메뉴 건너뛰기




Volumn 4, Issue , 2007, Pages 1209-1239

The Quantum Kramers Approach to Enzymatic Hydrogen Transfer - Protein Dynamics as it Couples to Catalysis

Author keywords

Alcohol dehydrogenase; Biological aspects; Catalysis; Derivation of Quantum Kramers method; Dynamics of hydrogen transfer; Electronic polarization; Enzymatic hydrogen transfer; Lactate dehydrogenase; Promoting vibrations; Protein dynamics; Proton coupled electron transfer; Quantum Kramers approach; Quantum tunneling

Indexed keywords


EID: 84891297024     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527611546.ch38     Document Type: Chapter
Times cited : (4)

References (103)
  • 1
    • 0000421878 scopus 로고
    • Nature of forces between large molecules of biological interest
    • L. Pauling, Nature of forces between large molecules of biological interest, Nature 161, 707-709 (1948).
    • (1948) Nature , vol.161 , pp. 707-709
    • Pauling, L.1
  • 2
    • 0032860328 scopus 로고    scopus 로고
    • Enzymatic Transition State Analysis and Transition-State Analogues
    • V. L. Schramm, ''Enzymatic Transition State Analysis and Transition-State Analogues, Methods Enzymol. 308, 301-354 (1999);
    • (1999) Methods Enzymol , vol.308 , pp. 301-354
    • Schramm, V.L.1
  • 4
    • 0035859446 scopus 로고    scopus 로고
    • Internal Enzyme Motions as a Source of Catalytic Activity: Rate Promoting Vibrations and Hydrogen Tunneling
    • D. Antüniüu, S. D. Schwartz, Internal Enzyme Motions as a Source of Catalytic Activity: Rate Promoting Vibrations and Hydrogen Tunneling, J. Phys. Chem. B, 105, 5553-5558 (2001).
    • (2001) J. Phys. Chem. B , vol.105 , pp. 5553-5558
    • Antüniüu, D.1    Schwartz, S.D.2
  • 5
    • 0001378703 scopus 로고    scopus 로고
    • Quantum Activated Rates-An Evolution Operator Approach
    • S. D. Schwartz, Quantum Activated Rates-An Evolution Operator Approach, J. Chem. Phys., 105, 6871-6879 (1996);
    • (1996) J. Chem. Phys , vol.105 , pp. 6871-6879
    • Schwartz, S.D.1
  • 6
    • 0031209362 scopus 로고    scopus 로고
    • Quantum Reaction in a Condensed Phase-Turnover Behavior from New Adiabatic Factorizations and Corrections
    • S. D. Schwartz, Quantum Reaction in a Condensed Phase-Turnover Behavior from New Adiabatic Factorizations and Corrections, J. Chem. Phys., 107, 2424-2429 (1997).
    • (1997) J. Chem. Phys , vol.107 , pp. 2424-2429
    • Schwartz, S.D.1
  • 7
    • 0000320320 scopus 로고    scopus 로고
    • Transition pathways in many body systems: application to hydrogen bond breaking in water
    • F. S. Csajka, D. Chandler, Transition pathways in many body systems: application to hydrogen bond breaking in water, J. Chem. Phys., 109, 1125-1133 (1998);
    • (1998) J. Chem. Phys , vol.109 , pp. 1125-1133
    • Csajka, F.S.1    Chandler, D.2
  • 8
    • 2742515916 scopus 로고    scopus 로고
    • Sampling ensembles of deterministic pathways
    • P. G. Bülhuis, C. Dellagü, D. Chandler, Sampling ensembles of deterministic pathways, Faraday Discuss., 110, 421-436 (1998);
    • (1998) Faraday Discuss , vol.110 , pp. 421-436
    • Bülhuis, P.G.1    Dellagü, C.2    Chandler, D.3
  • 10
    • 0001167624 scopus 로고
    • Molecular Dynamics Study of an Isomerizing Diatomic in a Lennard-Jones Fluid
    • J. E. Straub, M. Borkovec, B. J. Berne, Molecular Dynamics Study of an Isomerizing Diatomic in a Lennard-Jones Fluid, J. Chem. Phys., 89, 4833 (1988);
    • (1988) J. Chem. Phys , vol.89 , pp. 4833
    • Straub, J.E.1    Borkovec, M.2    Berne, B.J.3
  • 11
    • 2742571961 scopus 로고
    • Nonequilibrium Solvation Effects on Reaction Rates for Model SN2 Reactions in Water
    • B. J. Gertner, K. R. Wilson, J. T. Hynes, Nonequilibrium Solvation Effects on Reaction Rates for Model SN2 Reactions in Water, J. Chem. Phys., 90, 3537 (1988).
    • (1988) J. Chem. Phys , vol.90 , pp. 3537
    • Gertner, B.J.1    Wilson, K.R.2    Hynes, J.T.3
  • 12
    • 36549101755 scopus 로고
    • On the Generalized Langevin Equation: Classical and Quantum Mechanical
    • E. Cortes, B. J. West, K. Lindenberg, On the Generalized Langevin Equation: Classical and Quantum Mechanical, J. Chem. Phys., 82, 2708-2717 (1985).
