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Volumn 4, Issue 12, 1997, Pages 1032-1038

Crystal structure of horseradish peroxidase C at 2.15 Å resolution

Author keywords

[No Author keywords available]

Indexed keywords

HORSERADISH PEROXIDASE;

EID: 0030780270     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb1297-1032     Document Type: Article
Times cited : (681)

References (67)
  • 1
    • 0002154654 scopus 로고
    • Horseradish peroxidase: Structure and Kinetic Properties
    • eds Everse, I., Everse, K.E. & Grisham, M. B. (CRC Press, Boca Raton)
    • Dunford, H.B. Horseradish peroxidase: Structure and Kinetic Properties. In Peroxidases in Chemistry and Biology Vol. 2 (eds Everse, I., Everse, K.E. & Grisham, M. B.) 1-24 (CRC Press, Boca Raton; 1991).
    • (1991) Peroxidases in Chemistry and Biology , vol.2 , pp. 1-24
    • Dunford, H.B.1
  • 3
    • 0001277376 scopus 로고
    • The kinetics of the enzyme-substrate compound of peroxidase
    • Chance, B. The kinetics of the enzyme-substrate compound of peroxidase. J. Biol. Chem. 151, 553-577 (1943).
    • (1943) J. Biol. Chem. , vol.151 , pp. 553-577
    • Chance, B.1
  • 4
    • 0019321508 scopus 로고
    • The stereochemistry of peroxidase catalysis
    • Poulos, T.L. & Kraut, J. The stereochemistry of peroxidase catalysis J. Biol. Chem. 255, 8199-8205 (1980).
    • (1980) J. Biol. Chem. , vol.255 , pp. 8199-8205
    • Poulos, T.L.1    Kraut, J.2
  • 5
    • 0027421337 scopus 로고
    • Histidine 52 is a critical residue for rapid formation of cytochrome ⊂ peroxidase compound I
    • Erman, J. E. et al. Histidine 52 is a critical residue for rapid formation of cytochrome ⊂ peroxidase compound I. Biochemistry 32, 9798-9806 (1993).
    • (1993) Biochemistry , vol.32 , pp. 9798-9806
    • Erman, J.E.1
  • 6
    • 0027424783 scopus 로고
    • Effect of Arginine-48 replacement on the reactions between cytochrome ⊂ peroxidase and hydrogen peroxide
    • Vitello, L.B., Erman, J.E., Miller, M.A., Wang, J. & Kraut, J. Effect of Arginine-48 replacement on the reactions between cytochrome ⊂ peroxidase and hydrogen peroxide. Biochemistry 32, 9807-9818 (1993).
    • (1993) Biochemistry , vol.32 , pp. 9807-9818
    • Vitello, L.B.1    Erman, J.E.2    Miller, M.A.3    Wang, J.4    Kraut, J.5
  • 7
    • 3242866521 scopus 로고    scopus 로고
    • Recombinant Horseradish Peroxidase Isoenzyme C: The Effect of Distal Haem Cavity Mutations (His 42→Leu and Arg 38→Leu) on Compound I Formation and Substrate Binding
    • Rodriguez-Lopez, J.N., Smith, A.T. & Thorneley, R.N.F. Recombinant Horseradish Peroxidase Isoenzyme C: The Effect of Distal Haem Cavity Mutations (His 42→Leu and Arg 38→Leu) on Compound I Formation and Substrate Binding. J. Biol. Inorg. Chem. 1, 136-142 (1996).
    • (1996) J. Biol. Inorg. Chem. , vol.1 , pp. 136-142
    • Rodriguez-Lopez, J.N.1    Smith, A.T.2    Thorneley, R.N.F.3
  • 8
    • 0030068091 scopus 로고    scopus 로고
    • Role of Arg-38 in Horseradish peroxidase. A critical residue for substrate binding and catalysis
    • Rodriguez-Lopez, J.N., Smith. A.T. & Thorneley, R.N.F. Role of Arg-38 in Horseradish peroxidase. A critical residue for substrate binding and catalysis. J. Biol. Chem. 271, 4023-4030 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 4023-4030
    • Rodriguez-Lopez, J.N.1    Smith, A.T.2    Thorneley, R.N.F.3
  • 9
    • 0030028437 scopus 로고    scopus 로고
    • Rates of reaction of Indoleacetic acids with horseradish peroxidase compound I and their dependence on redox potentials
    • Candeias, L.P., Folkes, L.P., Porssa, M., Parrick, J. & Wardman, P. Rates of reaction of Indoleacetic acids with horseradish peroxidase compound I and their dependence on redox potentials. Biochemistry 35, 102-108 (1996).
