메뉴 건너뛰기




Volumn 5, Issue 3, 1997, Pages 371-379

A critical assessment of the evidence from XAFS and crystallography for the breakage of the imidazolate bridge during catalysis in CuZn superoxide dismutase

Author keywords

enzyme; EXAFS; superoxide dismutase; X ray absorption; X ray crystallography; XAFS

Indexed keywords


EID: 0031569326     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00194-9     Document Type: Article
Times cited : (72)

References (40)
  • 1
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide-dismutase gene are associated with familial amyotrophiclateral-sclerosis
    • Rosen, D.R., et al., & Brown, R.H. (1993). Mutations in Cu/Zn superoxide-dismutase gene are associated with familial amyotrophiclateral-sclerosis. Nature 362, 59-62.
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Brown, R.H.2
  • 2
    • 0027426169 scopus 로고
    • Amyotrophic-lateral-sclerosis and structural defects in Cu,Zn superoxide-dismutase
    • Deng, H.-X., et al., & Siddiqui, T. (1993). Amyotrophic-lateral-sclerosis and structural defects in Cu,Zn superoxide-dismutase. Science 261, 1047-1051.
    • (1993) Science , vol.261 , pp. 1047-1051
    • Deng, H.-X.1    Siddiqui, T.2
  • 3
    • 0015520578 scopus 로고
    • Studies of the metal sites of copper proteins: Symmetry of copper in bovine superoxide dismutase and its functional significance
    • Rotilio, G., Morpurgo, L., Giovagnoli, C., Calabrese, L. & Mondovi, B. (1972). Studies of the metal sites of copper proteins: symmetry of copper in bovine superoxide dismutase and its functional significance. Biochemistry 11, 2187-2192.
    • (1972) Biochemistry , vol.11 , pp. 2187-2192
    • Rotilio, G.1    Morpurgo, L.2    Giovagnoli, C.3    Calabrese, L.4    Mondovi, B.5
  • 4
    • 0015501473 scopus 로고
    • A direct demonstration of the catalytic action of bovine erythrocyte superoxide dismutase through the use of pulse radiolysis
    • Klug, D., Rabani, J. & Fridovih, I. (1972). A direct demonstration of the catalytic action of bovine erythrocyte superoxide dismutase through the use of pulse radiolysis. J. Biol. Chem. 247, 4839-4842.
    • (1972) J. Biol. Chem. , vol.247 , pp. 4839-4842
    • Klug, D.1    Rabani, J.2    Fridovih, I.3
  • 5
    • 0015982070 scopus 로고
    • The mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance
    • Fielden, E.M., et al., & Calabrese, L. (1974). The mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Biochem. J. 139, 49-60.
    • (1974) Biochem. J. , vol.139 , pp. 49-60
    • Fielden, E.M.1    Calabrese, L.2
  • 6
    • 0020374498 scopus 로고
    • Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutase
    • Tainer, J.A., Getzoff, E.D., Beem, K.M., Richardson, J.S. & Richardson, D.C. (1982). Determination and analysis of the 2 Å structure of 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
  • 7
    • 0021081808 scopus 로고
    • Structure and mechanism of copper, zinc superoxide dismutase
    • Tainer, J.A., Getzoff, E.D., Richardson, J.S. & Richardson, D.C. (1983). Structure and mechanism of copper, zinc superoxide dismutase. Nature 306, 284-287.
    • (1983) Nature , vol.306 , pp. 284-287
    • Tainer, J.A.1    Getzoff, E.D.2    Richardson, J.S.3    Richardson, D.C.4
  • 8
    • 0026021532 scopus 로고
    • Three-dimensional structure of Cu,Zn superoxide dismutase from spinach at 2.0 Å resolution
    • Tokyo
    • Kitagawa, Y., et al., & Morita, Y. (1991). Three-dimensional structure of Cu,Zn superoxide dismutase from spinach at 2.0 Å resolution. J. Biochem. (Tokyo) 109, 447-485.
