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Volumn 1814, Issue 8, 2011, Pages 1077-1092

Protein dynamics and enzyme catalysis: Insights from simulations

Author keywords

Computational enzymology; Conformational change; Enzyme catalysis; Functional dynamics; Molecular dynamics; Molecular mechanics; Protein dynamics; Quantum mechanics; Quantum tunnelling

Indexed keywords

BIOCHEMISTRY; CATALYSIS; CONFORMATIONAL TRANSITION; ENZYME MECHANISM; HUMAN; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN DYNAMICS; QUANTUM MECHANICS; REVIEW; SIMULATION;

EID: 79958826524     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.12.002     Document Type: Review
Times cited : (84)

References (232)
  • 2
    • 37849017099 scopus 로고    scopus 로고
    • Cooperative symmetric to asymmetric conformational transition of the apo-form of scavenger decapping enzyme revealed by simulations
    • U. Pentikäinen, O.T. Pentikäinen, A.J. Mulholland, Cooperative symmetric to asymmetric conformational transition of the apo-form of scavenger decapping enzyme revealed by simulations, Proteins: Struct. Funct. Bioinf. 70 (2008) 498-508.
    • (2008) Proteins: Struct. Funct. Bioinf. , vol.70 , pp. 498-508
    • Pentikäinen, U.1    Pentikäinen, O.T.2    Mulholland, A.J.3
  • 4
  • 5
    • 0035957144 scopus 로고    scopus 로고
    • A signature of the T-NR transition in human hemoglobin
    • M.R. Mihailescu, I.M. Russu, A signature of the T-NR transition in human hemoglobin, Proc. Natl. Acad. Sci. USA 98 (2001) 3773-3777.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3773-3777
    • Mihailescu, M.R.1    Russu, I.M.2
  • 6
    • 0029894282 scopus 로고    scopus 로고
    • Kinetic pathways and barriers for ligand binding to myoglobin
    • J.S. Olson, G.N. Phillips, Kinetic pathways and barriers for ligand binding to myoglobin, J. Biol. Chem. 271 (1996) 17593-17596.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17593-17596
    • Olson, J.S.1    Phillips, G.N.2
  • 7
    • 0033574735 scopus 로고    scopus 로고
    • A steric mechanism for inhibition of CO binding to heme proteins
    • DOI 10.1126/science.284.5413.473
    • G.S. Kachalova, A.N. Popov, H.D. Bartunik, A steric mechanism for inhibition of CO binding to heme proteins, Science 284 (1999) 473-476. (Pubitemid 29289617)
    • (1999) Science , vol.284 , Issue.5413 , pp. 473-476
    • Kachalova, G.S.1    Popov, A.N.2    Bartunik, H.D.3
  • 8
    • 0035923445 scopus 로고    scopus 로고
    • Protein conformational relaxation and ligand migration in myoglobin: A nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction
    • DOI 10.1021/bi010715u
    • V. Srajer, Z. Ren, T.Y. Teng, M. Schmidt, T. Ursby, D. Bourgeois, C. Pradervand, W. Schildkamp, M. Wulff, K. Moffat, Protein conformational relaxation and ligand migration in myoglobin: a nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction, Biochemistry 40 (2001) 13802-13815. (Pubitemid 33078849)
    • (2001) Biochemistry , vol.40 , Issue.46 , pp. 13802-13815
    • Srajer, V.1    Ren, Z.2    Teng, T.-Y.3    Schmidt, M.4    Ursby, T.5    Bourgeois, D.6    Pradervand, C.7    Schildkamp, W.8    Wulff, M.9    Moffat, K.10
  • 9
    • 33645789373 scopus 로고    scopus 로고
    • The Fe-CO bond energy in myoglobin: A QM/MM study of the effect of tertiary structure
    • N. Strickland, A.J. Mulholland, J.N. Harvey, The Fe-CO bond energy in myoglobin: a QM/MM study of the effect of tertiary structure, Biophys. J. 90 (2006) 27-29.
