메뉴 건너뛰기




Volumn 54, Issue 6, 1999, Pages 491-504

Enzyme mimics complexing Cu(II) ion: Structure-function relationships

Author keywords

Copper proteins; Kinetics; Mimics; Molecular modeling; NMR; Peptide design

Indexed keywords

CHELATE; COPPER COMPLEX; COPPER ZINC SUPEROXIDE DISMUTASE;

EID: 0032760041     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.1999.00139.x     Document Type: Article
Times cited : (8)

References (51)
  • 1
    • 0002190643 scopus 로고
    • General properties and biological functions of oxygenases
    • (Hayaishi, O., ed.). Academic Press, New York
    • Hayaishi, O. (1974) General properties and biological functions of oxygenases. In Molecular Mechanism of Oxygen Activation (Hayaishi, O., ed.). Academic Press, New York pp. 1-28.
    • (1974) Molecular Mechanism of Oxygen Activation , pp. 1-28
    • Hayaishi, O.1
  • 2
    • 0000211392 scopus 로고
    • Plastocyanin and the blu copper proteins
    • (Clarke M.J., Goodenough, J.B., Jørgensen C.K., et al., eds). Springer-Verlag Berlin
    • Sykes, A.G. (1991) Plastocyanin and the blu copper proteins. In Long Range Electron Transfer in Biology. Structure and Bonding 75 (Clarke M.J., Goodenough, J.B., Jørgensen C.K., et al., eds). Springer-Verlag Berlin, pp. 175-224.
    • (1991) Long Range Electron Transfer in Biology. Structure and Bonding 75 , pp. 175-224
    • Sykes, A.G.1
  • 3
    • 0000933501 scopus 로고
    • Superoxide radical and superoxide dismutase
    • Fridovich, I. (1972) Superoxide radical and superoxide dismutase. Acc. Chem. Res. 5, 321-326.
    • (1972) Acc. Chem. Res. , vol.5 , pp. 321-326
    • Fridovich, I.1
  • 4
    • 0024249184 scopus 로고
    • Design of peptides and proteins
    • De Grado, W.F. (1989) Design of peptides and proteins. Adv. Prot. Chem. 39, 51-124.
    • (1989) Adv. Prot. Chem. , vol.39 , pp. 51-124
    • De Grado, W.F.1
  • 6
    • 0019322337 scopus 로고
    • Modeling coordination sites in metallobiomolecules
    • Ibers, J.A. & Holm, R.H. (1980) Modeling coordination sites in metallobiomolecules. Science 209, 223-235.
    • (1980) Science , vol.209 , pp. 223-235
    • Ibers, J.A.1    Holm, R.H.2
  • 7
    • 0000316697 scopus 로고    scopus 로고
    • Ascorbate oxidation catalyzed by his (histidine) copper (II)
    • Scarpa, M., Vianello, F., Signor, L., Zennaro, L. & Rigo, A. (1996) Ascorbate oxidation catalyzed by his (histidine) copper (II). Inorg. Chem. 35, 5201-5206.
    • (1996) Inorg. Chem. , vol.35 , pp. 5201-5206
    • Scarpa, M.1    Vianello, F.2    Signor, L.3    Zennaro, L.4    Rigo, A.5
  • 8
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • Fields, G.B. & Noble, R.L. (1990) Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Peptide Prot. Res. 35, 161-214.
    • (1990) Int. J. Peptide Prot. Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 10
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler, L. & Ernst, R.R. (1983) Coherence transfer by isotropic mixing: application to proton correlation spectroscopy. J. Magn. Reson. 53, 521-528.
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 12
  • 13
    • 0017392955 scopus 로고
    • Simultaneous determination of superoxide dismutase and catalase in biological materials by polarography
    • Rigo, A. & Rotilio, G. (1977) Simultaneous determination of superoxide dismutase and catalase in biological materials by polarography. Anal. Biochem. 81, 157-166.
    • (1977) Anal. Biochem. , vol.81 , pp. 157-166
    • Rigo, A.1    Rotilio, G.2
  • 15
    • 0001849379 scopus 로고
    • Complexes of α-amino acids with chelatable side chain donor atoms
    • (Siegel, H., ed.). Marcel Dekker Inc, New York