    • (1996) Biochemistry , vol.35 , pp. 102-108
    • Candeias, L.P.1    Folkes, L.P.2    Porssa, M.3    Parrick, J.4    Wardman, P.5
  • 10
    • 0025240595 scopus 로고
    • Kinetic and molecular orbital studies on the rate of oxidation of monosubstituted phenols and anilines by horseradish peroxidase compound I
    • Sakurada, J., Sekiguchi, R., Sato, K., & Hosoya, T. Kinetic and molecular orbital studies on the rate of oxidation of monosubstituted phenols and anilines by horseradish peroxidase compound I. Biochemistry 29, 4093-4098 (1990).
    • (1990) Biochemistry , vol.29 , pp. 4093-4098
    • Sakurada, J.1    Sekiguchi, R.2    Sato, K.3    Hosoya, T.4
  • 11
    • 0025195803 scopus 로고
    • 1H-NMR studies of horseradish peroxidase C and its interaction with indole-3-propionic acid
    • 1H-NMR studies of horseradish peroxidase C and its interaction with indole-3-propionic acid. Eur. J. Biochem. 189, 351-362 (1990).
    • (1990) Eur. J. Biochem. , vol.189 , pp. 351-362
    • Veitch, N.C.1    Williams, R.J.P.2
  • 12
    • 0002510166 scopus 로고
    • Two dimensional proton nuclear magnetic resonance studies of plant peroxidase interactions with aromatic donor molecules
    • eds Lobarzewski, J., Greppin, H., Penel, C. & Gaspar, T. (University of Geneva, Switzerland)
    • Veitch, N.C. & Williams, R.J.P. Two dimensional proton nuclear magnetic resonance studies of plant peroxidase interactions with aromatic donor molecules. In Biochemical, molecular and physiological aspects of plant peroxidases (eds Lobarzewski, J., Greppin, H., Penel, C. & Gaspar, T.) 99-109 (University of Geneva, Switzerland; 1991).
    • (1991) Biochemical, Molecular and Physiological Aspects of Plant Peroxidases , pp. 99-109
    • Veitch, N.C.1    Williams, R.J.P.2
  • 13
    • 0022974617 scopus 로고
    • Nuclear Magnetic Resonance Studies on the Spatial Relationship of Aromatic Donor Molecules to the Heme Iron of Horseradish Peroxidase
    • Sakurada, J., Takahashi, S. & Hosoya, T. Nuclear Magnetic Resonance Studies on the Spatial Relationship of Aromatic Donor Molecules to the Heme Iron of Horseradish Peroxidase. J. Biol. Chem. 261, 9657-9662 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 9657-9662
    • Sakurada, J.1    Takahashi, S.2    Hosoya, T.3
  • 15
    • 0028954014 scopus 로고
    • The use of methylsubstituted benzhydroxamic acids as structural probes of peroxidase substrate binding
    • Veitch, N.C. & Williams, R.J.P. The use of methylsubstituted benzhydroxamic acids as structural probes of peroxidase substrate binding, Eur. J. Biochem. 229, 629-40 (1995).
    • (1995) Eur. J. Biochem. , vol.229 , pp. 629-640
    • Veitch, N.C.1    Williams, R.J.P.2
  • 16
    • 0023644531 scopus 로고
    • Protein control of prosthetic heme reactivity
    • Ator, M.A. & Ortiz de Montellano, P.R. Protein control of prosthetic heme reactivity. J. Biol. Chem. 262, 1542-1551 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 1542-1551
    • Ator, M.A.1    Ortiz de Montellano, P.R.2
  • 19
    • 0025275451 scopus 로고
    • 2+ and heme
    • 2+ and heme. J. Biol. Chem. 265, 13335-13343 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 13335-13343
    • Smith, A.T.1
  • 20
    • 0026760509 scopus 로고
    • Baculovirus expression and characterization of catalytically active horseradish peroxidase
    • Hartmann, C. & Ortiz de Montellano, P.R. Baculovirus expression and characterization of catalytically active horseradish peroxidase. Arch. Biochem. Biophys. 297, 61-72 (1992).
