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Volumn 261, Issue 1, 1999, Pages 261-268

Effects of divalent metal ions on the activity and conformation of native and 3-fluorotyrosine-PvuII endonucleases

Author keywords

3 Fluorotyrosine; Conformation; Divalent metal ions; NMR spectroscopy; Restriction endonuclease

Indexed keywords

3 FLUOROTYROSINE PVUII ENDONUCLEASE; CALCIUM; MAGNESIUM; RESTRICTION ENDONUCLEASE; UNCLASSIFIED DRUG;

EID: 0033118838     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00265.x     Document Type: Article
Times cited : (29)

References (55)
  • 1
    • 0027184481 scopus 로고
    • A general two-metal ion mechanism for catalytic RNA
    • 1. Steitz, T.A. & Steitz, J.A. (1993) A general two-metal ion mechanism for catalytic RNA. Proc. Natl Acad. Sci. USA 90, 6498-6502.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 2
    • 0031836886 scopus 로고    scopus 로고
    • A critical evaluation of metal-promoted Klenow 3′-5′ exonuclease activity: Calorimetric and kinetic analyses support a one-metal-ion mechanism
    • 2. Black, C.B. & Cowan, J.A. (1998) A critical evaluation of metal-promoted Klenow 3′-5′ exonuclease activity: calorimetric and kinetic analyses support a one-metal-ion mechanism. J. Bioinorg. Chem. 3, 292-299.
    • (1998) J. Bioinorg. Chem. , vol.3 , pp. 292-299
    • Black, C.B.1    Cowan, J.A.2
  • 3
    • 0031882388 scopus 로고    scopus 로고
    • A two-metal ion mechanism operates in the hammerhead ribozyme-mediated cleavage of a an RNA substrate
    • 3. Lott, W.B., Pontius, B.W. & von Hippel, P.H. (1998) A two-metal ion mechanism operates in the hammerhead ribozyme-mediated cleavage of a an RNA substrate. Proc. Natl Acad. Sci. USA 95, 542-547.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 542-547
    • Lott, W.B.1    Pontius, B.W.2    Von Hippel, P.H.3
  • 4
    • 0029815519 scopus 로고    scopus 로고
    • Ribozyme mechanism revisited: Evidence against direct coordination of Mg (II) ion with the pro-R oxygen of the scissile phosphate in the transition state of a hammerhead ribozyme-catalyzed reaction
    • 4. Zhou, D.-M., Kumar, P.K.R., Zhang, L.-H. & Taira, K. (1996) Ribozyme mechanism revisited: Evidence against direct coordination of Mg (II) ion with the pro-R oxygen of the scissile phosphate in the transition state of a hammerhead ribozyme-catalyzed reaction. J. Am. Chem. Soc. 118, 8969-8970.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8969-8970
    • Zhou, D.-M.1    Kumar, P.K.R.2    Zhang, L.-H.3    Taira, K.4
  • 5
    • 0026650908 scopus 로고
    • On the catalytic mechanism of EcoRI and EcoRV
    • 5. Jeltsch, A., Alves, J., Maass, G. & Pingoud, A. (1992) On the catalytic mechanism of EcoRI and EcoRV. FEBS Lett. 304, 4-8.
    • (1992) Febs Lett. , vol.304 , pp. 4-8
    • Jeltsch, A.1    Alves, J.2    Maass, G.3    Pingoud, A.4
  • 6
    • 0030886344 scopus 로고    scopus 로고
    • Does the restriction endonuclease EcoRV employ a two-metal-Ion mechanism for DNA cleavage?
    • 6. Groll, D.H., Jeltsch, A., Selent, U. & Pingoud, A. (1997) Does the restriction endonuclease EcoRV employ a two-metal-Ion mechanism for DNA cleavage? Biochemistry 23, 11389-11401.
    • (1997) Biochemistry , vol.23 , pp. 11389-11401
    • Groll, D.H.1    Jeltsch, A.2    Selent, U.3    Pingoud, A.4
  • 7
    • 0032571245 scopus 로고    scopus 로고
    • Structural principles for the inhibition of the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase 1 by phosphorothioates
    • 7. Brautigam, C.A. & Steitz, T.A. (1998) Structural principles for the inhibition of the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase 1 by phosphorothioates. J. Mol. Biol. 277, 363-377.