    • Martin, B. (1979) Complexes of α-amino acids with chelatable side chain donor atoms. In Metal Ions in Biological Systems Vol. 9 (Siegel, H., ed.). Marcel Dekker Inc, New York pp. 1-39.
    • (1979) Metal Ions in Biological Systems , vol.9 , pp. 1-39
    • Martin, B.1
  • 16
    • 0026410002 scopus 로고
    • Structural aspects of metal liganding to functional groups in proteins
    • Glusker, J. (1991) Structural aspects of metal liganding to functional groups in proteins. Adv. Prot. Chem. 42, 1-76.
    • (1991) Adv. Prot. Chem. , vol.42 , pp. 1-76
    • Glusker, J.1
  • 17
  • 18
    • 0024961798 scopus 로고
    • Refined crystal structure of ascorbate oxidase at 1.9 Å resolution
    • Masserschmidt, A., Rossi, A., Ladenstein, R. et al. (1989) Refined crystal structure of ascorbate oxidase at 1.9 Å resolution. J. Mol. Biol. 206, 513-529.
    • (1989) J. Mol. Biol. , vol.206 , pp. 513-529
    • Masserschmidt, A.1    Rossi, A.2    Ladenstein, R.3
  • 19
    • 0024975122 scopus 로고
    • Pseudo 2-fold symmetry in the copper-binding domain of arthropodan haemocyanins
    • Volbeda, A. & Hol, W. G. J. (1989) Pseudo 2-fold symmetry in the copper-binding domain of arthropodan haemocyanins. J. Mol. Biol. 209, 249-279.
    • (1989) J. Mol. Biol. , vol.209 , pp. 249-279
    • Volbeda, A.1    Hol, W.G.J.2
  • 20
    • 0026736225 scopus 로고
    • Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases
    • Bode, W., Gomis-Rüth, F.X., Huber, R., Zwilling, R. & Stöcker, W. (1992) Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases. Nature 358, 164-167.
    • (1992) Nature , vol.358 , pp. 164-167
    • Bode, W.1    Gomis-Rüth, F.X.2    Huber, R.3    Zwilling, R.4    Stöcker, W.5
  • 21
    • 0029016430 scopus 로고
    • Protein design: Novel metal-binding sites
    • Regan, L. (1995) Protein design: novel metal-binding sites. Trends. Biochem. Sci. 20, 280-285.
    • (1995) Trends. Biochem. Sci. , vol.20 , pp. 280-285
    • Regan, L.1
  • 22
    • 0023673238 scopus 로고
    • Proposed structure for the zinc-binding domains from transcription factor IIIA and related proteins
    • Berg, J.M. (1988) Proposed structure for the zinc-binding domains from transcription factor IIIA and related proteins. Proc. Natl. Acad. Sci. USA 85, 99-102.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 99-102
    • Berg, J.M.1
  • 24
    • 0031891742 scopus 로고    scopus 로고
    • Alzheimer's beta-amyloid peptide: Affinity for metal chelates
    • Balakrishnan, R., Parthasarathy, R. & Sulkowski, E. (1998) Alzheimer's beta-amyloid peptide: affinity for metal chelates. J. Pept. Res. 51, 91-95.
    • (1998) J. Pept. Res. , vol.51 , pp. 91-95
    • Balakrishnan, R.1    Parthasarathy, R.2    Sulkowski, E.3
  • 25
    • 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
  • 26
    • 0028258569 scopus 로고
    • Electrostatic control of oxidative deamination catalysed by bovine serum amine oxidase
    • Stevanato, R., Mondovi', B., Befani, O., Scarpa, M. & Rigo, A. (1994) Electrostatic control of oxidative deamination catalysed by bovine serum amine oxidase. Biochem. J. 299, 317-320.
    • (1994) Biochem. J. , vol.299 , pp. 317-320
    • Stevanato, R.1    Mondovi', B.2    Befani, O.3    Scarpa, M.4    Rigo, A.5
  • 28
    • 0023122030 scopus 로고
    • Tests of the helix dipole model for stabilization of alpha-helices
    • Shoemaker, K.R., Kim, P.S., York, E.J., Stewart, J.M. & Baldwin, R.L. (1987) Tests of the helix dipole model for stabilization of alpha-helices. Nature 326, 563-567.
    • (1987) Nature , vol.326 , pp. 563-567
    • Shoemaker, K.R.1    Kim, P.S.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 29
    • 0009549839 scopus 로고
    • Predominant scalar interactions in selective broadening of ligand nuclear magnetic resonances by copper (II) ions
