메뉴 건너뛰기




Volumn 73, Issue 18, 2008, Pages 6960-6969

Dineopentyl phosphate hydrolysis: Evidence for stepwise water attack

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; CATALYSTS; ENZYMES; ESTERIFICATION; ESTERS; FOOD ADDITIVES; FREE ENERGY; HYDROCARBONS; HYDROLYSIS; ORGANIC COMPOUNDS; PROTEINS; PROTON TRANSFER; PROTONS; RATE CONSTANTS;

EID: 52449134610     PISSN: 00223263     EISSN: None     Source Type: Journal    
DOI: 10.1021/jo801207q     Document Type: Article
Times cited : (46)

References (68)
  • 2
    • 33748591572 scopus 로고    scopus 로고
    • Enzymatic Mechanisms of Phosphate and Sulfate Transfer
    • Cleland, W. W.; Hengge, A. C. Enzymatic Mechanisms of Phosphate and Sulfate Transfer. Chem. Rev. 2006, 106, 3252-3278.
    • (2006) Chem. Rev , vol.106 , pp. 3252-3278
    • Cleland, W.W.1    Hengge, A.C.2
  • 3
    • 11744329951 scopus 로고
    • Mechanisms of Nucleophilic Substitution in Phosphate Esters
    • Cor, J. R., Jr.; Ramsey, O. B. Mechanisms of Nucleophilic Substitution in Phosphate Esters. Chem. Rev. 1964, 64, 317-352.
    • (1964) Chem. Rev , vol.64 , pp. 317-352
    • Cor Jr., J.R.1    Ramsey, O.B.2
  • 5
    • 0018657633 scopus 로고
    • The Role of Metals in Enzyme-Catalyzed Substitutions at Each of the Phosphorous Atoms of ATP
    • Mildvan, A. S. The Role of Metals in Enzyme-Catalyzed Substitutions at Each of the Phosphorous Atoms of ATP. Adv. Enzymol. Relat. Areas Mol. Biol. 1979, 49, 103-126.
    • (1979) Adv. Enzymol. Relat. Areas Mol. Biol , vol.49 , pp. 103-126
    • Mildvan, A.S.1
  • 6
    • 0033511228 scopus 로고    scopus 로고
    • Nucleoside Triphosphate-Binding Proteins: Different Scaffolds to Achieve Phosphoryl Transfer
    • Vetter, I. R.; Wittinghofer, A. Nucleoside Triphosphate-Binding Proteins: Different Scaffolds to Achieve Phosphoryl Transfer. Q. Rev. Biophys. 1999, 32, 1-56.
    • (1999) Q. Rev. Biophys , vol.32 , pp. 1-56
    • Vetter, I.R.1    Wittinghofer, A.2
  • 7
    • 51249090160 scopus 로고
    • Monomeric Metaphosphates
    • Westheimer, F. H. Monomeric Metaphosphates. Chem. Rev. 1981, 64, 317-352.
    • (1981) Chem. Rev , vol.64 , pp. 317-352
    • Westheimer, F.H.1
  • 9
    • 84961974064 scopus 로고    scopus 로고
    • Computer Simulations of the Chemical Catalysis of DNA Polymerases: Discriminating between Alternative Nucleotide Insertion Mechanisms for T7 DNA Polymerase
    • Florián, J.; Goodman, M. F.; Warshel, A. Computer Simulations of the Chemical Catalysis of DNA Polymerases: Discriminating between Alternative Nucleotide Insertion Mechanisms for T7 DNA Polymerase. J. Am. Chem. Soc. 2003, 125, 8163-8177.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 8163-8177
    • Florián, J.1    Goodman, M.F.2    Warshel, A.3
  • 10
    • 18744402486 scopus 로고    scopus 로고
    • Computer Simulations of Protein Functions: Searching for the Molecular Origin of the Replication Fidelity of DNA Polymerases
    • Florián, J.; Goodman, M. F.; Warshel, A. Computer Simulations of Protein Functions: Searching for the Molecular Origin of the Replication Fidelity of DNA Polymerases. Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 6819-6824.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 6819-6824
    • Florián, J.1    Goodman, M.F.2    Warshel, A.3
  • 11
    • 33745052090 scopus 로고    scopus 로고
    • Simulating the Effect of DNA Polymerase Mutations on Transition State Energetics and Fidelity: Evaluations Amino Acid Group Contributions and Allosteric Coupling for Ionized Residues in Human pol beta
    • Xiang, Y.; Oelschlager, P.; Florián, J.; Goodman, M. F.; Warshel, A. Simulating the Effect of DNA Polymerase Mutations on Transition State Energetics and Fidelity: Evaluations Amino Acid Group Contributions and Allosteric Coupling for Ionized Residues in Human pol beta. Biochemistry 2006, 45, 7036-7048.