    • (1991) J. Biochem. , vol.109 , pp. 447-485
    • Kitagawa, Y.1    Morita, Y.2
  • 9
    • 0026715882 scopus 로고
    • Crystal structure of yeast Cu,Zn superoxide dismutase: Crystallographic refinement at 2.5 Å resolution
    • Djinovic, K., et al., & Bolognesi, M. (1992). Crystal structure of yeast Cu,Zn superoxide dismutase: crystallographic refinement at 2.5 Å resolution. J. Mol. Biol. 225, 791-809.
    • (1992) J. Mol. Biol. , vol.225 , pp. 791-809
    • Djinovic, K.1    Bolognesi, M.2
  • 10
    • 0026711256 scopus 로고
    • Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase
    • Parge, H.E., Hallewell, R.A. & Tainer, J.A. (1992). Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase. Proc. Natl. Acad. Sci. USA 89, 6109-6113.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6109-6113
    • Parge, H.E.1    Hallewell, R.A.2    Tainer, J.A.3
  • 11
    • 0028301573 scopus 로고
    • Crystal structure of the cyanide inhibited Xenopus laevis Cu,Zn superoxide dismutase at 98K
    • Carugo, K.D., et al., & Bolognesi, M. (1994). Crystal structure of the cyanide inhibited Xenopus laevis Cu,Zn superoxide dismutase at 98K. FEBS Lett. 349, 93-98.
    • (1994) FEBS Lett. , vol.349 , pp. 93-98
    • Carugo, K.D.1    Bolognesi, M.2
  • 12
    • 0017875552 scopus 로고
    • Superoxide dismutase, a study of the electronic properties of the copper and zinc by X-ray absorption spectroscopy
    • Blumberg, W.E., Peisach, J., Eisenberger, P. & Fee, J.A. (1978). Superoxide dismutase, a study of the electronic properties of the copper and zinc by X-ray absorption spectroscopy. Biochemistry 17, 1842-1846.
    • (1978) Biochemistry , vol.17 , pp. 1842-1846
    • Blumberg, W.E.1    Peisach, J.2    Eisenberger, P.3    Fee, J.A.4
  • 13
    • 0020824247 scopus 로고
    • An extended X-ray absorption-fine-structure study of the copper and zinc sites of freeze-dried bovine superoxide dismutase
    • Blackburn, N.J., Hasnain, S.S., Diakun, G.P., Knowles, P.F., Binsted, N. & Garner, C.D. (1983). An extended X-ray absorption-fine-structure study of the copper and zinc sites of freeze-dried bovine superoxide dismutase. Biochem. J. 213, 765-768.
    • (1983) Biochem. J. , vol.213 , pp. 765-768
    • Blackburn, N.J.1    Hasnain, S.S.2    Diakun, G.P.3    Knowles, P.F.4    Binsted, N.5    Garner, C.D.6
  • 14
    • 0021426764 scopus 로고
    • An extended X-ray absorption fine structure study of bovine erythrocyte superoxide dismutase in aqueous solution
    • Blackburn, N.J., Hasnain, S.S., Binsted, N., Diakun, G.P., Garner, C.D. & Knowles, P.F. (1984). An extended X-ray absorption fine structure study of bovine erythrocyte superoxide dismutase in aqueous solution. Biochem. J. 219, 985-990.
    • (1984) Biochem. J. , vol.219 , pp. 985-990
    • Blackburn, N.J.1    Hasnain, S.S.2    Binsted, N.3    Diakun, G.P.4    Garner, C.D.5    Knowles, P.F.6
  • 15
    • 0023619853 scopus 로고
    • Anion binding to bovine erythrocyte superoxide dismutase studied by X-ray absorption spectroscopy. A detailed structural analysis of the native enzyme and the azido and cyano derivatives using a multiple scattering approach
    • Blackburn, N.J., Strange, R.W., McFadden, L.M. & Hasnain, S.S. (1987). Anion binding to bovine erythrocyte superoxide dismutase studied by X-ray absorption spectroscopy. A detailed structural analysis of the native enzyme and the azido and cyano derivatives using a multiple scattering approach. J. Am. Chem. Soc. 109, 7162-7170.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 7162-7170
    • Blackburn, N.J.1    Strange, R.W.2    McFadden, L.M.3    Hasnain, S.S.4
  • 16
    • 0030040864 scopus 로고    scopus 로고
    • Three-dimensional structure of Xenopus laevis Cu,Zn superoxide dismutase b determined by X-ray crystallography at 1.5 Å resolution
    • Djinovic-Carugo, K., et al., & Bolognesi, M. (1996). Three-dimensional structure of Xenopus laevis Cu,Zn superoxide dismutase b determined by X-ray crystallography at 1.5 Å resolution. Acta Cryst. D 52, 176-188.