    • (1985) J. Chem. Phys , vol.82 , pp. 2708-2717
    • Cortes, E.1    West, B.J.2    Lindenberg, K.3
  • 13
    • 18844402460 scopus 로고
    • The nonlinear Generalized Langevin Equation
    • R. ZwaNziG, The nonlinear Generalized Langevin Equation, J. Stat. Phys., 9, 215 (1973);
    • (1973) J. Stat. Phys , vol.9 , pp. 215
    • ZwaNziG, R.1
  • 15
    • 0009750748 scopus 로고
    • Accurate Quantum Mechanics From High Order Resumed Operator Expansions
    • S. D. Schwartz, Accurate Quantum Mechanics From High Order Resumed Operator Expansions, J. Chem. Phys., 100, 8795-8801 (1994);
    • (1994) J. Chem. Phys , vol.100 , pp. 8795-8801
    • Schwartz, S.D.1
  • 16
    • 0009682191 scopus 로고
    • Vibrational Energy Transfer from Resumed Evolution Operators
    • S. D. Schwartz, Vibrational Energy Transfer from Resumed Evolution Operators, J. Chem. Phys., 101, 10436-10441 (1994);
    • (1994) J. Chem. Phys , vol.101 , pp. 10436-10441
    • Schwartz, S.D.1
  • 17
    • 0009682790 scopus 로고
    • Vibrational Energy Transfer in Linear Hydrocarbon Chains: New Quantum Results
    • D. Antoniou, S. D. Schwartz, Vibrational Energy Transfer in Linear Hydrocarbon Chains: New Quantum Results, J. Chem. Phys., 103, 7277-7286 (1995);
    • (1995) J. Chem. Phys , vol.103 , pp. 7277-7286
    • Antoniou, D.1    Schwartz, S.D.2
  • 18
    • 0000795030 scopus 로고    scopus 로고
    • The Interaction Representation and Non-Adiabatic Corrections to Adiabatic Evolution Operators
    • S. D. Schwartz, The Interaction Representation and Non-Adiabatic Corrections to Adiabatic Evolution Operators, J. Chem. Phys., 104, 1394-1398 (1996);
    • (1996) J. Chem. Phys , vol.104 , pp. 1394-1398
    • Schwartz, S.D.1
  • 19
    • 0001397379 scopus 로고    scopus 로고
    • Nonadiabatic Effects in a Method that Combines Classical and Quantum Mechanics
    • D. Antoniou, S. D. Schwartz, Nonadiabatic Effects in a Method that Combines Classical and Quantum Mechanics, J. Chem. Phys., 104, 3526-3530 (1996);
    • (1996) J. Chem. Phys , vol.104 , pp. 3526-3530
    • Antoniou, D.1    Schwartz, S.D.2
  • 20
    • 0009716722 scopus 로고    scopus 로고
    • The Interaction Representation and Non-Adiabatic Corrections to Adiabatic Evolution Operators II: Nonlinear Quantum Systems
    • S. D. Schwartz, The Interaction Representation and Non-Adiabatic Corrections to Adiabatic Evolution Operators II: Nonlinear Quantum Systems, J. Chem. Phys., 104, 7985-7987 (1996).
    • (1996) J. Chem. Phys , vol.104 , pp. 7985-7987
    • Schwartz, S.D.1
  • 21
    • 0009750748 scopus 로고
    • Accurate Quantum Mechanics From High Order Resummed Operator Expansions
    • S. D. Schwartz, Accurate Quantum Mechanics From High Order Resummed Operator Expansions, J. Chem. Phys., 100, 8795-8801 (1994);
    • (1994) J. Chem. Phys , vol.100 , pp. 8795-8801
    • Schwartz, S.D.1
  • 22
    • 0009682191 scopus 로고
    • Vibrational Energy Transfer from Resummed Evolution Operators
    • S. D. Schwartz. Vibrational Energy Transfer from Resummed Evolution Operators, J. Chem. Phys., 101, 10436-10441 (1994);
    • (1994) J. Chem. Phys , vol.101 , pp. 10436-10441
    • Schwartz, S.D.1
  • 23
    • 0009682790 scopus 로고
    • Vibrational Energy Transfer in Linear Hydrocarbon Chains: New Quantum Results
    • D. Antoniou, S. D. Schwartz, Vibrational Energy Transfer in Linear Hydrocarbon Chains: New Quantum Results, J. Chem. Phys., 103, 7277-7286 (1995);
    • (1995) J. Chem. Phys , vol.103 , pp. 7277-7286
    • Antoniou, D.1    Schwartz, S.D.2
  • 24
    • 0000795030 scopus 로고    scopus 로고
    • The Interaction Representation and Non-Adiabatic Corrections to Adiabatic Evolution Operators
    • S. D. Schwartz, The Interaction Representation and Non-Adiabatic Corrections to Adiabatic Evolution Operators, J. Chem. Phys., 104, 1394-1398 (1996);
    • (1996) J. Chem. Phys , vol.104 , pp. 1394-1398
    • Schwartz, S.D.1
  • 25
    • 0001397379 scopus 로고    scopus 로고
    • Nonadiabatic Effects in a Method that Combines Classical and Quantum Mechanics
    • D. Antoniou, S. D. Schwartz, Nonadiabatic Effects in a Method that Combines Classical and Quantum Mechanics, J. Chem. Phys., 104, 3526-3530 (1996);
    • (1996) J. Chem. Phys , vol.104 , pp. 3526-3530
    • Antoniou, D.1    Schwartz, S.D.2
  • 26
    • 0009716722 scopus 로고    scopus 로고
    • The Interaction Representation and Non-Adiabatic Corrections to Adiabatic Evolution Operators II: Nonlinear Quantum Systems
    • S. D. Schwartz, The Interaction Representation and Non-Adiabatic Corrections to Adiabatic Evolution Operators II: Nonlinear Quantum Systems, J. Chem. Phys., 104, 7985-7987 (1996).