    • (1992) Arch. Biochem. Biophys. , vol.297 , pp. 61-72
    • Hartmann, C.1    Ortiz de Montellano, P.R.2
  • 21
    • 0029151614 scopus 로고
    • Horseradish peroxidase H42A, H42V and F41A, mutants -histidine catalysis and control of substrate access to the heme iron
    • Newmyer, S.L. & Ortiz de Montellano, P.R. Horseradish peroxidase H42A, H42V and F41A, mutants -histidine catalysis and control of substrate access to the heme iron. J. Biol. Chem. 270, 19430-19438 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 19430-19438
    • Newmyer, S.L.1    Ortiz de Montellano, P.R.2
  • 22
    • 17544377403 scopus 로고    scopus 로고
    • Rescue of the catalytic activity of an H42A mutant of horseradish peroxidase by exogenous imidazoles
    • Newmyer, S.L. & Ortiz de Montellano, P.R. Rescue of the catalytic activity of an H42A mutant of horseradish peroxidase by exogenous imidazoles. J. Biol. Chem. 271, 14891-14896 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 14891-14896
    • Newmyer, S.L.1    Ortiz de Montellano, P.R.2
  • 23
    • 0029793799 scopus 로고    scopus 로고
    • Rescue of the horseradish peroxidase H170A mutant activity by imidazole - Importance of proximal ligand tethering
    • Newmyer, S.L., Sun J., Loehr, T.M. & Ortiz de Montellano, P.R. Rescue of the horseradish peroxidase H170A mutant activity by imidazole - importance of proximal ligand tethering. Biochemistry 35, 12788-12795 (1996).
    • (1996) Biochemistry , vol.35 , pp. 12788-12795
    • Newmyer, S.L.1    Sun, J.2    Loehr, T.M.3    Ortiz de Montellano, P.R.4
  • 24
    • 0031031466 scopus 로고    scopus 로고
    • Effect of distal cavity mutations on the binding and activation of oxygen by ferrous horseradish peroxidase
    • Rodriguez-Lopez, J.N., Smith, A.T. & Thorneley, R.N. Effect of distal cavity mutations on the binding and activation of oxygen by ferrous horseradish peroxidase. J. Biol. Chem. 272, 389-395 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 389-395
    • Rodriguez-Lopez, J.N.1    Smith, A.T.2    Thorneley, R.N.3
  • 25
    • 0029849202 scopus 로고    scopus 로고
    • Catalytic roles of the distal site asparagine-histidine couple in peroxidases
    • Nagano, S., Tanaka, M., Ishimori, K., Watanabe, Y. & Morishima, I. Catalytic roles of the distal site asparagine-histidine couple in peroxidases. Biochemistry 35, 14251-14258 (1996).
    • (1996) Biochemistry , vol.35 , pp. 14251-14258
    • Nagano, S.1    Tanaka, M.2    Ishimori, K.3    Watanabe, Y.4    Morishima, I.5
  • 26
    • 0031037679 scopus 로고    scopus 로고
    • Mutation of distal residues of horseradish peroxidase: Influence on substrate binding and cavity properties
    • Howes, B.D., Rodriguez-Lopez, J.N., Smith, A.T. & Smulevich, G. Mutation of distal residues of horseradish peroxidase: influence on substrate binding and cavity properties. Biochemistry 36, 1532-1543 (1997).
    • (1997) Biochemistry , vol.36 , pp. 1532-1543
    • Howes, B.D.1    Rodriguez-Lopez, J.N.2    Smith, A.T.3    Smulevich, G.4
  • 27
    • 0029906497 scopus 로고    scopus 로고
    • Refinement of 3D models of Horeseradish peroxidase: Predictions of 2D NMR assignments and substrate binding sites
    • Zhao, D., Gilfoyle, D. J., Smith A.T. & Loew, G. Refinement of 3D models of Horeseradish peroxidase: Predictions of 2D NMR assignments and substrate binding sites. Prot. Struc. Func. Gen. 26, 204-216 (1996).