    • (2006) Biophys. J. , vol.90 , pp. 27-29
    • Strickland, N.1    Mulholland, A.J.2    Harvey, J.N.3
  • 11
    • 43249092579 scopus 로고    scopus 로고
    • The use of X-ray crystallography to determine absolute configuration
    • DOI 10.1002/chir.20473
    • H.D. Flack, G. Bernardinelli, The use of X-ray crystallography to determine absolute configuration, Chirality 20 (2008) 681-690. (Pubitemid 351656172)
    • (2008) Chirality , vol.20 , Issue.5 , pp. 681-690
    • Flack, H.D.1    Bernardinelli, G.2
  • 13
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • DOI 10.1038/nsb0902-646
    • M. Karplus, J.A. McCammon, Molecular dynamics simulations of biomolecules, Nat. Struct. Biol. 9 (2002) 646-652. (Pubitemid 34977295)
    • (2002) Nature Structural Biology , vol.9 , Issue.9 , pp. 646-652
    • Karplus, M.1    McCammon, J.A.2
  • 15
    • 0015859467 scopus 로고
    • Principles that govern folding of protein chains
    • C.B. Anfinsen, Principles that govern folding of protein chains, Science 181 (1973) 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 16
    • 76249126156 scopus 로고    scopus 로고
    • Multiple native states reveal persistent ruggedness of an RNA folding landscape
    • S.V. Solomatin, M. Greenfeld, S. Chu, D. Herschlag, Multiple native states reveal persistent ruggedness of an RNA folding landscape, Nature 463 (2010) 681-684.
    • (2010) Nature , vol.463 , pp. 681-684
    • Solomatin, S.V.1    Greenfeld, M.2    Chu, S.3    Herschlag, D.4
  • 17
    • 0026580844 scopus 로고
    • Evidence for Processivity and 2-Step Binding of the RNA Substrate from Studies of J1/2 Mutants of the Tetrahymena Ribozyme
    • D. Herschlag, Evidence for Processivity and 2-Step Binding of the RNA Substrate from Studies of J1/2 Mutants of the Tetrahymena Ribozyme, Biochemistry 31 (1992) 1386-1399.
    • (1992) Biochemistry , vol.31 , pp. 1386-1399
    • Herschlag, D.1
  • 19
    • 0000870544 scopus 로고
    • The kinetics of the inversion effect
    • L. Michaelis, M.L. Menten, The kinetics of the inversion effect, Biochem. Z. 49 (1913) 333-369.
    • (1913) Biochem. Z. , vol.49 , pp. 333-369
    • Michaelis, L.1    Menten, M.L.2
  • 20
  • 23
  • 24
    • 0004214524 scopus 로고
    • Longmans Green & co, London
    • J.B.S. Haldane, Enzymes, Longmans Green & co, London, 1930.
    • (1930) Enzymes
    • Haldane, J.B.S.1
  • 25
    • 84912208190 scopus 로고
    • Chemical achievement and hope for the future
    • L. Pauling, Chemical achievement and hope for the future,Am. Sci. 36 (1948) 51-58.
    • (1948) Am. Sci. , vol.36 , pp. 51-58
    • Pauling, L.1
  • 26
    • 0001858251 scopus 로고
    • Application of a Theory of Enzyme Specificity to Protein Synthesis
    • D.E. Koshland, Application of a Theory of Enzyme Specificity to Protein Synthesis, Proc. Natl. Acad. Sci. USA 44 (1958) 98-104.
    • (1958) Proc. Natl. Acad. Sci. USA , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 27
  • 29
    • 77953080085 scopus 로고    scopus 로고
    • Exploring atomic resolution physiology on a femtosecond to millisecond timescale using molecular dynamics simulations
    • R.O. Dror, M.O. Jensen, D.W. Borhani, D.E. Shaw, Exploring atomic resolution physiology on a femtosecond to millisecond timescale using molecular dynamics simulations, J. Gen. Physiol. 135 (2010) 555-562.
    • (2010) J. Gen. Physiol. , vol.135 , pp. 555-562
    • Dror, R.O.1    Jensen, M.O.2    Borhani, D.W.3    Shaw, D.E.4
  • 30
    • 76149136021 scopus 로고    scopus 로고
    • Molecular simulation of ab initio protein folding for a millisecond folder NTL9(1-39)
    • V.A. Voelz, G.R. Bowman, K. Beauchamp, V.S. Pande, Molecular simulation of ab initio protein folding for a millisecond folder NTL9(1-39), J. Am. Chem. Soc. 132 (2010) 1526-1528.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1526-1528
    • Voelz, V.A.1    Bowman, G.R.2    Beauchamp, K.3    Pande, V.S.4
  • 33
    • 0035889760 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the hydrocarbon region of a biomembrane using a reduced representation model
    • L. Whitehead, C.M. Edge, J.W. Essex, Molecular dynamics simulation of the hydrocarbon region of a biomembrane using a reduced representation model, J. Comput. Chem. 22 (2001) 1622-1633.