    • (1996) J. Chem. Phys , vol.104 , pp. 7985-7987
    • Schwartz, S.D.1
  • 27
    • 84940252991 scopus 로고
    • On the Exponential Solution of Differential Equations for a Linear Operator
    • W. Magnus, On the Exponential Solution of Differential Equations for a Linear Operator, Commun. Pure Appl. Math., VII, 649 (1954).
    • (1954) Commun. Pure Appl. Math , vol.VII , pp. 649
    • Magnus, W.1
  • 28
    • 36749104477 scopus 로고
    • Solution of the Schrodinger Equation by a Spectral Method II: Vibrational Energy Levels of Triatomic Molecules
    • M. D. Feit, J. A. Fleck Jr., Solution of the Schrodinger Equation by a Spectral Method II: Vibrational Energy Levels of Triatomic Molecules, J. Chem. Phys., 78, 301 (1983).
    • (1983) J. Chem. Phys , vol.78 , pp. 301
    • Feit, M.D.1    Fleck Jr., J.A.2
  • 29
    • 0000795030 scopus 로고    scopus 로고
    • The Interaction Representation and Non-Adiabatic Corrections to Adiabatic Evolution Operators
    • S. D. Schwartz, The Interaction Representation and Non-Adiabatic Corrections to Adiabatic Evolution Operators, J. Chem. Phys., 104, 1394-1398 (1996).
    • (1996) J. Chem. Phys , vol.104 , pp. 1394-1398
    • Schwartz, S.D.1
  • 30
    • 0343791207 scopus 로고
    • Quantum Mechanical Rate Constants for Bimolecular Reactions
    • Wm. H. Miller, S. D. Schwartz, and J. W. Tromp, Quantum Mechanical Rate Constants for Bimolecular Reactions, J. Chem. Phys., 79, 4889-4898 (1983).
    • (1983) J. Chem. Phys , vol.79 , pp. 4889-4898
    • Miller, W.H.1    Schwartz, S.D.2    Tromp, J.W.3
  • 31
    • 0001378703 scopus 로고    scopus 로고
    • Quantum Activated Rates-An Evolution Operator Approach
    • S. D. Schwartz, Quantum Activated Rates-An Evolution Operator Approach, J. Chem. Phys., 105, 6871-6879 (1996).
    • (1996) J. Chem. Phys , vol.105 , pp. 6871-6879
    • Schwartz, S.D.1
  • 32
    • 0035967362 scopus 로고    scopus 로고
    • Nonequilibrium solvation and the Quantum Kramers problem: proton transfer in aqueous glycine
    • (Bill Miller festschrift)
    • R. Karmacharya, D. Antoniou. S. D. Schwartz, Nonequilibrium solvation and the Quantum Kramers problem: proton transfer in aqueous glycine, J. Phys. Chem. B (Bill Miller festschrift), 105, 2563-2567 (2001);
    • (2001) J. Phys. Chem. B , vol.105 , pp. 2563-2567
    • Karmacharya, R.1    Schwartz, D.2    Antoniou, S.D.3
  • 33
    • 0032615369 scopus 로고    scopus 로고
    • A Molecular Dynamics Quantum Kramers Study of Proton Transfer in Solution
    • D. Antoniou, S. D. Schwartz, A Molecular Dynamics Quantum Kramers Study of Proton Transfer in Solution, J. Chem. Phys., 110, 465-472 (1999);
    • (1999) J. Chem. Phys , vol.110 , pp. 465-472
    • Antoniou, D.1    Schwartz, S.D.2
  • 34
    • 0000378543 scopus 로고    scopus 로고
    • Quantum Proton Transfer with Spatially Dependent Friction: Phenol-Amine in Methyl Chloride
    • D. Antoniou, S. D. Schwartz, Quantum Proton Transfer with Spatially Dependent Friction: Phenol-Amine in Methyl Chloride, J. Chem. Phys., 110, 7359-7364 (1999).
    • (1999) J. Chem. Phys , vol.110 , pp. 7359-7364
    • Antoniou, D.1    Schwartz, S.D.2
  • 35
    • 0001672288 scopus 로고
    • Chemical and electrochemical electron transfer theory
    • R. A. Marcus, Chemical and electrochemical electron transfer theory, Annu. Rev. Phys. Chem., 15, 155-181 (1964);
    • (1964) Annu. Rev. Phys. Chem , vol.15 , pp. 155-181
    • Marcus, R.A.1
  • 36
    • 36749105488 scopus 로고
    • Dynamics of Hydrogen Atom and Proton Transfer reactions: Symmetric Case
    • V. Babamüv, R. A. Marcus, Dynamics of Hydrogen Atom and Proton Transfer reactions: Symmetric Case, J. Chem. Phys. 74, 1790 (1981).
