메뉴 건너뛰기




Volumn 275-276, Issue , 1998, Pages 65-72

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

Author keywords

Crystal structures; EXAFS; Superoxide dismutase

Indexed keywords

ABSORPTION SPECTRA; ATOMIC PHYSICS; CRYSTAL STRUCTURE; CRYSTAL SYMMETRY; CRYSTALS; ELECTRON RESONANCE; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYMES; EXTENDED X RAY ABSORPTION FINE STRUCTURE SPECTROSCOPY; IONIC STRENGTH; MOLECULES; PARAMAGNETIC RESONANCE; PARAMAGNETISM; X RAY ABSORPTION;

EID: 0002215568     PISSN: 00201693     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0020-1693(97)06061-1     Document Type: Article
Times cited : (12)

References (21)
  • 1
    • 0023030627 scopus 로고
    • A streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor
    • M.E. Martin, B.R. Byers, M.O.J. Olson, M.L. Salin, E.L. Arcenaeaux and C. Tolbert, A streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor, J. Biol. Chem., 261 (1986) 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    Arcenaeaux, E.L.5    Tolbert, C.6
  • 2
    • 0001122503 scopus 로고    scopus 로고
    • X-ray structure of the cambialistic superoxide dismutase from Propionibacterium shermanii active with Fe or Mn
    • M. Schmidt, B. Meier and F. Parak, X-ray structure of the cambialistic superoxide dismutase from Propionibacterium shermanii active with Fe or Mn, J. Biol. Inorg. Chem. (JBIC) 1 (1996) 532-541.
    • (1996) J. Biol. Inorg. Chem. (JBIC) , vol.1 , pp. 532-541
    • Schmidt, M.1    Meier, B.2    Parak, F.3
  • 3
    • 0029997688 scopus 로고    scopus 로고
    • EXAFS investigations of the active site of iron superoxide dismutase of Escherichia coli and Propionibacterium shermanii
    • C. Scherk, M. Schmidt, H.F. Nolting, B. Meier and F. Parak, EXAFS investigations of the active site of iron superoxide dismutase of Escherichia coli and Propionibacterium shermanii, Eur. Biophys. J., 24 (1996) 243-250.
    • (1996) Eur. Biophys. J. , vol.24 , pp. 243-250
    • Scherk, C.1    Schmidt, M.2    Nolting, H.F.3    Meier, B.4    Parak, F.5
  • 4
    • 0000625192 scopus 로고
    • Collaborative computational project, number 4
    • Collaborative computational project, number 4, Acta Crystallogr. Sect. D, 50 (1994) 760-763.
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
  • 5
    • 0004283186 scopus 로고
    • Yale University, New Haven, CT
    • A.T. Brünger, X-plor 3.1, Yale University, New Haven, CT, 1992.
    • (1992) X-plor 3.1
    • Brünger, A.T.1
  • 6
    • 0026597444 scopus 로고
    • The free R-value: A novel statistical quality for assessing the accuracy of crystal structures
    • A.T. Brünger, The free R-value: a novel statistical quality for assessing the accuracy of crystal structures, Nature, 335 (1992) 472-474.
    • (1992) Nature , vol.335 , pp. 472-474
    • Brünger, A.T.1
  • 9
    • 35949033161 scopus 로고
    • New method for the calculation of atomic phase shifts: Application to extended X-ray absorption fine structure (EXAFS) in molecules and crystals
    • P.A. Lee and G. Beni, New method for the calculation of atomic phase shifts: application to extended X-ray absorption fine structure (EXAFS) in molecules and crystals, Phys. Rev. B, 15 (1977) 2862-2883.
    • (1977) Phys. Rev. B , vol.15 , pp. 2862-2883
    • Lee, P.A.1    Beni, G.2
  • 10
    • 0001060218 scopus 로고
    • Spin-lattice relaxation in Mössbauer spectra of Fe(III) high spin complexes in an orthorhombic crystal field
