen, B. Prodhom, W. E. Reiher, B. Roux, M. Schlenkrich, J. C. Smith, R. Stote, J. Straub, M. Watanabe, J. Wiorkiewicz-Kuczera, D. Yin, and M. Karplus, 1998. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B., 102, 3586-3616.
  • 75
    • 33847086509 scopus 로고
    • An intermediate neglect of differential overlap technique for spectra of transition-metal complexes: Ferrocene
    • Zerner, M. C., G. H. Loew, R. F. Kirchner, and U. T. Mueller-Westerhof, 1980. An intermediate neglect of differential overlap technique for spectra of transition-metal complexes: Ferrocene. J. Am. Chem. Soc., 102, 589.
    • (1980) J. Am. Chem. Soc , vol.102 , pp. 589
    • Zerner, M.C.1    Loew, G.H.2    Kirchner, R.F.3    Mueller-Westerhof, U.T.4
  • 76
    • 84962449543 scopus 로고    scopus 로고
    • A critical evaluation of DFT, including time-dependent DFT, applied to bioinorganic chemistry
    • Neese, F. 2006. A critical evaluation of DFT, including time-dependent DFT, applied to bioinorganic chemistry. J. Biol. Inorg. Chem., 11, 702-711.
    • (2006) J. Biol. Inorg. Chem , vol.11 , pp. 702-711
    • Neese, F.1
  • 77
    • 84961980743 scopus 로고
    • COSMO: A new approach to dielectric screening in solvents with explicit expressions for the screening energy and its gradient
    • Klamt, A. and G. Schüürmann, 1993. COSMO: A new approach to dielectric screening in solvents with explicit expressions for the screening energy and its gradient. J. Chem. Soc., Perkin Trans., 2, 799-805.
    • (1993) J. Chem. Soc., Perkin Trans , vol.2 , pp. 799-805
    • Klamt, A.1    Schüürmann, G.2
  • 79
    • 0026612756 scopus 로고
    • Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin
    • Bashford, D. and K. Gerwert, 1992. Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin. J. Mol. Biol., 224, 473-486.
    • (1992) J. Mol. Biol , vol.224 , pp. 473-486
    • Bashford, D.1    Gerwert, K.2
  • 80
    • 33751159055 scopus 로고
    • Incorporating solvation effects into density functional electronic structure calculations
    • Chen, J. L., L. Noodleman, D. A. Case, and D. Bashford, 1994. Incorporating solvation effects into density functional electronic structure calculations. J. Phys. Chem., 98, 11059-11068.
    • (1994) J. Phys. Chem , vol.98 , pp. 11059-11068
    • Chen, J.L.1    Noodleman, L.2    Case, D.A.3    Bashford, D.4
  • 81
    • 33745727307 scopus 로고    scopus 로고
    • Structure of reduced and oxidized manganese superoxide dismutase: A combined computational and experimental approach
    • Rulíšek, L. and U. Ryde, 2006. Structure of reduced and oxidized manganese superoxide dismutase: A combined computational and experimental approach. J. Phys. Chem. B., 110, 11511-11518.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 11511-11518
    • Rulíšek, L.1    Ryde, U.2
  • 82
    • 43649099121 scopus 로고    scopus 로고
    • Spectroscopic and computational investigation of second-sphere contributions to redox tuning in Escherichia coli iron superoxide dismutase
    • Grove, L. E., J. Xie, E. Yikilmaz, A.-F. Miller, and T. C. Brunold, 2008. Spectroscopic and computational investigation of second-sphere contributions to redox tuning in Escherichia coli iron superoxide dismutase. Inorg. Chem., 47, 3978-3992.
    • (2008) Inorg. Chem , vol.47 , pp. 3978-3992
    • Grove, L.E.1    Xie, J.2    Yikilmaz, E.3    Miller, A.-F.4    Brunold, T.C.5
  • 83
    • 0037656286 scopus 로고    scopus 로고
    • Density functional methods applied to metalloenzymes
    • Lowell, T., F. Himo, W. G. Han, and L. Noodleman, 2003. Density functional methods applied to metalloenzymes. Coord. Chem. Rev., 238, 211-232.