    • (1981) J. Chem. Phys , vol.74 , pp. 1790
    • Babamüv, V.1    Marcus, R.A.2
  • 37
    • 0344400850 scopus 로고
    • Dynamics of Double Proton Transfer Reactions in the Excited State Model of Hydrogen Bonded Base Pairs
    • K. FukE, K. Kaya, Dynamics of Double Proton Transfer Reactions in the Excited State Model of Hydrogen Bonded Base Pairs, J. Phys. Chem., 93, 614 (1989);
    • (1989) J. Phys. Chem , vol.93 , pp. 614
    • FukE, K.1    Kaya, K.2
  • 39
    • 36749105823 scopus 로고
    • Structure and Dynamics of Intramolecular Hydrogel Bonds in Carboxylic Acid Dimers: A Solid State NMR Study
    • B. H. Meier, F. Graf, R. R. Ernst, Structure and Dynamics of Intramolecular Hydrogel Bonds in Carboxylic Acid Dimers: A Solid State NMR Study, J. Chem. Phys. 76, 767 (1982);
    • (1982) J. Chem. Phys , vol.76 , pp. 767
    • Meier, B.H.1    Graf, F.2    Ernst, R.R.3
  • 40
    • 14344278556 scopus 로고
    • Hydrogen bond dynamics in isotopically substituted benzoic acid dimers
    • A. StockLi, B. H. Meier, R. Kreis, R. Meyer, R. R. Ernst, Hydrogen bond dynamics in isotopically substituted benzoic acid dimers, J. Chem. Phys., 93, 1502 (1990);
    • (1990) J. Chem. Phys , vol.93 , pp. 1502
    • StockLi, A.1    Meier, B.H.2    Kreis, R.3    Meyer, R.4    Ernst, R.R.5
  • 41
    • 0032209231 scopus 로고    scopus 로고
    • Proton Tunneling in Benzoic Acid Crystals at Intermediate Temperatures: Nuclear Magnetic Resonance and Neutron Scattering Studies
    • M. Neumann, D. F. Brougham, C. J. McGloin, M. R. Johnson, A. J. Horsewill, H. P. Trommsdorff, Proton Tunneling in Benzoic Acid Crystals at Intermediate Temperatures: Nuclear Magnetic Resonance and Neutron Scattering Studies, J. Chem. Phys., 109, 7300 (1998).
    • (1998) J. Chem. Phys , vol.109 , pp. 7300
    • Neumann, M.1    Brougham, D.F.2    McGloin, C.J.3    Johnson, M.R.4    Horsewill, A.J.5    Trommsdorff, H.P.6
  • 42
    • 0347866726 scopus 로고    scopus 로고
    • Activated Chemistry in the Presence of a Strongly Symmetrically Coupled Vibration
    • D. Antoniou, S. D. Schwartz, Activated Chemistry in the Presence of a Strongly Symmetrically Coupled Vibration, J. Chem. Phys., 108, 3620-3625 (1998).
    • (1998) J. Chem. Phys , vol.108 , pp. 3620-3625
    • Antoniou, D.1    Schwartz, S.D.2
  • 43
    • 0000118674 scopus 로고    scopus 로고
    • Proton Transfer in Benzoic Acid Crystals: Another Look Using Quantum Operator Theory
    • D. Antoniou, S. D. Schwartz, Proton Transfer in Benzoic Acid Crystals: Another Look Using Quantum Operator Theory, J. Chem. Phys., 109, 2287-2293 (1998).
    • (1998) J. Chem. Phys , vol.109 , pp. 2287-2293
    • Antoniou, D.1    Schwartz, S.D.2
  • 46
    • 11744322797 scopus 로고
    • Low-temperature Chemical Reactions. Effect of Symmetrically Coupled Vibrations in Collinear Exchange Reactions
    • V. A. Benderskii, V. I. Gθldanskii, D. E. Makarov, Low-temperature Chemical Reactions. Effect of Symmetrically Coupled Vibrations in Collinear Exchange Reactions, Chem. Phys. 154, 407 (1991).
    • (1991) Chem. Phys , vol.154 , pp. 407
    • Benderskii, V.A.1    Gθldanskii, V.I.2    Makarov, D.E.3
  • 47
    • 0034679001 scopus 로고    scopus 로고
    • Computational studies of the mechanism for proton and hydride transfer in liver alcohol dehydrogenase
    • P. K. Agarwal, S. P. Webb, S. Hammes-Schiffer, Computational studies of the mechanism for proton and hydride transfer in liver alcohol dehydrogenase, J. Am. Chem. Soc., 122, 4803-4812 (2000).
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 4803-4812
    • Agarwal, P.K.1    Webb, S.P.2    Hammes-Schiffer, S.3
  • 48
    • 0033519723 scopus 로고    scopus 로고
    • Enzyme dynamics and hydrogen tunneling in a thermophilic alcohol dehydrogenase
    • A. Kohen, R. Canniü, S. Bartülucci, J. P. Klinman, Enzyme dynamics and hydrogen tunneling in a thermophilic alcohol dehydrogenase, Nature 399, 496-499 (1999).