    • (2006) Biochemistry , vol.45 , pp. 7036-7048
    • Xiang, Y.1    Oelschlager, P.2    Florián, J.3    Goodman, M.F.4    Warshel, A.5
  • 13
    • 34247549227 scopus 로고    scopus 로고
    • A Water-Mediated and Substrate-Assisted Catalytic Mechanism for Sulfolobus Solfataricus and DNA Polymerase IV
    • Wang, L.; Yu, X.; Hu, P.; Broyde, S.; Zhang, Y. A Water-Mediated and Substrate-Assisted Catalytic Mechanism for Sulfolobus Solfataricus and DNA Polymerase IV. J. Am. Chem. Soc. 2007, 129, 4731-4737.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 4731-4737
    • Wang, L.1    Yu, X.2    Hu, P.3    Broyde, S.4    Zhang, Y.5
  • 14
    • 0028049441 scopus 로고
    • Structures of Ternary Complexes of Rat DNA Polymerase beta, a DNA Template-Primer and ddCTP
    • Petellier, H.; Sawaya, M. R.; Kumar, A.; Wilson, S. H.; Kraut, J. Structures of Ternary Complexes of Rat DNA Polymerase beta, a DNA Template-Primer and ddCTP. Science 1994, 264, 1893-1903.
    • (1994) Science , vol.264 , pp. 1893-1903
    • Petellier, H.1    Sawaya, M.R.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 16
    • 52449084675 scopus 로고    scopus 로고
    • Bunton, C. A.; Mhala, M. M.; Oldham, K. G.; vernon, C. A. The Reactions of Organic Phosphates. J. Chem. Soc. 1960, 329, 3-3301.
    • Bunton, C. A.; Mhala, M. M.; Oldham, K. G.; vernon, C. A. The Reactions of Organic Phosphates. J. Chem. Soc. 1960, 329, 3-3301.
  • 18
    • 37049128024 scopus 로고
    • The Reactivity of Phosphate Esters
    • Kirby, J. A.; Younas, M. The Reactivity of Phosphate Esters. J. Chem. Soc. B. 1970, 51, 0-513.
    • (1970) J. Chem. Soc. B , vol.51 , pp. 0-513
    • Kirby, J.A.1    Younas, M.2
  • 19
    • 0028918401 scopus 로고
    • A Proficient Enzyme
    • Radzicka, A.; Wolfenden, R. A Proficient Enzyme. Science 1995, 267, 90-93.
    • (1995) Science , vol.267 , pp. 90-93
    • Radzicka, A.1    Wolfenden, R.2
  • 20
    • 0032481372 scopus 로고    scopus 로고
    • Spontaneous Hydrolysis of Ionised Phosphate Monoesters and Diesters and the Proficiencies of the Phosphatases and Phosphodiesterases As Catalysts
    • Wolfenden, R.; Ridgeway, C.; Young, G. Spontaneous Hydrolysis of Ionised Phosphate Monoesters and Diesters and the Proficiencies of the Phosphatases and Phosphodiesterases As Catalysts. J. Am. Chem. Soc. 1998, 120, 833-834.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 833-834
    • Wolfenden, R.1    Ridgeway, C.2    Young, G.3
  • 21
    • 0030724727 scopus 로고    scopus 로고
    • Mechanisms of Signaling and Related Enzymes
    • Mildvan, A. S. Mechanisms of Signaling and Related Enzymes. Proteins: Structure, Function Genet. 1997, 29, 401-416.
    • (1997) Proteins: Structure, Function Genet , vol.29 , pp. 401-416
    • Mildvan, A.S.1
  • 22
    • 0024309235 scopus 로고
    • Calculations of Free Energy Profiles for the Staphylococcal Nuclease Catalysed Reaction
    • Aqvist, J.; Warshel, A. Calculations of Free Energy Profiles for the Staphylococcal Nuclease Catalysed Reaction. Biochemistry 1989, 28, 4680-4689.