    • (1998) J. Mol. Biol. , vol.277 , pp. 363-377
    • Brautigam, C.A.1    Steitz, T.A.2
  • 9
    • 0025187081 scopus 로고
    • Refinement of EcoRI endonuclease crystal structure: A revised protein chain tracing
    • 9. Kim, Y., Grable, J.C., Love, R., Greene, P.J. & Rosenberg, J.M. (1990) Refinement of EcoRI endonuclease crystal structure: a revised protein chain tracing. Science 249, 1307-1309.
    • (1990) Science , vol.249 , pp. 1307-1309
    • Kim, Y.1    Grable, J.C.2    Love, R.3    Greene, P.J.4    Rosenberg, J.M.5
  • 10
    • 0001076529 scopus 로고
    • Structure and function of restriction endonucleases
    • 10. Rosenberg, J.M. (1991) Structure and function of restriction endonucleases. Curr. Opin. Struct. Biol. 1, 104-113.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 104-113
    • Rosenberg, J.M.1
  • 12
    • 0028988416 scopus 로고
    • 2+ binding to the active site of EcoRV endonuclease: A crystallographic study of complexes with substrate and product DNA at 2 Å resolution
    • 2+ binding to the active site of EcoRV endonuclease: a crystallographic study of complexes with substrate and product DNA at 2 Å resolution. Biochemistry 34, 683-696.
    • (1995) Biochemistry , vol.34 , pp. 683-696
    • Kostrewa, D.1    Winkler, F.K.2
  • 13
    • 0029048413 scopus 로고
    • Structure of BamHI endonuclease bound to DNA: Partial folding and unfolding on DNA binding
    • 13. Newman, M., Strzelecka, T., Dorner, L.F., Schildkraut, I. & Aggarwal, A.K. (1995) Structure of BamHI endonuclease bound to DNA: partial folding and unfolding on DNA binding. Science 269, 656-663.
    • (1995) Science , vol.269 , pp. 656-663
    • Newman, M.1    Strzelecka, T.2    Dorner, L.F.3    Schildkraut, I.4    Aggarwal, A.K.5
  • 14
    • 0028024850 scopus 로고
    • Structure of PvuII endonuclease with cognate DNA
    • 14. Cheng, X., Balendiran, K., Schildkraut, I. & Anderson, J.E. (1994) Structure of PvuII endonuclease with cognate DNA. EMBO J. 13, 3927-3935.
    • (1994) EMBO J. , vol.13 , pp. 3927-3935
    • Cheng, X.1    Balendiran, K.2    Schildkraut, I.3    Anderson, J.E.4
  • 15
    • 0029995002 scopus 로고    scopus 로고
    • Crystal structure of Citrobacter freundii restriction endonuclease Cfr10I at 2.15 Å resolution
    • 15. Bozic, D., Grazulis, A., Siksnys, V. & Huber, R. (1996) Crystal structure of Citrobacter freundii restriction endonuclease Cfr10I at 2.15 Å resolution. J. Mol. Biol. 255, 176-186.
    • (1996) J. Mol. Biol. , vol.255 , pp. 176-186
    • Bozic, D.1    Grazulis, A.2    Siksnys, V.3    Huber, R.4
  • 16
    • 0032530311 scopus 로고    scopus 로고
    • Crystal structure of restriction endonuclease BglI bound to its interrupted DNA recognition sequence
    • 16. Newman, M., Lunnen, K., Wilson, G., Greci, J., Schildkraut, I. & Phillips, S.E.V. (1998) Crystal structure of restriction endonuclease BglI bound to its interrupted DNA recognition sequence. EMBO J. 17, 5466-5476.