    • (1999) Nature , vol.399 , pp. 496-499
    • Kohen, A.1    Canniü, R.2    Bartülucci, S.3    Klinman, J.P.4
  • 49
    • 0024573393 scopus 로고
    • Hydrogen Tunneling in Enzyme Reactions
    • Y. Cha, C. J. Murray, J. P. Klinman, Hydrogen Tunneling in Enzyme Reactions, Science 243, 1325 (1989).
    • (1989) Science , vol.243 , pp. 1325
    • Cha, Y.1    Murray, C.J.2    Klinman, J.P.3
  • 50
    • 0024379962 scopus 로고
    • Evidence that both Protium and Deuterium Undergo Significant Tunneling in the Reaction Catalyzed by Bovine Serum Amine Oxidase
    • K. L. Grant, J. P. Klinman, Evidence that both Protium and Deuterium Undergo Significant Tunneling in the Reaction Catalyzed by Bovine Serum Amine Oxidase, Biochemistry 28, 6597 (1989);
    • (1989) Biochemistry , vol.28 , pp. 6597
    • Grant, K.L.1    Klinman, J.P.2
  • 51
    • 0000205312 scopus 로고    scopus 로고
    • Enzyme Catalysis: Beyond Classical Paradigms
    • A. Kohen, J. P. Klinman, Enzyme Catalysis: Beyond Classical Paradigms, Acc. Chem. Res. 31, 397 (1998);
    • (1998) Acc. Chem. Res , vol.31 , pp. 397
    • Kohen, A.1    Klinman, J.P.2
  • 52
    • 0028954039 scopus 로고
    • Hydrogen Tunneling in Enzyme Catalysis
    • B. J. Bahnson, J. P. Klinman, Hydrogen Tunneling in Enzyme Catalysis, Methods Enzymol., 249, 373 (1995);
    • (1995) Methods Enzymol , vol.249 , pp. 373
    • Bahnson, B.J.1    Klinman, J.P.2
  • 53
    • 0026454264 scopus 로고
    • Role of Internal Thermodynamics in Determining Hydrogen Tunneling in Enzyme-Catalyzed Hydrogen Transfer Reactions
    • J. Rucker, Y. Cha, T. Jonsson, K. L. Grant, J. P. Klinman, Role of Internal Thermodynamics in Determining Hydrogen Tunneling in Enzyme-Catalyzed Hydrogen Transfer Reactions, Biochemistry, 31, 11489 (1992).
    • (1992) Biochemistry , vol.31 , pp. 11489
    • Rucker, J.1    Cha, Y.2    Jonsson, T.3    Grant, K.L.4    Klinman, J.P.5
  • 54
    • 0034327617 scopus 로고    scopus 로고
    • Protein Flexibility Correlates with Degree of Hydrogen Tunneling in Thermophilic and Mesophilic Alcohol Dehydrogenases
    • A. Kohen, J. P. Klinman, Protein Flexibility Correlates with Degree of Hydrogen Tunneling in Thermophilic and Mesophilic Alcohol Dehydrogenases, J. Am. Chem. Soc., 122, 10738-10739 (2000).
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 10738-10739
    • Kohen, A.1    Klinman, J.P.2
  • 55
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
    • P. Zavodsky, J. Kardos, A. Svingor. G. A. Petsko, Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins, Proc. Natl. Acad. Sci. U.S.A. 95, 7406-7411 (1998).
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 7406-7411
    • Zavodsky, P.1    Kardos, J.2    Petsko, A.3    Svingor, G.A.4
  • 56
    • 3042709505 scopus 로고    scopus 로고
    • Thermal-activated protein mobility and its correlation with catalysis in thermophilic alcohol dehydrogenase
    • Z.-X. Liang, T. Lee, K. A. Resing. N. G. Ahn, J. P. Klinman, Thermal-activated protein mobility and its correlation with catalysis in thermophilic alcohol dehydrogenase, Proc. Natl. Acad. Sci. U.S.A., 101, 9556-9561 (2004).
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 9556-9561
    • Liang, Z.-X.1    Lee, T.2    Ahn, K.A.3    Resing, N.G.4    Klinman, J.P.5
  • 58
    • 0027196492 scopus 로고
    • Unmasking of hydrogen tunneling in the horse liver alcohol dehydrogenase reaction by site-directed mutagenesis
    • B. J. Bahnson, D-H. Park, K. Kim. B. V. Plapp, J. P. Klinman. Unmasking of hydrogen tunneling in the horse liver alcohol dehydrogenase reaction by site-directed mutagenesis, Biochemistry 32, 5503-5507 (1993).
    • (1993) Biochemistry , vol.32 , pp. 5503-5507
    • Bahnson, B.J.1    Park, D.-H.2    Plapp, K.3    Kim, B.V.4    Klinman, J.P.5
  • 59
    • 0032817216 scopus 로고    scopus 로고
    • + by PhCH2 OH on the distance between reactants when catalyzed by horse liver alcohol dehydrogenase and 203 single point mutants
    • + by PhCH2 OH on the distance between reactants when catalyzed by horse liver alcohol dehydrogenase and 203 single point mutants, Bioorg. Chem. 27, 289-296 (1999).