    • (1989) Biochemistry , vol.28 , pp. 4680-4689
    • Aqvist, J.1    Warshel, A.2
  • 23
    • 33748633480 scopus 로고    scopus 로고
    • Warshel, A.; Sharma, P. K.; Kato, M.; Xiang, Y.; Liu, H.; Olsson, M. H. Electrostatic Basis for Enzyme Catalysis. Chem. Rev. 2006, 106, 3210-3235.
    • Warshel, A.; Sharma, P. K.; Kato, M.; Xiang, Y.; Liu, H.; Olsson, M. H. Electrostatic Basis for Enzyme Catalysis. Chem. Rev. 2006, 106, 3210-3235.
  • 24
    • 11944269619 scopus 로고
    • Structure energy analysis of the role of metal ions in phosphodiester bond hydrolysis by DNA Polymerase I
    • Fothergill, M.; Goodman, M. F.; Petruska, J.; Warshel, A. Structure energy analysis of the role of metal ions in phosphodiester bond hydrolysis by DNA Polymerase I. J. Am. Chem. Soc. 1995, 117, 11619-11627.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 11619-11627
    • Fothergill, M.1    Goodman, M.F.2    Petruska, J.3    Warshel, A.4
  • 25
    • 0038286174 scopus 로고    scopus 로고
    • The Rate of Hydrolysis of Phosphomonoester Dianions and the Exceptional Catalytic Proficiencies of Protein and Inositol Phosphatases
    • Lad, C.; Williams, N. H.; Wolfenden, R. The Rate of Hydrolysis of Phosphomonoester Dianions and the Exceptional Catalytic Proficiencies of Protein and Inositol Phosphatases. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 5607-5610.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 5607-5610
    • Lad, C.1    Williams, N.H.2    Wolfenden, R.3
  • 26
    • 33748592810 scopus 로고    scopus 로고
    • Degrees of Difficulty of Water-Consuming Reactions in the Absence of Enzymes
    • Wolfenden, R. Degrees of Difficulty of Water-Consuming Reactions in the Absence of Enzymes. Chem. Rev. 2006, 106, 3379-3396.
    • (2006) Chem. Rev , vol.106 , pp. 3379-3396
    • Wolfenden, R.1
  • 27
    • 33845198350 scopus 로고    scopus 로고
    • On the Mechanism of Hydrolysis of Phosphate Monoester Dianions in Solution and Proteins
    • Klahn, M.; Rosta, E.; Warshel, A. On the Mechanism of Hydrolysis of Phosphate Monoester Dianions in Solution and Proteins. J. Am. Chem. Soc. 2006, 128, 15310-15323.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 15310-15323
    • Klahn, M.1    Rosta, E.2    Warshel, A.3
  • 28
    • 0026713142 scopus 로고
    • On the Mechanism of Guanosine Triphosphate Hydrolysis in ras p21 Proteins
    • Langen, R.; Schweins, T.; Warshel, A. On the Mechanism of Guanosine Triphosphate Hydrolysis in ras p21 Proteins. Biochemistry 1992, 31, 8691-8696.
    • (1992) Biochemistry , vol.31 , pp. 8691-8696
    • Langen, R.1    Schweins, T.2    Warshel, A.3
  • 29
    • 0024463212 scopus 로고
    • Structure of the Guanine-Nucleotide Binding Domain of the Ha-ras Oncogene Produced p21 in the Triphosphate Conformation
    • Pai, E. F.; Kabsch, W.; Krengel, U.; Holmes, K.; John, J.; Wittinghofer, A. Structure of the Guanine-Nucleotide Binding Domain of the Ha-ras Oncogene Produced p21 in the Triphosphate Conformation. Nature 1989, 341, 209-214.
    • (1989) Nature , vol.341 , pp. 209-214
    • Pai, E.F.1    Kabsch, W.2    Krengel, U.3    Holmes, K.4    John, J.5    Wittinghofer, A.6
  • 30
    • 0025310575 scopus 로고
    • Refined Crystal Structure of the Triphosphate Conformation of H-ras p21 at 1.35A Resolution: Implications for the Mechanism of GTP Hydrolysis
    • Pai, E. F.; Krengel, U.; Petsko, G. A.; Goody, R. S.; Kabsch, W.; Wittinghofer, A. Refined Crystal Structure of the Triphosphate Conformation of H-ras p21 at 1.35A Resolution: Implications for the Mechanism of GTP Hydrolysis. EMBO J. 1990, 9, 2351-2359.