    • (1996) Acta Cryst. D , vol.52 , pp. 176-188
    • Djinovic-Carugo, K.1    Bolognesi, M.2
  • 17
    • 0021491550 scopus 로고
    • On the mechanism of superoxide dismutase: A theoretical study
    • Osman, R. & Basch, H. (1984). On the mechanism of superoxide dismutase: a theoretical study. J. Am. Chem. Soc. 106, 5710-5714.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 5710-5714
    • Osman, R.1    Basch, H.2
  • 18
    • 0007304755 scopus 로고
    • Ab initio calculations of the Cu(II)-O2(-) interaction as a model for the mechanism of copper/zinc superoxide dismutase
    • Rosi, M., Sgamellotti, A., Tarantelli, F., Bertini, I. & Luchinat, C. (1986). Ab initio calculations of the Cu(II)-O2(-) interaction as a model for the mechanism of copper/zinc superoxide dismutase. Inorg. Chem. 25, 1005-1008.
    • (1986) Inorg. Chem. , vol.25 , pp. 1005-1008
    • Rosi, M.1    Sgamellotti, A.2    Tarantelli, F.3    Bertini, I.4    Luchinat, C.5
  • 19
    • 0000136590 scopus 로고
    • Electronic structure of the Cu,Zn superoxide dismutase active site and its interactions with the substrate
    • Carloni, P., Blöchl, P.E. & Parrinello, M. (1994). Electronic structure of the Cu,Zn superoxide dismutase active site and its interactions with the substrate. J. Phys. Chem. 99, 1338-1348.
    • (1994) J. Phys. Chem. , vol.99 , pp. 1338-1348
    • Carloni, P.1    Blöchl, P.E.2    Parrinello, M.3
  • 20
    • 0022918523 scopus 로고
    • Steady-state kinetic studies of superoxide dismutase
    • Fee, J.A. & Bull, C. (1986). Steady-state kinetic studies of superoxide dismutase. J. Biol. Chem. 261, 13000-13005.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13000-13005
    • Fee, J.A.1    Bull, C.2
  • 21
    • 0028111860 scopus 로고
    • X-ray, NMR and molecular dynamics studies on reduced bovine superoxide dismutase: Implications for the mechanism
    • Banci, L., et al., & Wilson, K.S. (1994). X-ray, NMR and molecular dynamics studies on reduced bovine superoxide dismutase: implications for the mechanism. Biochem. Biophys. Res. Commun. 202, 1088-1095.
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 1088-1095
    • Banci, L.1    Wilson, K.S.2
  • 22
    • 0029152034 scopus 로고
    • Crystal structure of reduced bovine erythrocyte superoxide dismutase at 1.9 Å resolution
    • Rypniewski, W.R., Mangani, S., Bruni, B., Orioli, P.L., Casati, M. & Wilson, K.S. (1995). Crystal structure of reduced bovine erythrocyte superoxide dismutase at 1.9 Å resolution. J. Mol. Biol. 251, 282-296.
    • (1995) J. Mol. Biol. , vol.251 , pp. 282-296
    • Rypniewski, W.R.1    Mangani, S.2    Bruni, B.3    Orioli, P.L.4    Casati, M.5    Wilson, K.S.6
  • 23
    • 13344285361 scopus 로고    scopus 로고
    • Unusual trigonal-planar configuration revealed in the atomic structure of yeast copper-zinc superoxide dismutase
    • Ogihara, N., et al., & Tanier, J.A. (1996). Unusual trigonal-planar configuration revealed in the atomic structure of yeast copper-zinc superoxide dismutase. Biochemistry 35, 2316-2321.