    • (1999) Bioorg. Chem , vol.27 , pp. 289-296
    • Luo, J.1    Kahn, K.2    Bruice, T.C.3
  • 60
    • 0035916307 scopus 로고    scopus 로고
    • Probes of Hydrogen tunneling with horse liver alcohol dehydrogenase at subzero temperatures
    • S-C. Tsai, J. P. Klinman, Probes of Hydrogen tunneling with horse liver alcohol dehydrogenase at subzero temperatures, Biochemistry, 40, 2303-2311 (1999).
    • (1999) Biochemistry , vol.40 , pp. 2303-2311
    • Tsai, S.-C.1    Klinman, J.P.2
  • 61
    • 0000809846 scopus 로고
    • Reaction coordinate tunneling in hydride-transfer reactions
    • P. Huskey, R. Schowen, Reaction coordinate tunneling in hydride-transfer reactions, J. Am. Chem. Soc. 105, 5704-5706 (1983).
    • (1983) J. Am. Chem. Soc , vol.105 , pp. 5704-5706
    • Huskey, P.1    Schowen, R.2
  • 63
    • 0031250160 scopus 로고    scopus 로고
    • Three Pulse Stimulated Photon Echo Experiments as a Probe of Polar Solvation Dynamics: Utility of Harmonic Bath Modes
    • S. A. Passino, Y. Nagasawa, G. R. Fleming, Three Pulse Stimulated Photon Echo Experiments as a Probe of Polar Solvation Dynamics: Utility of Harmonic Bath Modes, J. Chem. Phys. 107, 6094 (1997).
    • (1997) J. Chem. Phys , vol.107 , pp. 6094
    • Passino, S.A.1    Nagasawa, Y.2    Fleming, G.R.3
  • 64
    • 0000378543 scopus 로고    scopus 로고
    • Quantum Proton Transfer with Spatially Dependent Friction: Phenol-Amine in Methyl Chloride
    • D. Antoniou, S. D. Schwartz. Quantum Proton Transfer with Spatially Dependent Friction: Phenol-Amine in Methyl Chloride, J. Chem. Phys. 110, 7359-7364 (1999).
    • (1999) J. Chem. Phys , vol.110 , pp. 7359-7364
    • Antoniou, D.1    Schwartz, S.D.2
  • 65
    • 0035249366 scopus 로고    scopus 로고
    • A computational method to discover the existence of promoting vibrations for chemical reactions in condensed phases
    • S. Caratzoulas, S. D. Schwartz, A computational method to discover the existence of promoting vibrations for chemical reactions in condensed phases, J. Chem. Phys., 114, 2910-2918 (2001).
    • (2001) J. Chem. Phys , vol.114 , pp. 2910-2918
    • Caratzoulas, S.1    Schwartz, S.D.2
  • 70
    • 0037426823 scopus 로고    scopus 로고
    • A computational method to identify residues important in creating a protein promoting-vibration in enzymes
    • J. S. Mincer, S. D. Schwartz, A computational method to identify residues important in creating a protein promoting-vibration in enzymes, J. Phys. Chem. B, 107, 366-371 (2003).
    • (2003) J. Phys. Chem. B , vol.107 , pp. 366-371
    • Mincer, J.S.1    Schwartz, S.D.2
  • 72
    • 0037452898 scopus 로고    scopus 로고
    • Amino Acid Residues in the Nicotinamide Binding site Contribute to Catalysis by Horse Liver Alcohol Dehydrogenase
    • J. K. Rubach, B. V. Plapp, Amino Acid Residues in the Nicotinamide Binding site Contribute to Catalysis by Horse Liver Alcohol Dehydrogenase, Biochemistry, 42, 2907-2915 (2003).
    • (2003) Biochemistry , vol.42 , pp. 2907-2915
    • Rubach, J.K.1    Plapp, B.V.2
  • 73
    • 0035940450 scopus 로고    scopus 로고
    • Contributions of Valine-292 in the Nicotinamide Binding Site of Liver Alcohol Dehydrogenase and Dynamics to Catalysis
    • J. K. Rubach, S. Ramaswamy, B. V. Plapp, Contributions of Valine-292 in the Nicotinamide Binding Site of Liver Alcohol Dehydrogenase and Dynamics to Catalysis, Biochemistry 40, 12686-12694 (2001).
    • (2001) Biochemistry , vol.40 , pp. 12686-12694
    • Rubach, J.K.1    Ramaswamy, S.2    Plapp, B.V.3
  • 74
    • 0027196492 scopus 로고
    • Unmasking of hydrogen tunneling in the horse liver alcohol dehydrogenase reaction by site-directed mutagenesis
    • B. J. Bahnson, D.-H. Park, K. Kim, B. V. Plapp, J. P. Klinman, Unmasking of hydrogen tunneling in the horse liver alcohol dehydrogenase reaction by site-directed mutagenesis, Biochemistry, 32, 5503-5507 (1993);
    • (1993) Biochemistry , vol.32 , pp. 5503-5507
    • Bahnson, B.J.1    Park, D.-H.2    Kim, K.3    Plapp, B.V.4    Klinman, J.P.5
  • 75
    • 0034673157 scopus 로고    scopus 로고
    • Probes of a Role for Remote Binding Interactions on Hydrogen Tunneling in the Horse Liver Alcohol Dehydrogenase Reaction
    • J. K. Chin, J. P. Klinman, Probes of a Role for Remote Binding Interactions on Hydrogen Tunneling in the Horse Liver Alcohol Dehydrogenase Reaction, Biochemistry, 39, 1278-1284 (2000).