    • (1990) EMBO J , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsch, W.5    Wittinghofer, A.6
  • 31
    • 0028464366 scopus 로고
    • Why Have Mutagenesis Studies Not Located the General Base in ras p21
    • Schweins, T.; Langen, R.; Warshel, A. Why Have Mutagenesis Studies Not Located the General Base in ras p21. Nat. Struct. Biol. 1994, 1, 476-484.
    • (1994) Nat. Struct. Biol , vol.1 , pp. 476-484
    • Schweins, T.1    Langen, R.2    Warshel, A.3
  • 33
    • 0034663856 scopus 로고    scopus 로고
    • How Does GAP Catalyse the GTPase Reaction of Ras? A Computer Simulation Study
    • Glennon, T. M.; Villa, J.; Warshel, A. How Does GAP Catalyse the GTPase Reaction of Ras? A Computer Simulation Study. Biochemistry 2000, 39, 9641-9651.
    • (2000) Biochemistry , vol.39 , pp. 9641-9651
    • Glennon, T.M.1    Villa, J.2    Warshel, A.3
  • 34
    • 1442324695 scopus 로고    scopus 로고
    • Why Does the Ras Switch "Break" by Oncogenic Mutations
    • Shurki, A.; Warshel, A. Why Does the Ras Switch "Break" by Oncogenic Mutations. Proteins 2004, 55, 1-10.
    • (2004) Proteins , vol.55 , pp. 1-10
    • Shurki, A.1    Warshel, A.2
  • 35
    • 0029825324 scopus 로고    scopus 로고
    • Linear Free Energy Relationships in the Intrinsic and Gtpase Activating Protein-Stimulated Guanosine 5′-Triphosphate Hydrolysis of p21 ras
    • Schweins, T.; Geyer, M.; Kalbitzer, H. R.; Wittinghofer, A.; Warshel, A. Linear Free Energy Relationships in the Intrinsic and Gtpase Activating Protein-Stimulated Guanosine 5′-Triphosphate Hydrolysis of p21 ras. Biochemistry 1996, 35, 14225-14231.
    • (1996) Biochemistry , vol.35 , pp. 14225-14231
    • Schweins, T.1    Geyer, M.2    Kalbitzer, H.R.3    Wittinghofer, A.4    Warshel, A.5
  • 36
    • 0029410712 scopus 로고
    • Mapping the Transition State for ATP Hydrolysis: Implications for Enzymatic Catalysis
    • Admiraal, S. J.; Herschlag, D. Mapping the Transition State for ATP Hydrolysis: Implications for Enzymatic Catalysis. Chem. Biol. 1995, 2, 729-739.
    • (1995) Chem. Biol , vol.2 , pp. 729-739
    • Admiraal, S.J.1    Herschlag, D.2
  • 37
    • 0034654214 scopus 로고    scopus 로고
    • Admiraal, S. J.; Herschlag, D. The Substrate-Assisted General Base Catalysis Model for Phosphate Monoester Hydrolysis: Evaluation Using Reactivity Comparisons. J. Am. Chem. Soc. 2000, 122, 2145-2148.
    • Admiraal, S. J.; Herschlag, D. The Substrate-Assisted General Base Catalysis Model for Phosphate Monoester Hydrolysis: Evaluation Using Reactivity Comparisons. J. Am. Chem. Soc. 2000, 122, 2145-2148.
  • 38
    • 0029781354 scopus 로고    scopus 로고
    • Ras-Catalyzed Hydrolysis of GTP: A New Perspective from Model Studies
    • Maegley, K. A.; Admiraal, S. J.; Herschlag, D. Ras-Catalyzed Hydrolysis of GTP: A New Perspective from Model Studies. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 8160-8166.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 8160-8166
    • Maegley, K.A.1    Admiraal, S.J.2    Herschlag, D.3
  • 39
    • 0029843561 scopus 로고    scopus 로고
    • Mechanistic Analysis of the Observed Linear Free Energy Relationships in p21ras and Related Systems
    • Schweins, T.; Warshel, A. Mechanistic Analysis of the Observed Linear Free Energy Relationships in p21ras and Related Systems. Biochemistry 1996, 35, 14232-14243.