    • (2003) Coord. Chem. Rev , vol.238 , pp. 211-232
    • Lowell, T.1    Himo, F.2    Han, W.G.3    Noodleman, L.4
  • 84
    • 84962463451 scopus 로고    scopus 로고
    • Calculation of redox potentials and pK(a) values of hydrated transition metal cations by a combined density functional and continuum dielectric theory
    • Li, J., C. L. Fisher, J. L. Chen, D. Bashford, and L. Noodleman, 1996. Calculation of redox potentials and pK(a) values of hydrated transition metal cations by a combined density functional and continuum dielectric theory. Inorg. Chem., 35, 4694-4702.
    • (1996) Inorg. Chem , vol.35 , pp. 4694-4702
    • Li, J.1    Fisher, C.L.2    Chen, J.L.3    Bashford, D.4    Noodleman, L.5
  • 85
    • 0001272489 scopus 로고    scopus 로고
    • Density-functional and electrostatic calculations for a model of a manganese Superoxide dismutase active site in aqueous solution
    • Fisher, C. L., J. L. Chen, X Li, D. Bashford, and L. Noodleman, 1996. Density-functional and electrostatic calculations for a model of a manganese Superoxide dismutase active site in aqueous solution. J. Phys. Chem., 100, 13498-13505.
    • (1996) J. Phys. Chem , vol.100 , pp. 13498-13505
    • Fisher, C.L.1    Chen, J.L.2    Li, X.3    Bashford, D.4    Noodleman, L.5
  • 86
    • 31544448000 scopus 로고    scopus 로고
    • The crucial importance of chemistry in the structure-function link: Manipulating hydrogen bonding in iron-containing superoxide dismutase
    • Yikilmaz, E., D. W. Rodgers, and A.-F. Miller, 2006. The crucial importance of chemistry in the structure-function link: Manipulating hydrogen bonding in iron-containing superoxide dismutase. Biochem., 45, 1151-1161.
    • (2006) Biochem , vol.45 , pp. 1151-1161
    • Yikilmaz, E.1    Rodgers, D.W.2    Miller, A.-F.3
  • 87
    • 0014691242 scopus 로고
    • Superoxide dismutase; an enzymic function for erythrocuprein (hemocuprein)
    • McCord, J. M. and I. Fridovich, 1969. Superoxide dismutase; an enzymic 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
  • 88
    • 56849130953 scopus 로고    scopus 로고
    • Consequences of the Q69H mutation in E. coli iron superoxide dismutase: Spectroscopic and computational insight into active site properties
    • in preparation
    • Grove, L. E., E. Yikilmaz, J. Xie, A.-F. Miller, and T. C. Brunold, 2008. Consequences of the Q69H mutation in E. coli iron superoxide dismutase: Spectroscopic and computational insight into active site properties. Biochemistry, in preparation.
    • (2008) Biochemistry
    • Grove, L.E.1    Yikilmaz, E.2    Xie, J.3    Miller, A.-F.4    Brunold, T.C.5
  • 89
    • 0032554625 scopus 로고    scopus 로고
    • Spectroscopic comparisons of the pH dependencies of Fe-substituted (Mn)superoxide dismutase and Fe-superoxide dismutase
    • Vance, C. K. and A.-F. Miller, 1998. Spectroscopic comparisons of the pH dependencies of Fe-substituted (Mn)superoxide dismutase and Fe-superoxide dismutase. Biochemistry, 37, 5518-5527.
    • (1998) Biochemistry , vol.37 , pp. 5518-5527
    • Vance, C.K.1    Miller, A.-F.2
  • 91
    • 0002215568 scopus 로고    scopus 로고
    • The structure of the azide coordinated superoxide dismutase of Propionibacterium shermanii investigated by X-ray structure analysis, extended X-ray absorption fine structure, Mössbauer and electron paramagnetic resonance spectroscopy
    • Schmidt, M., C. Scherk, O. Iakovleva, H. F. Nolting, B. Meier, and F. Parak, 1998. The structure of the azide coordinated superoxide dismutase of Propionibacterium shermanii investigated by X-ray structure analysis, extended X-ray absorption fine structure, Mössbauer and electron paramagnetic resonance spectroscopy. Inorg. Chim. Acta., 276, 65-72.
    • (1998) Inorg. Chim. Acta , vol.276 , pp. 65-72
    • Schmidt, M.1    Scherk, C.2    Iakovleva, O.3    Nolting, H.F.4    Meier, B.5    Parak, F.6


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