    • (2000) Biochemistry , vol.39 , pp. 1278-1284
    • Chin, J.K.1    Klinman, J.P.2
  • 76
    • 4444371260 scopus 로고    scopus 로고
    • Anticorrelated motions as a driving force in enzyme catalysis: The dehydrogenase reaction
    • J. Luo, T. C. Bruice, Anticorrelated motions as a driving force in enzyme catalysis: The dehydrogenase reaction, Proc. Natl. Acad. Sci. U.S.A., 101, 13152-13156 (2004).
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 13152-13156
    • Luo, J.1    Bruice, T.C.2
  • 77
    • 0037066140 scopus 로고    scopus 로고
    • Toward an Understanding of the Role of Dynamics on Enzymatic Catalysis in Lactate Dehydrogenase
    • M. Gulotta, H. Deng, R. B. Dyer, R. H. Callender, Toward an Understanding of the Role of Dynamics on Enzymatic Catalysis in Lactate Dehydrogenase, Biochemistry, 41, 3353-3363 (2002).
    • (2002) Biochemistry , vol.41 , pp. 3353-3363
    • Gulotta, M.1    Deng, H.2    Dyer, R.B.3    Callender, R.H.4
  • 79
    • 1042282260 scopus 로고    scopus 로고
    • Donor acceptor distance and protein promoting vibration coupling as a mechanism for kinetic control in isozymes of Human Lactate Dehydrogenase
    • J. E. Bassner, S. D. Schwartz, Donor acceptor distance and protein promoting vibration coupling as a mechanism for kinetic control in isozymes of Human Lactate Dehydrogenase, J. Phys. Chem. B., 108, 444-451 (2004).
    • (2004) J. Phys. Chem. B , vol.108 , pp. 444-451
    • Bassner, J.E.1    Schwartz, S.D.2
  • 80
    • 84891292187 scopus 로고    scopus 로고
    • How Enzyme Dynamics Helps Catalyze a Chemical Reaction in Atomic Detail: A Transition Path Sampling Study
    • submitted.
    • J. E. Bassner, S. D. Schwartz, How Enzyme Dynamics Helps Catalyze a Chemical Reaction in Atomic Detail: A Transition Path Sampling Study, J. Am. Chem. Soc., submitted.
    • J. Am. Chem. Soc
    • Bassner, J.E.1    Schwartz, S.D.2
  • 82
    • 0037012441 scopus 로고    scopus 로고
    • Identification of a protein promoting vibration in the reaction catalyzed by Horse Liver Alcohol Dehydrogenase
    • S. Caratzoulas, J. S. Mincer, S. D. Schwartz, Identification of a protein promoting vibration in the reaction catalyzed by Horse Liver Alcohol Dehydrogenase, J. Am. Chem. Soc., 124 (13), 3270-3276 (2002).
    • (2002) J. Am. Chem. Soc , vol.124 , Issue.13 , pp. 3270-3276
    • Caratzoulas, S.1    Mincer, J.S.2    Schwartz, S.D.3
  • 83
    • 0000801009 scopus 로고    scopus 로고
    • Efficient transition path sampling: application to Lennard-Jones cluster rearrangements
    • C. Dellagü, P. G. Bülhuis, D. Chandler, Efficient transition path sampling: application to Lennard-Jones cluster rearrangements, J. Chem. Phys., 108, 9236-9245 (1998).
    • (1998) J. Chem. Phys , vol.108 , pp. 9236-9245
    • Dellagü, C.1    Bülhuis, P.G.2    Chandler, D.3
  • 90
    • 0037123216 scopus 로고    scopus 로고
    • Temperature-Dependent Isotope Effects in Soybean Lipoxygenase-1: Correlating Hydrogen Tunneling with Protein Dynamics
    • M. J. Knapp, K. Rickert, J. P. Klinman, Temperature-Dependent Isotope Effects in Soybean Lipoxygenase-1: Correlating Hydrogen Tunneling with Protein Dynamics, J. Am. Chem. Soc. 124, 3865 (2002);
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 3865
    • Knapp, M.J.1    Rickert, K.2    Klinman, J.P.3
  • 91
    • 0036301901 scopus 로고    scopus 로고
    • Environmentally coupled hydrogen tunneling
    • M. J. Knapp, J. P. Klinman, Environmentally coupled hydrogen tunneling, Eur. J. Biochem. 269, 3113 (2002).