    • O. Iakovleva, T. Rimke, B. Meier and F. Parak, Spin-lattice relaxation in Mössbauer spectra of Fe(III) high spin complexes in an orthorhombic crystal field, Hyperfine Int., 91 (1994) 879-883.
    • (1994) Hyperfine Int. , vol.91 , pp. 879-883
    • Iakovleva, O.1    Rimke, T.2    Meier, B.3    Parak, F.4
  • 11
    • 0028799032 scopus 로고
    • An interpretation of EPR spectra of azide ligated superoxide dismutase from Propionibacterium shermanii
    • O. Iakovleva, F. Parak, T. Rimke, B. Meier, J. Hüttermann and R. Kappl, An interpretation of EPR spectra of azide ligated superoxide dismutase from Propionibacterium shermanii, Eur. Biophys. J., 24 (1995) 65-68.
    • (1995) Eur. Biophys. J. , vol.24 , pp. 65-68
    • Iakovleva, O.1    Parak, F.2    Rimke, T.3    Meier, B.4    Hüttermann, J.5    Kappl, R.6
  • 15
    • 0002376131 scopus 로고
    • The electronic state of iron in some natural iron compounds: Determination by Mössbauer and ESR spectroscopy, struct
    • W.T. Oosterhuis, The electronic state of iron in some natural iron compounds: determination by Mössbauer and ESR spectroscopy, Struct. Bonding, 20 (1974) 59-99.
    • (1974) Bonding , vol.20 , pp. 59-99
    • Oosterhuis, W.T.1
  • 16
    • 0001637751 scopus 로고
    • Electronic state of the iron in enterobacterin using Mössbauer spectroscopy
    • K. Spartalian, W.T. Oosterhuis and J.B. Neilands, Electronic state of the iron in enterobacterin using Mössbauer spectroscopy, J. Chem. Phys., 62 (1975) 3538-3543.
    • (1975) J. Chem. Phys. , vol.62 , pp. 3538-3543
    • Spartalian, K.1    Oosterhuis, W.T.2    Neilands, J.B.3
  • 17
    • 0029129263 scopus 로고
    • Kinetic and spectroscopic studies on a superoxide dismutase from Propionibacterium shermanii which is active with iron or manganese: pH dependence
    • B. Meier, A.P. Sehn, C. Michel, M. Saran, J. Hüttermann, F. Parak and G. Rotilio, Kinetic and spectroscopic studies on a superoxide dismutase from Propionibacterium shermanii which is active with iron or manganese: pH dependence, Biochem. J., 310 (1995) 945-950.
    • (1995) Biochem. J. , vol.310 , pp. 945-950
    • Meier, B.1    Sehn, A.P.2    Michel, C.3    Saran, M.4    Hüttermann, J.5    Parak, F.6    Rotilio, G.7
  • 18
    • 0025606630 scopus 로고
    • The structure of iron superoxide dismutase from Pseudomonas ovalis complexed with the inhibitor azide
    • B.L. Stoddard, D. Ringe and G.A. Petsko, The structure of iron superoxide dismutase from Pseudomonas ovalis complexed with the inhibitor azide, Protein Eng., 4 (2) (1990) 113-119.
    • (1990) Protein Eng. , vol.4 , Issue.2 , pp. 113-119
    • Stoddard, B.L.1    Ringe, D.2    Petsko, G.A.3
  • 19
    • 0028933323 scopus 로고
    • Structure-function in Escherichia coli iron superoxide dismutase: Comparisons with manganese enzyme from Thermus thermophilus
    • M.S. Lah, M.M. Dixon, K.A. Pattridge, W.C. Stallings, J.A. Fee and M.L. Ludwig, Structure-function in Escherichia coli iron superoxide dismutase: comparisons with manganese enzyme from Thermus thermophilus, Biochemistry, 34 (1995) 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
  • 20
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • A. Jones, J.Y. Zou, S.W. Couran and M. Kielgaard, Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. Sect. A, 47 (1991) 110-119.
    • (1991) Acta Crystallogr. Sect. A , vol.47 , pp. 110-119
    • Jones, A.1    Zou, J.Y.2    Couran, S.W.3    Kielgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.