    • (1996) Prot. Struc. Func. Gen. , vol.26 , pp. 204-216
    • Zhao, D.1    Gilfoyle, D.J.2    Smith, A.T.3    Loew, G.4
  • 29
    • 0002043346 scopus 로고    scopus 로고
    • The peroxidase gene family of Arabidopsis Thaliana
    • eds Obinger, C. et al. (University of Geneva, Switzerland)
    • Simon, P. et al. The peroxidase gene family of Arabidopsis Thaliana. In Plant Peroxidases: Biochemistry and Physiology (eds Obinger, C. et al.) 179-183 (University of Geneva, Switzerland; 1996).
    • (1996) Plant Peroxidases: Biochemistry and Physiology , pp. 179-183
    • Simon, P.1
  • 30
    • 0019332103 scopus 로고
    • The structure of cytochrome C at 2.5 Å resolution
    • Poulos, T. L., et al., & Kraut J. The structure of cytochrome C at 2.5 Å resolution. J. Biol. Chem. 255, 575-580 (1980).
    • (1980) J. Biol. Chem. , vol.255 , pp. 575-580
    • Poulos, T.L.1    Kraut, J.2
  • 31
    • 0028901185 scopus 로고
    • Crystal structure of recombinant pea cytosolic ascorbate peroxidase
    • Patterson, W.R. & Poulos, T.L. Crystal structure of recombinant pea cytosolic ascorbate peroxidase. Biochemistry 34, 4331-4341 (1995).
    • (1995) Biochemistry , vol.34 , pp. 4331-4341
    • Patterson, W.R.1    Poulos, T.L.2
  • 32
    • 0027957704 scopus 로고
    • Crystal structure of the fungal peroxidase from Arthromyces rarnocus at 1.9 Å resolution
    • Kunishima, N. et al., & Amachi, T. Crystal structure of the fungal peroxidase from Arthromyces rarnocus at 1.9 Å resolution. J. Mol. Biol. 235, 331-344 (1994).
    • (1994) J. Mol. Biol. , vol.235 , pp. 331-344
    • Kunishima, N.1    Amachi, T.2
  • 33
    • 0027514159 scopus 로고
    • Crystallographic refinement of lignin peroxidase at 2 Å
    • Poulos, T.L., Edwards, S.L., Wariishi, H & Gold M.H. Crystallographic refinement of lignin peroxidase at 2 Å. J. Biol. Chem. 268, 4429-4440 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 4429-4440
    • Poulos, T.L.1    Edwards, S.L.2    Wariishi, H.3    Gold, M.H.4
  • 34
    • 0027514481 scopus 로고
    • Low pH crystal structure of glycosylated lignin peroxidase from Phanerocaete chrysosporium at 2.06 A resolution
    • Piontek, K, Glumoff, T. & Winterhalter, K. Low pH crystal structure of glycosylated lignin peroxidase from Phanerocaete chrysosporium at 2.06 A resolution. FEBs Lett. 315, 119-124 (1993).
    • (1993) FEBs Lett. , vol.315 , pp. 119-124
    • Piontek, K.1    Glumoff, T.2    Winterhalter, K.3
  • 35
    • 0040719612 scopus 로고
    • Homology modeling of horseradish peroxidase
    • ed. La Mar, G.N. (Kluwer Academic Publishers, Dordrecht, Netherlands)
    • Smith, A.T., Du, P. & Loew, G.H. Homology modeling of horseradish peroxidase. In Nuclear magnetic resonance of paramagnetic macromolecules (ed. La Mar, G.N.) 75-93 (Kluwer Academic Publishers, Dordrecht, Netherlands;1994).
    • (1994) Nuclear Magnetic Resonance of Paramagnetic Macromolecules , pp. 75-93
    • Smith, A.T.1    Du, P.2    Loew, G.H.3
  • 36
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these maps
    • Jones, A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these maps, Acta Crystallogr. A47, 110-119 (1991).