    • (1998) EMBO J. , vol.17 , pp. 5466-5476
    • Newman, M.1    Lunnen, K.2    Wilson, G.3    Greci, J.4    Schildkraut, I.5    Phillips, S.E.V.6
  • 17
    • 0023057187 scopus 로고
    • Site directed mutagenesis experiments suggest that Glu111, Glu144, and Arg145 are essential for endonucleolytic activity of EcoRI
    • 17. Wolfes, H., Alves, J., Fliess, A., Geiger, R. & Pingoud, A. (1986) Site directed mutagenesis experiments suggest that Glu111, Glu144, and Arg145 are essential for endonucleolytic activity of EcoRI. Nuc. Acids Res. 14, 9063-9081.
    • (1986) Nuc. Acids Res. , vol.14 , pp. 9063-9081
    • Wolfes, H.1    Alves, J.2    Fliess, A.3    Geiger, R.4    Pingoud, A.5
  • 18
    • 0024379261 scopus 로고
    • Glu-111 is required for activation of the DNA cleavage center of EcoRI endonuclease
    • 18. King, K., Benkovic, S.J. & Modrich, P. (1989) Glu-111 Is required for activation of the DNA cleavage center of EcoRI endonuclease. J. Biol. Chem. 264, 11807-11815.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11807-11815
    • King, K.1    Benkovic, S.J.2    Modrich, P.3
  • 19
    • 0024359479 scopus 로고
    • The negative charge of Glu-111 is required to activate the cleavage center of EcoRI endonuclease
    • 19. Wright, D.J., King, K. & Modrich, P. (1989) The negative charge of Glu-111 is required to activate the cleavage center of EcoRI endonuclease. J. Biol. Chem. 264, 11816-11821.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11816-11821
    • Wright, D.J.1    King, K.2    Modrich, P.3
  • 20
    • 0029063469 scopus 로고
    • Site-directed mutagenesis in the catalytic center of the restriction endonuclease EcoRI
    • 20. Grabowski, G., Jeltsch, A., Wolfes, H., Maass, G. & Alves, J. (1995) Site-directed mutagenesis in the catalytic center of the restriction endonuclease EcoRI. Gene 157, 113-118.
    • (1995) Gene , vol.157 , pp. 113-118
    • Grabowski, G.1    Jeltsch, A.2    Wolfes, H.3    Maass, G.4    Alves, J.5
  • 21
    • 0025865885 scopus 로고
    • Isolation of BamHI variants with reduced cleavage activities
    • 21. Xu, S. & Schildkraut, I. (1991) Isolation of BamHI variants with reduced cleavage Activities. J. Biol. Chem. 266, 4425-4429.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4425-4429
    • Xu, S.1    Schildkraut, I.2
  • 22
    • 0028303476 scopus 로고
    • Direct selection of binding proficient/catalytic deficient variants of BamHI endonuclease
    • 22. Dorner, L.F. & Schildkraut, I. (1994) Direct selection of binding proficient/catalytic deficient variants of BamHI endonuclease. Nuc. Acids Res. 22, 1068-1074.
    • (1994) Nuc. Acids Res. , vol.22 , pp. 1068-1074
    • Dorner, L.F.1    Schildkraut, I.2
  • 23
    • 0030867835 scopus 로고    scopus 로고
    • Catalytic and DNA binding properties of PvuII restriction endonuclease mutants
    • 23. Nastri, H.G., Evans, P.D., Walker, I.H. & Riggs, P.D. (1997) Catalytic and DNA binding properties of PvuII restriction endonuclease mutants. J. Biol. Chem. 272, 25761-25767.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25761-25767
    • Nastri, H.G.1    Evans, P.D.2    Walker, I.H.3    Riggs, P.D.4
  • 24
    • 0025819774 scopus 로고
    • Site-directed mutagenesis studies with EcoRV restriction endonuclease to identify regions involved in recognition and catalysis
    • 24. Thielking, V., Selent, U., Kohler, E., Wolfes, H., Pieper, U., Geiger, R., Urbanke, C., Winkler, F.K. & Pingoud, A. (1991) Site-directed mutagenesis studies with EcoRV restriction endonuclease to identify regions involved in recognition and catalysis. Biochemistry 30, 6416-6422.