    • (2002) Eur. J. Biochem , vol.269 , pp. 3113
    • Knapp, M.J.1    Klinman, J.P.2
  • 92
    • 0033537697 scopus 로고    scopus 로고
    • Enzymatic H-Transfer Requires Vibration-Driven Extreme Tunneling
    • J. Basran, M. Sutcliffe, N. Scrutton, Enzymatic H-Transfer Requires Vibration-Driven Extreme Tunneling, Biochemistry, 38, 3218 (1999);
    • (1999) Biochemistry , vol.38 , pp. 3218
    • Basran, J.1    Sutcliffe, M.2    Scrutton, N.3
  • 93
    • 0036305396 scopus 로고    scopus 로고
    • A new conceptual framework for enzyme catalysis
    • M. J. Sutcliffe, N. S. Scrutton, A new conceptual framework for enzyme catalysis, Eur. J. Biochem., 269, 3096 (2002).
    • (2002) Eur. J. Biochem , vol.269 , pp. 3096
    • Sutcliffe, M.J.1    Scrutton, N.S.2
  • 94
    • 33751158124 scopus 로고
    • Mechanism for Proton-Coupled Electron-Transfer Reactions
    • R. I. Cukier, Mechanism for Proton-Coupled Electron-Transfer Reactions, J. Phys. Chem. 98, 2377 (1994);
    • (1994) J. Phys. Chem , vol.98 , pp. 2377
    • Cukier, R.I.1
  • 95
    • 0000012384 scopus 로고
    • Molecular Dynamics and Quantum Chemistry Study of a Proton-Coupled Electron Transfer Reaction
    • X. Zhao, R. I. Cukier, Molecular Dynamics and Quantum Chemistry Study of a Proton-Coupled Electron Transfer Reaction, J. Phys. Chem. 99, 945 (1995);
    • (1995) J. Phys. Chem , vol.99 , pp. 945
    • Zhao, X.1    Cukier, R.I.2
  • 96
    • 0001077676 scopus 로고
    • Proton-Coupled Electron Transfer through an Asymmetric Hydrogen-Bonded Interface
    • R. I. Cukier, Proton-Coupled Electron Transfer through an Asymmetric Hydrogen-Bonded Interface, J. Phys. Chem. 99, 16101 (1995);
    • (1995) J. Phys. Chem , vol.99 , pp. 16101
    • Cukier, R.I.1
  • 97
    • 33748381480 scopus 로고    scopus 로고
    • Proton-Coupled Electron Transfer Reactions: Evaluation of Rate Constants
    • R. I. Cukier, Proton-Coupled Electron Transfer Reactions: Evaluation of Rate Constants, J. Phys. Chem. 100, 15428 (1996);
    • (1996) J. Phys. Chem , vol.100 , pp. 15428
    • Cukier, R.I.1
  • 98
    • 0000981534 scopus 로고
    • Nonadiabatic effects on the charge transfer rate constant: A numerical study of a simple model system
    • S. Shin, H. Metiu, Nonadiabatic effects on the charge transfer rate constant: A numerical study of a simple model system, J. Chem. Phys. 102, 9285 (1995);
    • (1995) J. Chem. Phys , vol.102 , pp. 9285
    • Shin, S.1    Metiu, H.2
  • 99
    • 0034859929 scopus 로고    scopus 로고
    • Theoretical perspectives on proton-coupled electron transfer reactions
    • S. Hammes-Schiffer. Theoretical perspectives on proton-coupled electron transfer reactions, Acc. Chem. Res. 34, 273-281 (2001);
    • (2001) Acc. Chem. Res , vol.34 , pp. 273-281
    • Hammes-Schiffer, S.1
  • 100
    • 0036570243 scopus 로고    scopus 로고
    • Theoretical investigation of large kinetic isotope effects for proton-coupled electron transfer in ruthenium polypyridyl complexes
    • N. Iordanova, S. Hammes-Schiffer. Theoretical investigation of large kinetic isotope effects for proton-coupled electron transfer in ruthenium polypyridyl complexes, J. Am. Chem. Soc. 124, 4848-4856 (2002).
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 4848-4856
    • Iordanova, N.1    Hammes-Schiffer, S.2
  • 101
    • 10044273966 scopus 로고    scopus 로고
    • Promoting vibrations in human purine nucleoside phosphorylase: A molecular dynamics and hybrid quantum mechanical/molecular mechanical study
    • S. Nunez, D. Antoniou, V. L. Schramm, S. D. Schwartz. Promoting vibrations in human purine nucleoside phosphorylase: A molecular dynamics and hybrid quantum mechanical/molecular mechanical study, J. Am. Chem. Soc., 126, 15720-15729 (2004).
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 15720-15729
    • Nunez, S.1    Antoniou, D.2    Schramm, V.L.3    Schwartz, S.D.4
  • 103
    • 10044273966 scopus 로고    scopus 로고
    • Electronic promoting motions in human purine nucleoside phosphorylase: a molecular dynamics and hybrid quantum mechanical/molecular mechanical study
    • S. Nunez, D. Antoniou, V. L. Schramm, S. D. Schwartz, Electronic promoting motions in human purine nucleoside phosphorylase: a molecular dynamics and hybrid quantum mechanical/molecular mechanical study, J. Am. Chem. Soc., 126, 15720-15729 (2004).
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 15720-15729
    • Nunez, S.1    Antoniou, D.2    Schramm, V.L.3    Schwartz, S.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.