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 37
    • 0018488111 scopus 로고
    • Amino acid sequence studies of horseradish peroxidase
    • Welinder, K.G. Amino acid sequence studies of horseradish peroxidase. Eur. J. Biochem. 96, 483-502 (1979).
    • (1979) Eur. J. Biochem. , vol.96 , pp. 483-502
    • Welinder, K.G.1
  • 38
    • 0028807809 scopus 로고
    • Comparative study of the inactivation of wild-type, recombinant and two mutant horseradish peroxidase isoenzymes C by hydrogen peroxide and m-chloroperoxybenzoic acid
    • Hiner, A.N. et al. comparative study of the inactivation of wild-type, recombinant and two mutant horseradish peroxidase isoenzymes C by hydrogen peroxide and m-chloroperoxybenzoic acid. Eur. J. Biochem. 234, 506-512 (1995).
    • (1995) Eur. J. Biochem. , vol.234 , pp. 506-512
    • Hiner, A.N.1
  • 39
    • 0029129561 scopus 로고
    • Crystal structures of cyanide- and triiodide-bound forms of Arthromyces ramosus peroxidase at different pH values
    • Fukuyama, K., Kunishima, N., Amada, F., Kubota, T. & Matsubara, H. Crystal structures of cyanide- and triiodide-bound forms of Arthromyces ramosus peroxidase at different pH values, J. Biol. Chem. 270, 21884-21892 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 21884-21892
    • Fukuyama, K.1    Kunishima, N.2    Amada, F.3    Kubota, T.4    Matsubara, H.5
  • 40
    • 0028283622 scopus 로고
    • Characterization of recombinant horseradish peroxidase C and three site-directed mutants, F41V, F41W, and R38K, by resonance Raman spectroscopy
    • Smulevich, G. et al. Characterization of recombinant horseradish peroxidase C and three site-directed mutants, F41V, F41W, and R38K, by resonance Raman spectroscopy. Biochemistry 33, 7398-407 (1994).
    • (1994) Biochemistry , vol.33 , pp. 7398-7407
    • Smulevich, G.1
  • 41
    • 0026062386 scopus 로고
    • Resonance Raman investigation of ferric ion in horseradish peroxidase and its aromatic donor complexes at room and low temperature
    • Smulevich, G., English A.M., Martini, A.R. & Marzocchi M.P. Resonance Raman investigation of ferric ion in horseradish peroxidase and its aromatic donor complexes at room and low temperature. Biochemistry 30, 772-779 (1991).
    • (1991) Biochemistry , vol.30 , pp. 772-779
    • Smulevich, G.1    English, A.M.2    Martini, A.R.3    Marzocchi, M.P.4
  • 42
    • 0027402748 scopus 로고
    • A step towards understanding the folding mechanism of horseradish peroxidase. Tryptophan fluorescence and circular dichroism equilibrium studies
    • Pappa, H. S. & Cass, A.E. A step towards understanding the folding mechanism of horseradish peroxidase. Tryptophan fluorescence and circular dichroism equilibrium studies, Eur. J. Biochem. 212, 227-235 (1995).
    • (1995) Eur. J. Biochem. , vol.212 , pp. 227-235
    • Pappa, H.S.1    Cass, A.E.2
  • 43
    • 0022976015 scopus 로고
    • Presence of endogenous calcium ion and its functional and structural regulation in horseradish peroxidase
    • Shiro, Y., Kurono, M. & Morishima, I. Presence of endogenous calcium ion and its functional and structural regulation in horseradish peroxidase. J. Biol. Chem. 261, 9382-9390 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 9382-9390
    • Shiro, Y.1    Kurono, M.2    Morishima, I.3
  • 44
    • 0002037932 scopus 로고
    • Structure and Evolution of Peroxidases
    • III International Symposium July 10-14 (eds Welinder, K.G., Rasmussen, S.K., Penel, C. & Greppin, H.) (University of Geneva, Elsinore, Denmark)
    • Welinder, K.G. & Gajhede, M. Structure and Evolution of Peroxidases. Proceedings of : Plant Peroxidases Biochemistry and Physiology. III International Symposium July 10-14 (eds Welinder, K.G., Rasmussen, S.K., Penel, C. & Greppin, H.) 35-42 (University of Geneva, Elsinore, Denmark; 1993).