    • (2001) J. Comput. Chem. , vol.22 , pp. 1622-1633
    • Whitehead, L.1    Edge, C.M.2    Essex, J.W.3
  • 34
    • 33847242278 scopus 로고    scopus 로고
    • Coarse-grained molecular dynamics simulations of membrane proteins and peptides
    • P.J. Bond, J. Holyoake, A. Ivetac, S. Khalid, M.S. Sansom, Coarse-grained molecular dynamics simulations of membrane proteins and peptides, J. Struct. Biol. 157 (2007) 593-605.
    • (2007) J. Struct. Biol. , vol.157 , pp. 593-605
    • Bond, P.J.1    Holyoake, J.2    Ivetac, A.3    Khalid, S.4    Sansom, M.S.5
  • 35
    • 33748266722 scopus 로고    scopus 로고
    • Mixed atomistic and coarse-grained molecular dynamics: Simulation of a membrane-bound ion channel
    • Q. Shi, S. Izvekov, G.A. Voth, Mixed atomistic and coarse-grained molecular dynamics: simulation of a membrane-bound ion channel, J. Phys. Chem. B 110 (2006) 15045-15048.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 15045-15048
    • Shi, Q.1    Izvekov, S.2    Voth, G.A.3
  • 36
    • 0034282901 scopus 로고    scopus 로고
    • Sequestration of the active site by interdomain shifting - Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase
    • J.J. Barycki, L.K. O'brien, A.W. Strauss, L.J. Banaszak, Sequestration of the active site by interdomain shifting - Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase, J. Biol. Chem. 275 (2000) 27186-27196.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27186-27196
    • Barycki, J.J.1    O'Brien, L.K.2    Strauss, A.W.3    Banaszak, L.J.4
  • 39
    • 0029871812 scopus 로고    scopus 로고
    • Mechanisms and control of mRNA turnover in Saccharomyces cerevisiae
    • G. Caponigro, R. Parker, Mechanisms and control of mRNA turnover in Saccharomyces cerevisiae, Microbiol. Rev. 60 (1996) 233-249.
    • (1996) Microbiol. Rev. , vol.60 , pp. 233-249
    • Caponigro, G.1    Parker, R.2
  • 42
    • 0037009517 scopus 로고    scopus 로고
    • The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases
    • DOI 10.1093/emboj/cdf448
    • H.D. Liu, N.D. Rodgers, X. Jiao, M. Kiledjian, The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases, EMBO J. 21 (2002) 4699-4708. (Pubitemid 34984357)
    • (2002) EMBO Journal , vol.21 , Issue.17 , pp. 4699-4708
    • Liu, H.1    Rodgers, N.D.2    Jiao, X.3    Kiledjian, M.4
  • 43
    • 4344641442 scopus 로고    scopus 로고
    • Functional analysis of mRNA scavenger decapping enzymes
    • DOI 10.1261/rna.7660804
    • S. Liu, X. Jiao, H. Liu, M. Gu, C.D. Lima, M. Kiledjian, Functional analysis of mRNA scavenger decapping enzymes, RNA 10 (2004) 1412-1422. (Pubitemid 39122111)
    • (2004) RNA , vol.10 , Issue.9 , pp. 1412-1422
    • Liu, S.-W.1    Jiao, X.2    Liu, H.3    Gu, M.4    Lima, C.D.5    Kiledjian, M.6
  • 44
    • 14844359631 scopus 로고    scopus 로고
    • Crystal structures of human DcpS in ligand-free and m7GDP-bound forms suggest a dynamic mechanism for scavenger mRNA decapping
    • N. Chen, M.A. Walsh, Y. Liu, R. Parker, H. Song, Crystal structures of human DcpS in ligand-free and m7GDP-bound forms suggest a dynamic mechanism for scavenger mRNA decapping, J. Mol. Biol. 347 (2005) 707-718.
    • (2005) J. Mol. Biol. , vol.347 , pp. 707-718
    • Chen, N.1    Walsh, M.A.2    Liu, Y.3    Parker, R.4    Song, H.5
  • 47
    • 41849108751 scopus 로고    scopus 로고
    • High-level QM/MMmodelling predicts an arginine as the acid in the condensation reaction catalysed by citrate synthase
    • M.W. Van Der Kamp, F. Perruccio, A.J. Mulholland, High-level QM/MMmodelling predicts an arginine as the acid in the condensation reaction catalysed by citrate synthase, Chem. Commun. (2008) 1874-1876.