    • (1991) Biochemistry , vol.30 , pp. 6416-6422
    • Thielking, V.1    Selent, U.2    Kohler, E.3    Wolfes, H.4    Pieper, U.5    Geiger, R.6    Urbanke, C.7    Winkler, F.K.8    Pingoud, A.9
  • 25
    • 0026696177 scopus 로고
    • A site-directed mutagenesis study to identify amino acid residues involved in the catalytic function of the restriction endonuclease EcoRV
    • 25. Selent, U., Ruter, T., Kohler, E., Liedtke, M., Thielking, V., Alves, J., Oelgeschlager, T., Wolfes, H., Peters, F. & Pingoud, A. (1992) A site-directed mutagenesis study to identify amino acid residues involved in the catalytic function of the restriction endonuclease EcoRV. Biochemistry 31, 4808-4815.
    • (1992) Biochemistry , vol.31 , pp. 4808-4815
    • Selent, U.1    Ruter, T.2    Kohler, E.3    Liedtke, M.4    Thielking, V.5    Alves, J.6    Oelgeschlager, T.7    Wolfes, H.8    Peters, F.9    Pingoud, A.10
  • 26
    • 0025998488 scopus 로고
    • Role of divalent metal ions in the hammerhead ribozyme RNA cleavage reaction
    • 26. Dahm, S.C. & Uhlenbeck, O.C. (1991) Role of divalent metal ions in the hammerhead ribozyme RNA cleavage reaction. Biochemistry 30, 9464-9469.
    • (1991) Biochemistry , vol.30 , pp. 9464-9469
    • Dahm, S.C.1    Uhlenbeck, O.C.2
  • 27
    • 1842577797 scopus 로고    scopus 로고
    • Magnesium vs. manganese cofactors for metallonuclease enzymes. A critical evaluation of thermo-dynamic binding parameters and stoichiometry
    • 27. Casareno, R.L. & Cowan, J.A. (1996) Magnesium vs. manganese cofactors for metallonuclease enzymes. A critical evaluation of thermo-dynamic binding parameters and stoichiometry. Chem. Commun. 15, 1813-1814.
    • (1996) Chem. Commun. , vol.15 , pp. 1813-1814
    • Casareno, R.L.1    Cowan, J.A.2
  • 28
    • 0030026560 scopus 로고    scopus 로고
    • Asp537 and Asp812 in bacteriophage T7 RNA polymerase as metal ion-binding sites studied by EPR, flow-dialysis, and transcription
    • 28. Woody, A.-Y.M., Eaton, S.S., Osumi-Davis, P.A. & Woody, R.W. (1996) Asp537 and Asp812 in bacteriophage T7 RNA polymerase as metal ion-binding sites studied by EPR, flow-dialysis, and transcription. Biochemistry 35, 144-152.
    • (1996) Biochemistry , vol.35 , pp. 144-152
    • Woody, A.-Y.M.1    Eaton, S.S.2    Osumi-Davis, P.A.3    Woody, R.W.4
  • 29
    • 0029951474 scopus 로고    scopus 로고
    • Ribozymes: Structure and mechanism in RNA catalysis
    • 29. Scott, W.G. & Klug, A. (1996) Ribozymes: structure and mechanism in RNA catalysis. Trends Biochem. Sci. 21, 220-224.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 220-224
    • Scott, W.G.1    Klug, A.2
  • 30
    • 0028938496 scopus 로고
    • Divalent metal ions at the active sites of the EcoRV and EcoRI restriction endonucleases
    • 30. Vipond, I.B., Baldwin, G.S. & Halford, S.E. (1995) Divalent metal ions at the active sites of the EcoRV and EcoRI restriction endonucleases. Biochemistry 34, 697-704.
    • (1995) Biochemistry , vol.34 , pp. 697-704
    • Vipond, I.B.1    Baldwin, G.S.2    Halford, S.E.3
  • 31
    • 0032516471 scopus 로고    scopus 로고
    • Unusual metal ion catalysis in an acyl-transferase ribozyme
    • 31. Suga, H., Cowan, J.A. & Szostak, J.W. (1998) Unusual metal ion catalysis in an acyl-transferase ribozyme. Biochemistry 37, 10118-10125.