    • (1993) Proceedings of : Plant Peroxidases Biochemistry and Physiology , pp. 35-42
    • Welinder, K.G.1    Gajhede, M.2
  • 45
    • 0026684348 scopus 로고
    • Structural studies by proton-NMR spectroscopy of plant peroxidase C, the wild-type recombinant protein from Escherichia coli and two protein variants, Phe41 Val and Arg38 Lys
    • Veitch, N.C. et al. Structural studies by proton-NMR spectroscopy of plant peroxidase C, the wild-type recombinant protein from Escherichia coli and two protein variants, Phe41 Val and Arg38 Lys. Eur. J. Biochem. 207, 521-531 (1992).
    • (1992) Eur. J. Biochem. , vol.207 , pp. 521-531
    • Veitch, N.C.1
  • 46
    • 0028137199 scopus 로고
    • Role of the proximal ligand in peroxidase catalysis. Crystallographic, kinetic, and spectral studies of cytochrome ⊂ peroxidase proximal ligand mutants
    • Choudhury, K. et al. Role of the proximal ligand in peroxidase catalysis. Crystallographic, kinetic, and spectral studies of cytochrome ⊂ peroxidase proximal ligand mutants. J Biol. Chem. 269, 20239-20249 (1994).
    • (1994) J Biol. Chem. , vol.269 , pp. 20239-20249
    • Choudhury, K.1
  • 47
    • 0024295374 scopus 로고
    • Tryptophan 191→phenylalanine, a proximal-side mutation in yeast cytochrome ⊂ peroxidase that strongly affects the kinetics of ferrocytochrome ⊂ oxidation
    • Mauro, J.M. et al. Tryptophan 191→phenylalanine, a proximal-side mutation in yeast cytochrome ⊂ peroxidase that strongly affects the kinetics of ferrocytochrome ⊂ oxidation. Biochemistry 27, 6243-6256 (1988).
    • (1988) Biochemistry , vol.27 , pp. 6243-6256
    • Mauro, J.M.1
  • 48
    • 0024473758 scopus 로고
    • Identification of Trp-191 as free radical site in CCP compound ES
    • Sivaraja, M., Goodin, D.B., Smith, M. & Hoffman, B.M. Identification of Trp-191 as free radical site in CCP compound ES. Science 245, 738-740 (1989).
    • (1989) Science , vol.245 , pp. 738-740
    • Sivaraja, M.1    Goodin, D.B.2    Smith, M.3    Hoffman, B.M.4
  • 49
    • 0028913020 scopus 로고
    • Identification of a porphyrin-cation radical in ascorbate peroxidase compound I
    • Patterson, W.R., Poulos, T.L. & Goodin D.B. Identification of a porphyrin-cation radical in ascorbate peroxidase compound I. Biochemistry 34, 4342-4345 (1995).
    • (1995) Biochemistry , vol.34 , pp. 4342-4345
    • Patterson, W.R.1    Poulos, T.L.2    Goodin, D.B.3
  • 50
    • 0030734513 scopus 로고    scopus 로고
    • Identification of a critical phenylalanine residue in the horseradish peroxidase, Phe 179, by site directed mutagenesis and H-NMR: Implications for complex formation with aromatic donor molecules
    • in press
    • Veitch, N.C., Gao, Y., Smith, A.T. & White C.G. Identification of a critical phenylalanine residue in the horseradish peroxidase, Phe 179, by site directed mutagenesis and H-NMR: Implications for complex formation with aromatic donor molecules. Biochemistry (in press) (1997).
    • (1997) Biochemistry
    • Veitch, N.C.1    Gao, Y.2    Smith, A.T.3    White, C.G.4
  • 51
    • 0026506023 scopus 로고
    • Comparison of structure and activities of peroxidases from Coprinus cinereus, Coprinus macrorhizus and Arthromyces ramosus
    • Kjalke, M. et al. Comparison of structure and activities of peroxidases from Coprinus cinereus, Coprinus macrorhizus and Arthromyces ramosus. Biochim. Biophys. Acta. 1120, 248-256 (1992).