    • (1996) Biochemistry , vol.35 , pp. 14232-14243
    • Schweins, T.1    Warshel, A.2
  • 40
    • 29244455678 scopus 로고    scopus 로고
    • Computational Study of a Transition State Analogue of Phosphoryl Transfer in the Ras-RasGAP Complex: AlFx versus MgF
    • Grigorenko, B.; Nemukhin, A. V.; Cachau, R. E.; Topol, I. A.; Burt, S. K. Computational Study of a Transition State Analogue of Phosphoryl Transfer in the Ras-RasGAP Complex: AlFx versus MgF. J. Phys. Chem. B. 2006, 11, 503-508.
    • (2006) J. Phys. Chem. B , vol.11 , pp. 503-508
    • Grigorenko, B.1    Nemukhin, A.V.2    Cachau, R.E.3    Topol, I.A.4    Burt, S.K.5
  • 41
    • 0027405662 scopus 로고
    • Probing the Structure and Mechanism of Ras Protein with an Expanded Genetic Code
    • Chung, H. H.; Benson, D. R.; Schultz, P. G. Probing the Structure and Mechanism of Ras Protein with an Expanded Genetic Code. Science 1993, 5, 806-809.
    • (1993) Science , vol.5 , pp. 806-809
    • Chung, H.H.1    Benson, D.R.2    Schultz, P.G.3
  • 42
    • 52449120294 scopus 로고    scopus 로고
    • Florian, J.; Warshel, A. A Fundamental Assumption about OH-Attack in Phosphate Hydrolysis Is Not Fully Justified. J. Am. Chem. Soc. 1997, 119, 4458-4472.
    • Florian, J.; Warshel, A. A Fundamental Assumption about OH-Attack in Phosphate Hydrolysis Is Not Fully Justified. J. Am. Chem. Soc. 1997, 119, 4458-4472.
  • 45
    • 0024827420 scopus 로고
    • Effective Charge Distrtibution for Attack of Phenoxide Ion on Aryl Methyl Phosphate Monoanion: Studies Related to the Action of Ribonuclease
    • Ba-Saif, S. A.; Davis, A. M.; Williams, A. J. Effective Charge Distrtibution for Attack of Phenoxide Ion on Aryl Methyl Phosphate Monoanion: Studies Related to the Action of Ribonuclease. J. Org. Chem. 1989, 54, 5483-5486.
    • (1989) J. Org. Chem , vol.54 , pp. 5483-5486
    • Ba-Saif, S.A.1    Davis, A.M.2    Williams, A.J.3
  • 46
    • 0001603966 scopus 로고
    • Transition-State Structural Variation and Mechanistic Change
    • Barnes, J. A.; Wilkie, J.; Williams, I. H. Transition-State Structural Variation and Mechanistic Change. J. Chem. Soc., Faraday Trans. 1994, 90, 1709-1714.