    • (1998) Biochemistry , vol.37 , pp. 10118-10125
    • Suga, H.1    Cowan, J.A.2    Szostak, J.W.3
  • 33
    • 0000648758 scopus 로고
    • Fluorine NMR of proteins
    • 33. Gerig, J.T. (1994) Fluorine NMR of proteins. Prog. NMR Spec. 26, 293-370.
    • (1994) Prog. NMR Spec. , vol.26 , pp. 293-370
    • Gerig, J.T.1
  • 35
    • 0028359609 scopus 로고
    • Expression, purification, and crystallization of restriction endonuclease PvuII with DNA containing its recognition site
    • 35. Balendiran, K., Bonventre, J., Knott, R., Jack, W., Benner, J., Schildkraut, I. & Anderson, J.E. (1994) Expression, purification, and crystallization of restriction endonuclease PvuII with DNA containing its recognition site. Proteins 19, 77-79.
    • (1994) Proteins , vol.19 , pp. 77-79
    • Balendiran, K.1    Bonventre, J.2    Knott, R.3    Jack, W.4    Benner, J.5    Schildkraut, I.6    Anderson, J.E.7
  • 36
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • 36. Pace, C.N., Vajdos, F., Fee, L., Grimsley, G. & Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 37
    • 0026628624 scopus 로고
    • EcoRV restriction endonuclease: Communication between catalytic metal ions and DNA recognition
    • 37. Vermote, C.L.M. & Halford, S.E. (1992) EcoRV restriction endonuclease: communication between catalytic metal ions and DNA recognition. Biochemistry 31, 6082-6089.
    • (1992) Biochemistry , vol.31 , pp. 6082-6089
    • Vermote, C.L.M.1    Halford, S.E.2
  • 39
    • 0030896611 scopus 로고    scopus 로고
    • Metal-mediated hydrolysis of biological phosphate esters
    • 38. Cowan, J.A. (1997) Metal-mediated hydrolysis of biological phosphate esters. J. Biol. Inorg. Chem. 2, 168-176.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 168-176
    • Cowan, J.A.1
  • 41
    • 0344277044 scopus 로고
    • Lac repressor: 3-fluorotyrosine substitution for nuclear magnetic resonance studies
    • 40. Lu, P., Jarema, M., Mosser, K. & Daniel, W.E. Jr (1976) Lac repressor: 3-fluorotyrosine substitution for nuclear magnetic resonance studies. Proc. Natl Acad. Sci. USA 73, 3471-3475.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 3471-3475
    • Lu, P.1    Jarema, M.2    Mosser, K.3    Daniel W.E., Jr.4
  • 42
    • 0019569785 scopus 로고
    • Genetic assignment of resonances in the NMR spectrum of a protein: Lac repressor
    • 41. Jarema, M.A., Lu, P. & Miller, J.H. (1981) Genetic assignment of resonances in the NMR spectrum of a protein: lac repressor. Proc. Natl Acad. Sci. USA 78, 2707-2711.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 2707-2711
    • Jarema, M.A.1    Lu, P.2    Miller, J.H.3
  • 43
    • 0017224909 scopus 로고
    • Fluorine-19 nuclear magnetic resonance study of fluorotyrosine alkaline phosphatase: The influence of zinc on protein structure and a conformational change induced by phosphate binding
    • 42. Hull, W.E. & Sykes, B.D. (1976) Fluorine-19 nuclear magnetic resonance study of fluorotyrosine alkaline phosphatase: The influence of zinc on protein structure and a conformational change induced by phosphate binding. Biochemistry 15, 1535-1546.
    • (1976) Biochemistry , vol.15 , pp. 1535-1546
    • Hull, W.E.1    Sykes, B.D.2
  • 45
    • 0031576347 scopus 로고    scopus 로고
    • Conformational transitions and structural deformability of EcoRV endonuclease revealed by crystal-lographic analysis
    • 44. Perona, J.J. & Martin, A.M. (1997) Conformational transitions and structural deformability of EcoRV endonuclease revealed by crystal-lographic analysis. J. Mol. Biol. 273, 207-225.