    • Espersen, G.W. & Martin, R.B. (1976) Predominant scalar interactions in selective broadening of ligand nuclear magnetic resonances by copper (II) ions. J. Am. Chem. Soc. 98, 40-44.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 40-44
    • Espersen, G.W.1    Martin, R.B.2
  • 30
    • 0018365329 scopus 로고
    • Nuclear magnetic relaxation of fluorine-19 as a novel assay method of superoxide dismutase
    • Rigo, A., Viglino, P., Argese, E., Terenzi, M. & Rotilio, G. (1979). Nuclear magnetic relaxation of fluorine-19 as a novel assay method of superoxide dismutase. J. Biol. Chem. 254, 1759-1760.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1759-1760
    • Rigo, A.1    Viglino, P.2    Argese, E.3    Terenzi, M.4    Rotilio, G.5
  • 35
    • 0017133724 scopus 로고
    • Evidence for a coordination position available to solute molecules on one of the metals at the active center of reduced bovine superoxide dismuatse
    • Fee, J.A. & Ward, R.L. (1976) Evidence for a coordination position available to solute molecules on one of the metals at the active center of reduced bovine superoxide dismuatse. Biochem. Biophys. Res. Commun. 71, 427-437.
    • (1976) Biochem. Biophys. Res. Commun. , vol.71 , pp. 427-437
    • Fee, J.A.1    Ward, R.L.2
  • 38
    • 0016260535 scopus 로고
    • Interactions of histidine and other imidazole derivatives with transition metal ions in chemical and biological systems
    • Sundberg, R.J. & Martin, R.B. (1974) Interactions of histidine and other imidazole derivatives with transition metal ions in chemical and biological systems. Chem. Rev. 74, 471-515.
    • (1974) Chem. Rev. , vol.74 , pp. 471-515
    • Sundberg, R.J.1    Martin, R.B.2
  • 39
    • 0016369980 scopus 로고
    • Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins
    • Peisach, J. & Blumberg, W. (1974) Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins. Arch. Biochem. Biophys. 165, 691-708.
    • (1974) Arch. Biochem. Biophys. , vol.165 , pp. 691-708
    • Peisach, J.1    Blumberg, W.2
  • 40
    • 0001367142 scopus 로고
    • Copper (II) complexing of Glycyl-L-histidine, Glycyl-L-histidylglycine, and Glycylglycyl-L-histidine in aqueous solution
    • Aiba, H., Yokoyama, A. & Tanaka, H. (1974) Copper (II) complexing of Glycyl-L-histidine, Glycyl-L-histidylglycine, and Glycylglycyl-L-histidine in aqueous solution. Bull. Chem. Soc. Jpn. 47, 1437-1441.
    • (1974) Bull. Chem. Soc. Jpn. , vol.47 , pp. 1437-1441
    • Aiba, H.1    Yokoyama, A.2    Tanaka, H.3
  • 41
    • 0001568320 scopus 로고
    • Force field calculations on the structures of transition metal complexes. 1. Application to copper (II) complexes in square-planar coordination
    • Wiesemann, F., Teipel, S., Krebs, B. & Hoeweler, U. (1994) Force field calculations on the structures of transition metal complexes. 1. Application to copper (II) complexes in square-planar coordination. Inorg. Chem. 33, 1891-1898.
    • (1994) Inorg. Chem. , vol.33 , pp. 1891-1898
    • Wiesemann, F.1    Teipel, S.2    Krebs, B.3    Hoeweler, U.4
  • 42
    • 0001224686 scopus 로고
    • In vacuo and in crystal molecular-mechanical modeling of copper (II) complexes with amino acids
    • Sabolovic, J. & Rasmussen, K. (1995) In vacuo and in crystal molecular-mechanical modeling of copper (II) complexes with amino acids. Inorg. Chem. 34, 1221-1232.
    • (1995) Inorg. Chem. , vol.34 , pp. 1221-1232
    • Sabolovic, J.1    Rasmussen, K.2
  • 43
    • 0000911032 scopus 로고
    • Chelates of ascorbic acid. Formation and catalytic properties
    • (Seib, P. & Tolbert, B., eds.), Adv. Chem. Ser. 200. American Chemical Society, Washington DC