    • (1994) J. Chem. Soc., Faraday Trans , vol.90 , pp. 1709-1714
    • Barnes, J.A.1    Wilkie, J.2    Williams, I.H.3
  • 47
    • 31944441501 scopus 로고    scopus 로고
    • Alkaline Phosphatases Mono- and Diesterase Reactions: Comparative Transition State Analysis
    • Zalatan, J. G.; Herschlag, D. Alkaline Phosphatases Mono- and Diesterase Reactions: Comparative Transition State Analysis. J. Am. Chem. Soc. 2006, 128, 1293-1303.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 1293-1303
    • Zalatan, J.G.1    Herschlag, D.2
  • 48
    • 0032547320 scopus 로고    scopus 로고
    • Reactivity of Phosphate Diesters Doubly Coordinated to a Dinuclear Cobalt(Iii) Complex: Dependence of the Reactivity on the Basicity of the Leaving Group
    • Williams, N. H.; Cheung, J.; Chin, J. Reactivity of Phosphate Diesters Doubly Coordinated to a Dinuclear Cobalt(Iii) Complex: Dependence of the Reactivity on the Basicity of the Leaving Group. J. Am. Chem. Soc. 1998, 120, 8079-8087.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 8079-8087
    • Williams, N.H.1    Cheung, J.2    Chin, J.3
  • 49
    • 33645212804 scopus 로고    scopus 로고
    • The Time Required for Water Attack at the Phosphorus Atom of Simple Phosphodiesters and of DNA
    • Schroeder, G. K.; Lad, C.; Wyman, P.; Williams, N. H.; Wolfenden, R. The Time Required for Water Attack at the Phosphorus Atom of Simple Phosphodiesters and of DNA. Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 4052-4055.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 4052-4055
    • Schroeder, G.K.1    Lad, C.2    Wyman, P.3    Williams, N.H.4    Wolfenden, R.5
  • 51
    • 84961976175 scopus 로고    scopus 로고
    • Theoretical Studies of the Hydroxide-Catalyzed P-O Cleavage Reactions of Neutral Phosphate Triesters and Diesters in Aqeuous Solution: Examination of the Changes Induced by H/Me substitution
    • Iché-Tarrat, N.; Barthelat, J.-C.; Rinaldi, D.; Vigroux, A. Theoretical Studies of the Hydroxide-Catalyzed P-O Cleavage Reactions of Neutral Phosphate Triesters and Diesters in Aqeuous Solution: Examination of the Changes Induced by H/Me substitution. J. Phys. Chem. B 2005, 109, 22570-225800.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 22570-225800
    • Iché-Tarrat, N.1    Barthelat, J.-C.2    Rinaldi, D.3    Vigroux, A.4
  • 52
    • 3042520570 scopus 로고
    • A Primer for the bema Hapothle. An Empirical Approach to the Characterization of Changing Transition-State Structures
    • Jencks, W. P. A Primer for the bema Hapothle. An Empirical Approach to the Characterization of Changing Transition-State Structures. Chem. Rev. 1985, 85, 511-527.
    • (1985) Chem. Rev , vol.85 , pp. 511-527
    • Jencks, W.P.1
  • 53
    • 1542331187 scopus 로고
    • Relationships between E2 and E1cB Mechanisms of beta-Elimination
    • More O'Ferrall, R. A. Relationships between E2 and E1cB Mechanisms of beta-Elimination. J. Chem. Soc. B 1970, 274-277.
    • (1970) J. Chem. Soc. B , pp. 274-277
    • More O'Ferrall, R.A.1
  • 54
    • 34250773963 scopus 로고    scopus 로고
    • The Role of Metal Ions in Phosphate Ester Hydrolysis
    • Kamerlin, S. C. L.; Wilkie, J. The Role of Metal Ions in Phosphate Ester Hydrolysis. Org. Biomol. Chem. 2007, 5, 2098-2108.
    • (2007) Org. Biomol. Chem , vol.5 , pp. 2098-2108
    • Kamerlin, S.C.L.1    Wilkie, J.2
  • 55
    • 52449085464 scopus 로고    scopus 로고
    • Frisch, M. J, Trucks, G. W, Schlegel, H. B, Scuseria, G. E, Robb, M. A, Cheeseman, J. R, Montgomery, J, J. A, Vreven, T, Kudin, K. N, Burant, J. C, Millam, J. M, Iyengar, S. S, Tomasi, J, Barone, V, Mennucci, B, Cossi, M, Scalmani, G, Rega, N, Petersson, G. A, Nakatsuji, M, Hada, M, Ehara, K, Toyota, R, Fukuda, J, Hasegawa, M, Ishida, T, Nakajima, Y, Honda, Y, Kitao, O, Nakai, H, Klene, M, Li, X, Knox, J. E, Hratchian, H. P, Cross, J. B, Adacmo, C, Jaramillo, J, Gomperts, R, Stratmann, R. E, Yazyev, O, Austin, A. J, Cammi, R, Pomelli, C, Ochterski, J, Ayala, P. Y, Morokuma, K, Voth, G. A, Salvador, P, Dannenberg, J. J, Zakrzewski, V. G, Dapprich, S, Daniels, A. D, Strain, M. C, Farkas, Ö, Malick, D. K, Rabuck, A. D, Clifford, K, Cioslowki, J, Stefanov, B. B, Liu, G, Liashenko, A, Piskorz, P, Komaromi, I, Martin, R. L, Fox, D. J, Keith, T, Al-Laham, M. A, Peng, C. Y, Nanayakkara, A, Challacombe, M, Gill, P. M. W