    • (1996) Biochemistry , vol.35 , pp. 2316-2321
    • Ogihara, N.1    Tanier, J.A.2
  • 24
    • 35548993600 scopus 로고
    • A rapid, exact curved-wave theory for EXAFS calculations
    • Gurman, S.J., Binsted, N. & Ross, I. (1984). A rapid, exact curved-wave theory for EXAFS calculations. J. Phys. C. 17, 143-151.
    • (1984) J. Phys. C. , vol.17 , pp. 143-151
    • Gurman, S.J.1    Binsted, N.2    Ross, I.3
  • 25
    • 33744602646 scopus 로고
    • A rapid, exact curved-wave theory for EXAFS calculations: II. The multiple scattering contributions
    • Gurman, S.J., Binsted, N. & Ross, I. (1986). A rapid, exact curved-wave theory for EXAFS calculations: II. The multiple scattering contributions. J. Phys. C. 19, 1845-1861.
    • (1986) J. Phys. C. , vol.19 , pp. 1845-1861
    • Gurman, S.J.1    Binsted, N.2    Ross, I.3
  • 26
    • 0026620970 scopus 로고
    • Constrained and restrained refinement in EXAFS data analysis with curved wave theory
    • Binsted, N., Strange, R.W. & Hasnain, S.S. (1992). Constrained and restrained refinement in EXAFS data analysis with curved wave theory. Biochemistry 31, 12117-12125.
    • (1992) Biochemistry , vol.31 , pp. 12117-12125
    • Binsted, N.1    Strange, R.W.2    Hasnain, S.S.3
  • 27
    • 0000695469 scopus 로고
    • X-ray absorption spectroscopy of metal-histidine coordination in metalloproteins. Exact simulation of the EXAFS of tetrakis(imidazole)copper(II) nitrate and other copper-imidazole complexes by the use of a multiple scattering treatment
    • Strange, R.W., Blackburn, N.J., Knowles, P.F. & Hasnain, S.S. (1987). X-ray absorption spectroscopy of metal-histidine coordination in metalloproteins. Exact simulation of the EXAFS of tetrakis(imidazole)copper(II) nitrate and other copper-imidazole complexes by the use of a multiple scattering treatment. J. Am. Chem. Soc. 109, 7157-7162.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 7157-7162
    • Strange, R.W.1    Blackburn, N.J.2    Knowles, P.F.3    Hasnain, S.S.4
  • 28
    • 33845283452 scopus 로고
    • X-ray absorption edge determination of the oxidation state and coordination number: Application to the type 3 Cu site in Rhus vernicefera laccase and its reaction with oxygen
    • Kau, L., Spira-Solomon, D., Penner-Hahn, J.E., Hodgson, K.O. & Solomon, E.I. (1987). X-ray absorption edge determination of the oxidation state and coordination number: application to the type 3 Cu site in Rhus vernicefera laccase and its reaction with oxygen. J. Am. Chem. Soc. 109, 6433-6442.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 6433-6442
    • Kau, L.1    Spira-Solomon, D.2    Penner-Hahn, J.E.3    Hodgson, K.O.4    Solomon, E.I.5
  • 29
    • 0001369913 scopus 로고
    • X-ray absorption edge spectroscopy of copper(I) complexes. Coordination geometry of copper(I) in reduced forms of copper proteins and their derivatives with carbon monoxide
    • Blackburn, N.J., et al., & Zubieta, J. (1989). X-ray absorption edge spectroscopy of copper(I) complexes. Coordination geometry of copper(I) in reduced forms of copper proteins and their derivatives with carbon monoxide, Inorg. Chem. 28, 1349-1357.
    • (1989) Inorg. Chem. , vol.28 , pp. 1349-1357
    • Blackburn, N.J.1    Zubieta, J.2
  • 30
    • 4243983807 scopus 로고
    • Bond valence parameters obtained from a systematic analysis of the inorganic crystal structure database
    • Brown, I.D. & Altermatt, D. (1985). Bond valence parameters obtained from a systematic analysis of the inorganic crystal structure database. Acta Cryst. B 41, 244-247.