    • (2008) Chem. Commun. , pp. 1874-1876
    • Van Der Kamp, M.W.1    Perruccio, F.2    Mulholland, A.J.3
  • 48
    • 0025214122 scopus 로고    scopus 로고
    • Proposed mechanism for the condensation reaction of citrate synthase: 1.9 Å structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A
    • M. Karpusas, B. Branchaud, S.J. Remington, Proposed mechanism for the condensation reaction of citrate synthase: 1.9 Å structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A, Biochemistry 29 (2002) 2213-2219.
    • (2002) Biochemistry , vol.29 , pp. 2213-2219
    • Karpusas, M.1    Branchaud, B.2    Remington, S.J.3
  • 49
    • 0035958660 scopus 로고    scopus 로고
    • Investigation of the mechanism of domain closure in citrate synthase by molecular dynamics simulation
    • D. Roccatano, A.E. Mark, S. Hayward, Investigation of the mechanism of domain closure in citrate synthase by molecular dynamics simulation, J. Mol. Biol. 310 (2001) 1039-1053.
    • (2001) J. Mol. Biol. , vol.310 , pp. 1039-1053
    • Roccatano, D.1    Mark, A.E.2    Hayward, S.3
  • 50
    • 0024420140 scopus 로고
    • Ligand-induced conformational changes of citrate synthase studied with the fluorescent probe 8-anilinonaphthalene 1-sulfonate
    • A. Kollmann-Koch, H. Eggerer, Ligand-induced conformational changes of citrate synthase studied with the fluorescent probe 8-anilinonaphthalene 1-sulfonate, Eur. J. Biochem. 185 (1989) 441-447.
    • (1989) Eur. J. Biochem. , vol.185 , pp. 441-447
    • Kollmann-Koch, A.1    Eggerer, H.2
  • 51
    • 0015983529 scopus 로고
    • Evidence that citrate synthase operates by an ordered ternary-complex mechanism
    • C.j. Johansso, G. Petterss, Evidence that citrate synthase operates by an ordered ternary-complex mechanism, Eur. J. Biochem. 42 (1974) 383-388.
    • (1974) Eur. J. Biochem. , vol.42 , pp. 383-388
    • Johansso, C.J.1    Petterss, G.2
  • 52
    • 2442612037 scopus 로고    scopus 로고
    • Investigating the accessibility of the closed domain conformation of citrate synthase using essential dynamics sampling
    • I. Daidone, D. Roccatano, S. Hayward, Investigating the accessibility of the closed domain conformation of citrate synthase using essential dynamics sampling, J. Mol. Biol. 339 (2004) 515-525.
    • (2004) J. Mol. Biol. , vol.339 , pp. 515-525
    • Daidone, I.1    Roccatano, D.2    Hayward, S.3
  • 53
    • 34848908954 scopus 로고    scopus 로고
    • Ab initio QM/MM modelling of acetyl-CoA deprotonation in the enzyme citrate synthase
    • M.W. Van Der Kamp, F. Perruccio, A.J. Mulholland, Ab initio QM/MM modelling of acetyl-CoA deprotonation in the enzyme citrate synthase, J. Mol. Graphics Modell. 26 (2007) 676-690.
    • (2007) J. Mol. Graphics Modell. , vol.26 , pp. 676-690
    • Van Der Kamp, M.W.1    Perruccio, F.2    Mulholland, A.J.3
  • 54
    • 35449000157 scopus 로고    scopus 로고
    • Substrate polarization in enzyme catalysis: QM/MM analysis of the effect of oxaloacetate polarization on acetyl-CoA enolization in citrate synthase
    • DOI 10.1002/prot.21482
    • M.W. Van Der Kamp, F. Perruccio, A.J. Mulholland, Substrate polarization in enzyme catalysis: QM/MM analysis of the effect of oxaloacetate polarization on acetyl-CoA enolization in citrate synthase, Proteins: Struct. Funct. Bioinf. 69 (2007) 521-535. (Pubitemid 47623869)
    • (2007) Proteins: Structure, Function and Genetics , vol.69 , Issue.3 , pp. 521-535
    • Van Der, K.M.W.1    Perruccio, F.2    Mulholland, A.J.3
  • 56
    • 0034705612 scopus 로고    scopus 로고
    • Movement of retinal along the visual transduction path
    • DOI 10.1126/science.288.5474.2209
    • B. Borhan, M.L. Souto, H. Imai, Y. Shichida, K. Nakanishi, Movement of retinal along the visual transduction path, Science 288 (2000) 2209-2212. (Pubitemid 30429605)