    • Frisch, M. J.; Trucks, G. W.; Schlegel, H. B.; Scuseria, G. E.; Robb, M. A.; Cheeseman, J. R.; Montgomery, J., J. A.; Vreven, T.; Kudin, K. N.; Burant, J. C.; Millam, J. M.; Iyengar, S. S.; Tomasi, J.; Barone, V.; Mennucci, B.; Cossi, M.; Scalmani, G.; Rega, N.; Petersson, G. A.; Nakatsuji, M.; Hada, M.; Ehara, K.; Toyota, R.; Fukuda, J.; Hasegawa, M.; Ishida, T.; Nakajima, Y.; Honda, Y.; Kitao, O.; Nakai, H.; Klene, M.; Li, X.; Knox, J. E.; Hratchian, H. P.; Cross, J. B.; Adacmo, C.; Jaramillo, J.; Gomperts, R.; Stratmann, R. E.; Yazyev, O.; Austin, A. J.; Cammi, R.; Pomelli, C.; Ochterski, J.; Ayala, P. Y.; Morokuma, K.; Voth, G. A.; Salvador, P.; Dannenberg, J. J.; Zakrzewski, V. G.; Dapprich, S.; Daniels, A. D.; Strain, M. C.; Farkas, Ö.; Malick, D. K.; Rabuck, A. D.; Clifford, K.; Cioslowki, J.; Stefanov, B. B.; Liu, G.; Liashenko, A.; Piskorz, P.; Komaromi, I.; Martin, R. L.; Fox, D. J.; Keith, T.; Al-Laham, M. A.; Peng, C. Y.; Nanayakkara, A.; Challacombe, M.; Gill, P. M. W.; Johnson, B. G.; Chen, W.; Wong, M. W.; Gonzalez, C.; Pople, J. A., GAUSSIAN 03 (Revision C.02); Gaussian: Pittsburgh, PA, 2004.
  • 56
    • 0000189651 scopus 로고
    • The Role of Exact Exchange
    • Becke, A. D., III. The Role of Exact Exchange. J. Chem. Phys. 1993, 98, 5648-5652.
    • (1993) J. Chem. Phys , vol.98 , pp. 5648-5652
    • Becke III, A.D.1
  • 57
    • 84961985847 scopus 로고    scopus 로고
    • Quantum Calculation of Molecular Energies and Energy Gradients in Solution by a Conductor Solvent Model
    • Barone, V.; Cossi, M. Quantum Calculation of Molecular Energies and Energy Gradients in Solution by a Conductor Solvent Model. J. Phys. Chem. A 1998, 102, 1995-2001.
    • (1998) J. Phys. Chem. A , vol.102 , pp. 1995-2001
    • Barone, V.1    Cossi, M.2
  • 58
    • 84961980743 scopus 로고
    • COSMO: A New Approach to Dielectric Screening in Solvents with Explicit Expressions for the Screening Energy and Its Gradient
    • Klamt, A.; Schüürmann, G. J. COSMO: a New Approach to Dielectric Screening in Solvents with Explicit Expressions for the Screening Energy and Its Gradient. J. Chem. Soc., Perkin Trans. 2 1993, 5, 799-805.
    • (1993) J. Chem. Soc., Perkin Trans. 2 , vol.5 , pp. 799-805
    • Klamt, A.1    Schüürmann, G.J.2
  • 59
    • 0030453048 scopus 로고    scopus 로고
    • Multidimensional Marcus Theory: An Analysis of Concerted Reactions
    • Guthrie, J. P. Multidimensional Marcus Theory: An Analysis of Concerted Reactions. J. Am. Chem. Soc. 1996, 118, 12878-12885.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 12878-12885
    • Guthrie, J.P.1
  • 60
    • 33748336069 scopus 로고    scopus 로고
    • Transition State Analogues for Nucleotidyl Transfer Reactions: Structure and Stability of Pentavalent Vanadate and Phosphate Ester Dianions
    • Borden, J.; Crans, D. C.; Florián, J. Transition State Analogues for Nucleotidyl Transfer Reactions: Structure and Stability of Pentavalent Vanadate and Phosphate Ester Dianions. J. Phys. Chem. B. 2006, 110, 14988-14999.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 14988-14999
    • Borden, J.1    Crans, D.C.2    Florián, J.3
  • 61
    • 23944472625 scopus 로고    scopus 로고
    • What Are the Roles of Substrate Assisted Catalysis and Proximity Effects in Peptide Bond Formation by the Ribosome
    • Sharma, P. K.; Xiang, Y.; Kato, M.; Warshel, A. What Are the Roles of Substrate Assisted Catalysis and Proximity Effects in Peptide Bond Formation by the Ribosome. Biochemistry 2005, 44, 11307-11314.