    • (1985) Acta Cryst. B , vol.41 , pp. 244-247
    • Brown, I.D.1    Altermatt, D.2
  • 31
    • 84872498969 scopus 로고
    • Chemical and steric constraints in inorganic solids
    • Brown, I.D. (1992). Chemical and steric constraints in inorganic solids. Acta Cryst. B 48, 553-572.
    • (1992) Acta Cryst. B , vol.48 , pp. 553-572
    • Brown, I.D.1
  • 32
    • 0000774586 scopus 로고
    • Bond valence sum analysis of metal-ligand bond lengths in metalloenzymes and model complexes
    • Thorp, H.H. (1992). Bond valence sum analysis of metal-ligand bond lengths in metalloenzymes and model complexes, Inorg. Chem. 31, 1585-1588.
    • (1992) Inorg. Chem. , vol.31 , pp. 1585-1588
    • Thorp, H.H.1
  • 33
    • 2542607780 scopus 로고    scopus 로고
    • VALENCE: A program for calculating bond valences
    • Brown, I.D. (1996). VALENCE: a program for calculating bond valences. J. Appl. Cryst. 29, 479-480.
    • (1996) J. Appl. Cryst. , vol.29 , pp. 479-480
    • Brown, I.D.1
  • 34
    • 0027995833 scopus 로고
    • Accuracy and precision in protein crystal structure analysis: Two independent refinements of the structure of poplar plastocyanin at 173K
    • Fields, B., Bartsch, H.H., Bartunik, H.D., Cordes, F., Guss, J.M. & Freeman, H.C. (1994). Accuracy and precision in protein crystal structure analysis: two independent refinements of the structure of poplar plastocyanin at 173K. Acta Cryst. D 50, 709-730.
    • (1994) Acta Cryst. D , vol.50 , pp. 709-730
    • Fields, B.1    Bartsch, H.H.2    Bartunik, H.D.3    Cordes, F.4    Guss, J.M.5    Freeman, H.C.6
  • 36
    • 33745231055 scopus 로고
    • Tables of bond lengths determined by X-ray and neutron diffraction. Part 2. Organometallic compounds and coordination complexes of the d- and f-block metals
    • Orpen, A.G., Brammer, L., Allen, F.H., Kennard, O., Watson, D.G. & Taylor, R. (1989). Tables of bond lengths determined by X-ray and neutron diffraction. Part 2. Organometallic compounds and coordination complexes of the d- and f-block metals. J. Chem. Soc. Dalton Trans. Supplement S1-S83.
    • (1989) J. Chem. Soc. Dalton Trans. , Issue.SUPPL.
    • Orpen, A.G.1    Brammer, L.2    Allen, F.H.3    Kennard, O.4    Watson, D.G.5    Taylor, R.6
  • 37
    • 0042838464 scopus 로고
    • 3D search and research using the Cambridge structural database
    • Allan, F.H. & Kennard, O. (1993). 3D search and research using the Cambridge structural database. Chemical Design Automation News 8, 130-137.
    • (1993) Chemical Design Automation News , vol.8 , pp. 130-137
    • Allan, F.H.1    Kennard, O.2
  • 39
    • 0028964815 scopus 로고
    • Structural and spectroscopic studies of the copper site of Stellacyanin
    • Strange, R.W., Reinhammar, B., Murphy, L.M. & Hasnain, S.S. (1995). Structural and spectroscopic studies of the copper site of Stellacyanin. Biochemistry 34, 220-231.
    • (1995) Biochemistry , vol.34 , pp. 220-231
    • Strange, R.W.1    Reinhammar, B.2    Murphy, L.M.3    Hasnain, S.S.4
  • 40
    • 0017411710 scopus 로고
    • The Protein Data Bank: A computer based archival file for macromolecular structures
    • Bernstein, F.C., et al., & Tasumi, M. (1977). The Protein Data Bank: a computer based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542.
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Bernstein, F.C.1    Tasumi, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.