    • (1992) Biochim. Biophys. Acta. , vol.1120 , pp. 248-256
    • Kjalke, M.1
  • 52
    • 0017144641 scopus 로고
    • Unit cell dimensions of crystalline horseradish peroxidase
    • Braithwaite, A. Unit cell dimensions of crystalline horseradish peroxidase. J. Mol. Biol. 106, 229-230 (1976).
    • (1976) J. Mol. Biol. , vol.106 , pp. 229-230
    • Braithwaite, A.1
  • 53
    • 0025999194 scopus 로고
    • The study of intact proteins and glycoproteins by electrospray m.s
    • Green, B.N. & Olivier, R.W.A. The study of intact proteins and glycoproteins by electrospray m.s. Biochem. Soc. Trans. 19, 929-935 (1991).
    • (1991) Biochem. Soc. Trans. , vol.19 , pp. 929-935
    • Green, B.N.1    Olivier, R.W.A.2
  • 54
    • 0029161309 scopus 로고
    • Preliminary X-ray Diffraction Studies of Recombinant Peroxidase Isoenzyme C
    • Henriksen A. et al. Preliminary X-ray Diffraction Studies of Recombinant Peroxidase Isoenzyme C. Acta, Crystallogr. D51, 121-123 (1995).
    • (1995) Acta, Crystallogr. , vol.D51 , pp. 121-123
    • Henriksen, A.1
  • 56
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A50, 157-163 (1994).
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 57
    • 0014432781 scopus 로고
    • Solvent content of proteins
    • Matthews, B.W. Solvent content of proteins. J. Mol. Biol. 33, 491-497 (1968).
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 58
    • 0028103275 scopus 로고
    • 1994 Collaborative Computing Project, number 4 the CCP4 suite: Programs for protein crystallography
    • CCP4, 1994 Collaborative Computing Project, number 4 The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50, 760-763 (1994).
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 59
    • 0001620026 scopus 로고    scopus 로고
    • MAGICSQUASH: More versatile non-crystallographic averaging with multiple constraints
    • Schuller, D.J. MAGICSQUASH: more versatile non-crystallographic averaging with multiple constraints. Acta Crystallogr. D52, 425-434 (1996).
    • (1996) Acta Crystallogr. , vol.D52 , pp. 425-434
    • Schuller, D.J.1
  • 60
    • 0030497978 scopus 로고    scopus 로고
    • Efficient rebuilding of protein structures
    • Kleywegt, GJ. & Jones, T.A. Efficient rebuilding of protein structures. Acta. Crystallogr. D52, 829-841 (1996).
    • (1996) Acta. Crystallogr. , vol.D52 , pp. 829-841
    • Kleywegt, G.J.1    Jones, T.A.2
  • 61
    • 1842286116 scopus 로고
    • X-PLOR Version 3.1
    • Yale University Press, New Haven, Connecticut, USA
    • Brnger, A.T. X-PLOR Version 3.1. A system for X-ray Crystallography and NMR (Yale University Press, New Haven, Connecticut, USA;1993).
    • (1993) A System for X-ray Crystallography and NMR
    • Brnger, A.T.1
  • 62
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R.A. & Huber, R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta. Crystallogr. A47, 392-400 (1991).
    • (1991) Acta. Crystallogr. , vol.A47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 63
    • 0025303764 scopus 로고
    • Protein multiple sequence alignment and flexible pattern matching
    • Barton, G.J. Protein multiple sequence alignment and flexible pattern matching. Meth. Enz. 183, 403-428 (1990).
    • (1990) Meth. Enz. , vol.183 , pp. 403-428
    • Barton, G.J.1
  • 64
    • 0027609916 scopus 로고
    • SETOR: Hardware-lighted three dimensional solid model representations of macromolecules
    • Evans, S.V. SETOR: Hardware-lighted three dimensional solid model representations of macromolecules. J. Mol. Graphics 11, 134-138 (1993).
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 65
    • 0026743174 scopus 로고
    • Multiple protein sequence alignment from tertiary structure comparison
    • Russell, R.B. & Barton, G.J. Multiple protein sequence alignment from tertiary structure comparison. Proteins 14, 309-323 (1992).
    • (1992) Proteins , vol.14 , pp. 309-323
    • Russell, R.B.1    Barton, G.J.2
  • 66
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40 (1993).
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.