    • (2005) Biochemistry , vol.44 , pp. 11307-11314
    • Sharma, P.K.1    Xiang, Y.2    Kato, M.3    Warshel, A.4
  • 62
    • 0000997465 scopus 로고    scopus 로고
    • Calculation of Activation Entropies of Chemical Reactions in Solution
    • Strajbl, M.; Sham, Y. Y.; Villa, J.; Chu, Z. T.; Warshel, A. Calculation of Activation Entropies of Chemical Reactions in Solution. J. Phys. Chem. B. 2000, 104, 4578-4584.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 4578-4584
    • Strajbl, M.1    Sham, Y.Y.2    Villa, J.3    Chu, Z.T.4    Warshel, A.5
  • 63
    • 0000961995 scopus 로고
    • Evaluation of the Configurational Entropy for Proteins - Application to Molecular Dynamics Simulations of an Alpha-Helix
    • Levy, R.; Karplus, M.; Kuschisk, J.; Perahia, D. Evaluation of the Configurational Entropy for Proteins - Application to Molecular Dynamics Simulations of an Alpha-Helix. Macromolecules 1984, 17, 1370-1374.
    • (1984) Macromolecules , vol.17 , pp. 1370-1374
    • Levy, R.1    Karplus, M.2    Kuschisk, J.3    Perahia, D.4
  • 64
    • 0000728542 scopus 로고
    • Microscopic and Semimicroscopic Calculations of Electrostatic Energies in Proteins by the POLARIS and ENZYMIX Programs
    • Lee, F. S.; Chu, Z. T.; Warshel, A. Microscopic and Semimicroscopic Calculations of Electrostatic Energies in Proteins by the POLARIS and ENZYMIX Programs. J. Comput. Chem. 1993, 14, 161-185.
    • (1993) J. Comput. Chem , vol.14 , pp. 161-185
    • Lee, F.S.1    Chu, Z.T.2    Warshel, A.3
  • 66
    • 0035928522 scopus 로고    scopus 로고
    • Base Catalysed Phosphate Diester Hydrolysis
    • Williams, N. H.; Wyman, P. Base Catalysed Phosphate Diester Hydrolysis. Chem. Commun. 2001, 1268-1269.
    • (2001) Chem. Commun , pp. 1268-1269
    • Williams, N.H.1    Wyman, P.2
  • 67
    • 41149118457 scopus 로고    scopus 로고
    • On the Interpretation of the Observed LFER in Phosphate Hydrolysis: A Thorough Computational Study of Phosphate Diester Hydrolysis in Solution
    • Rosta, E.; Kamerlin, S. C. L.; Warshel, A. On the Interpretation of the Observed LFER in Phosphate Hydrolysis: A Thorough Computational Study of Phosphate Diester Hydrolysis in Solution. Biochemistry 2008, 47, 3725-3735.
    • (2008) Biochemistry , vol.47 , pp. 3725-3735
    • Rosta, E.1    Kamerlin, S.C.L.2    Warshel, A.3
  • 68
    • 0034286430 scopus 로고    scopus 로고
    • Fragmentation of Methyl Hydrogen Alpha-Hydroxyiminophosphonates - Kinetics, Mechanism and the Question of Metaphosphate Formation
    • Katzhenlder, J.; Schneider, H.; Ta-Shma, R.; Breuer, E. Fragmentation of Methyl Hydrogen Alpha-Hydroxyiminophosphonates - Kinetics, Mechanism and the Question of Metaphosphate Formation. J. Chem. Soc., Perkin. Trans. 2 2000, 1961-1968.
    • (2000) J. Chem. Soc., Perkin. Trans. 2 , pp. 1961-1968
    • Katzhenlder, J.1    Schneider, H.2    Ta-Shma, R.3    Breuer, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.