    • (1997) J. Mol. Biol. , vol.273 , pp. 207-225
    • Perona, J.J.1    Martin, A.M.2
  • 46
    • 0029885422 scopus 로고    scopus 로고
    • Structural adaptations in the interaction of EcoRI endonuclease with methylated GAATTC sites
    • 45. Jen-Jacobson, L., Engler, L.E., Lesser, D.R., Kurpiewski, M.R., Yee, C. & McVerry, B. (1996) Structural adaptations in the interaction of EcoRI endonuclease with methylated GAATTC sites. EMBO J. 15, 2870-2882.
    • (1996) EMBO J. , vol.15 , pp. 2870-2882
    • Jen-Jacobson, L.1    Engler, L.E.2    Lesser, D.R.3    Kurpiewski, M.R.4    Yee, C.5    McVerry, B.6
  • 47
    • 0018980969 scopus 로고
    • The interaction of the EcoRI restriction endonuclease with its substrate
    • 46. Goppelt, M., Pingoud, A., Maass, G., Mayer, H., Koster, H. & Frank, R. (1980) The interaction of the EcoRI restriction endonuclease with its substrate. Eur. J. Biochem. 104, 101-107.
    • (1980) Eur. J. Biochem. , vol.104 , pp. 101-107
    • Goppelt, M.1    Pingoud, A.2    Maass, G.3    Mayer, H.4    Koster, H.5    Frank, R.6
  • 48
    • 0022267976 scopus 로고
    • 19F-Nuelear magnetic resonance studies of fluorotyrosine-labeled aspartate transcarbamoylase
    • 19F-Nuelear magnetic resonance studies of fluorotyrosine-labeled aspartate transcarbamoylase. J. Biol. Chem. 260, 11651-11658.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11651-11658
    • Wacks, D.B.1    Schachman, H.K.2
  • 50
    • 0013283113 scopus 로고
    • Fluorotyrosine alkaline phosphatase from Escherichia coli: Preparation, properties, and fluorine-19 nuclear magnetic resonance
    • 49. Sykes, B.D., Weingarten, H.I. & Schlesinger, M.J. (1974) Fluorotyrosine alkaline phosphatase from Escherichia coli: preparation, properties, and fluorine-19 nuclear magnetic resonance. Proc. Natl Acad. Sci. USA 71, 469-473.
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 469-473
    • Sykes, B.D.1    Weingarten, H.I.2    Schlesinger, M.J.3
  • 51
    • 0028153794 scopus 로고
    • Metallobiochemistry of the magnesium ion: Characterization of the essential metal-binding site in Escherichia coli ribonuclease H
    • 50. Huang, H.-W. & Cowan, J.A. (1994) Metallobiochemistry of the magnesium ion: characterization of the essential metal-binding site in Escherichia coli ribonuclease H. Eur. J. Biochem. 219, 253-260.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 253-260
    • Huang, H.-W.1    Cowan, J.A.2
  • 53
    • 0027732494 scopus 로고
    • Evidence for the role of solvated metal hydroxide in the hammerhead cleavage mechanism
    • 52. Dahm, S.C., Derrick, W.B. & Uhlenbeck, O.C. (1993) Evidence for the role of solvated metal hydroxide in the hammerhead cleavage mechanism. Biochemistry 32, 13040-13045.
    • (1993) Biochemistry , vol.32 , pp. 13040-13045
    • Dahm, S.C.1    Derrick, W.B.2    Uhlenbeck, O.C.3
  • 54
    • 0029168512 scopus 로고
    • Kinetic evidence based on a solvent isotope effects for the nonexistence of a proton-transfer process in reactions catalyzed by a hammerhead ribozyme: Implication to the double metal ion mechanism of catalysis
    • 53. Sawata, S., Komiyama, M. & Taira, K. (1995) Kinetic evidence based on a solvent isotope effects for the nonexistence of a proton-transfer process in reactions catalyzed by a hammerhead ribozyme: implication to the double metal ion mechanism of catalysis. J. Am. Chem. Soc. 117, 2357-2358.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2357-2358
    • Sawata, S.1    Komiyama, M.2    Taira, K.3


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