    • Martell, A.E. (1982) Chelates of ascorbic acid. Formation and catalytic properties. In Axcorbic Acid: Chemistry, Metabolism and Uses (Seib, P. & Tolbert, B., eds.), Adv. Chem. Ser. 200. American Chemical Society, Washington DC, pp. 153-178
    • (1982) Axcorbic Acid: Chemistry, Metabolism and Uses , pp. 153-178
    • Martell, A.E.1
  • 44
    • 0020546431 scopus 로고
    • Superoxide ion as active intermediate in the autoxidation of ascorbate by molecular oxygen
    • Scarpa, M., Stevanato, R., Viglino, P. & Rigo, A. (1983) Superoxide ion as active intermediate in the autoxidation of ascorbate by molecular oxygen. J. Biol. Chem. 258, 6695-6697.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6695-6697
    • Scarpa, M.1    Stevanato, R.2    Viglino, P.3    Rigo, A.4
  • 45
    • 0015526351 scopus 로고
    • The electron spin resonance spectra of radical intermediates in the oxidation of ascorbic acid and related substances
    • Laroff, G. P., Fessenden, R.W. & Schuler, R.H. (1972) The electron spin resonance spectra of radical intermediates in the oxidation of ascorbic acid and related substances. J. Am. Chem. Soc. 94, 9062-9073.
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 9062-9073
    • Laroff, G.P.1    Fessenden, R.W.2    Schuler, R.H.3
  • 46
    • 0019872779 scopus 로고
    • Superoxide dismutase activity of macrocyclic polyamine complexes
    • Kimura, E., Sakomnaka, A. & Nakamoto, M. (1981) Superoxide dismutase activity of macrocyclic polyamine complexes. Biochim. Biophys. Acta 678, 172-179.
    • (1981) Biochim. Biophys. Acta , vol.678 , pp. 172-179
    • Kimura, E.1    Sakomnaka, A.2    Nakamoto, M.3
  • 47
    • 0025128371 scopus 로고
    • A mechanistic study of the copper (II)-peptide-catalyzed superoxide dismutation. A pulse radiolysis study
    • Goldstein, S., Czapski, G. & Meyerstein, D. (1990) A mechanistic study of the copper (II)-peptide-catalyzed superoxide dismutation. A pulse radiolysis study. J. Am. Chem. Soc. 112, 6489-6492.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 6489-6492
    • Goldstein, S.1    Czapski, G.2    Meyerstein, D.3
  • 48
    • 0001030178 scopus 로고
    • Catalytic activity studies of some copper (II)-histidine-containing dipeptide complexes on aqueous superoxide ion dismutation
    • Amar, C., Vilkans, E. & Foos, J. (1982) Catalytic activity studies of some copper (II)-histidine-containing dipeptide complexes on aqueous superoxide ion dismutation. J. Inorg. Biochem. 17, 313.
    • (1982) J. Inorg. Biochem. , vol.17 , pp. 313
    • Amar, C.1    Vilkans, E.2    Foos, J.3
  • 49
    • 0002927485 scopus 로고
    • Amino acids, amines, amides, peptides and their derivatives
    • Clarendon Press, Oxford
    • Dawson, R., Elliott, D., Elliott, W. & Jones, K. (1984) Amino acids, amines, amides, peptides and their derivatives. In Data for Biochemical Research. Clarendon Press, Oxford, pp. 1-31.
    • (1984) Data for Biochemical Research , pp. 1-31
    • Dawson, R.1    Elliott, D.2    Elliott, W.3    Jones, K.4
  • 50
    • 0001232804 scopus 로고
    • Structure of the species in the copper (II)-L-histidine system
    • Kruck, T. & Sarkar, B. (1973) Structure of the species in the copper (II)-L-histidine system. Can. J. Chem. 51, 3563-3571.
    • (1973) Can. J. Chem. , vol.51 , pp. 3563-3571
    • Kruck, T.1    Sarkar, B.2
  • 51
    • 0020491099 scopus 로고
    • Kinetics and mechanism of the reduction of ferricytochrome c by superoxide anion
    • Butler, J., Koppenol, W.H. & Margoliash, E. (1982) Kinetics and mechanism of the reduction of ferricytochrome c by superoxide anion. J. Biol. Chem. 257, 10747-10750.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10747-10750
    • Butler, J.1    Koppenol, W.H.2    Margoliash, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.