    • (2000) Science , vol.288 , Issue.5474 , pp. 2209-2212
    • Borhan, B.1    Souto, M.L.2    Imai, H.3    Shichida, Y.4    Nakanishi, K.5
  • 58
    • 0037015153 scopus 로고    scopus 로고
    • Early steps of the intramolecular signal transduction in rhodopsin explored by molecular dynamics simulations
    • DOI 10.1021/bi026011h
    • U.F. Rohrig, L. Guidoni, U. Rothlisberger, Early steps of the intramolecular signal transduction in rhodopsin explored by molecular dynamics simulations, Biochemistry 41 (2002) 10799-10809. (Pubitemid 34971057)
    • (2002) Biochemistry , vol.41 , Issue.35 , pp. 10799-10809
    • Rohrig, U.F.1    Guidoni, L.2    Rothlisberger, U.3
  • 59
    • 0036930078 scopus 로고    scopus 로고
    • Molecular dynamics investigation of primary photoinduced events in the activation of rhodopsin
    • J. Saam, E. Tajkhorshid, S. Hayashi, K. Schulten, Molecular dynamics investigation of primary photoinduced events in the activation of rhodopsin, Biophys. J. 83 (2002) 3097-3112. (Pubitemid 36050036)
    • (2002) Biophysical Journal , vol.83 , Issue.6 , pp. 3097-3112
    • Saam, J.1    Tajkhorshid, E.2    Hayashi, S.3    Schulten, K.4
  • 61
    • 0037426865 scopus 로고    scopus 로고
    • Rhodopsin dimers in native disc membranes
    • DOI 10.1038/421127a
    • D. Fotiadis, Y. Liang, S. Filipek, D.A. Saperstein, A. Engel, K. Palczewski, Atomic-force microscopy: Rhodopsin dimers in native disc membranes, Nature 421 (2003) 127-128. (Pubitemid 36090969)
    • (2003) Nature , vol.421 , Issue.6919 , pp. 127-128
    • Fotiadis, D.1    Liang, Y.2    Filipek, S.3    Saperstein, D.A.4    Engel, A.5    Palczewski, K.6
  • 64
    • 72449147362 scopus 로고    scopus 로고
    • Dimerization in GPCR mobility and signaling
    • M.J. Lohse, Dimerization in GPCR mobility and signaling, Curr. Opin. Pharmacol. 10 (2010) 53-58.
    • (2010) Curr. Opin. Pharmacol. , vol.10 , pp. 53-58
    • Lohse, M.J.1
  • 68
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Y. Liang, D. Fotiadis, S. Filipek, D.A. Saperstein, K. Palczewski, A. Engel, Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes, J. Biol. Chem. 278 (2003) 21655-21662.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21655-21662
    • Liang, Y.1    Fotiadis, D.2    Filipek, S.3    Saperstein, D.A.4    Palczewski, K.5    Engel, A.6
  • 71
    • 66749144240 scopus 로고    scopus 로고
    • Observation of "Ionic Lock" Formation in Molecular Dynamics Simulations of Wild-Type beta(1) and beta(2) Adrenergic Receptors
    • S. Vanni, M. Neri, I. Tavernelli, U. Röthlisberger, Observation of "Ionic Lock" Formation in Molecular Dynamics Simulations of Wild-Type beta(1) and beta(2) Adrenergic Receptors, Biochemistry 48 (2009) 4789-4797.
    • (2009) Biochemistry , vol.48 , pp. 4789-4797
    • Vanni, S.1    Neri, M.2    Tavernelli, I.3    Röthlisberger, U.4
  • 72
    • 77950517052 scopus 로고    scopus 로고
    • A Conserved Protonation-Induced Switch can Trigger "Ionic-Lock" Formation in Adrenergic Receptors
    • S. Vanni, M. Neri, I. Tavernelli, U. Röthlisberger, A Conserved Protonation-Induced Switch can Trigger "Ionic-Lock" Formation in Adrenergic Receptors, J. Mol. Biol. 397 (2010) 1339-1349.
    • (2010) J. Mol. Biol. , vol.397 , pp. 1339-1349
    • Vanni, S.1    Neri, M.2    Tavernelli, I.3    Röthlisberger, U.4
  • 74
    • 0033167047 scopus 로고    scopus 로고
    • Accelerated molecular dynamics of infrequent events
    • S. Pal, K.A. Fichthorn, Accelerated molecular dynamics of infrequent events, Chem. Eng. J. 74 (1999) 77-83.
    • (1999) Chem. Eng. J. , vol.74 , pp. 77-83
    • Pal, S.1    Fichthorn, K.A.2
  • 75
    • 33644968698 scopus 로고    scopus 로고
    • Metadynamics as a tool for exploring free energy landscapes of chemical reactions
    • B. Ensing, M. De Vivo, Z.W. Liu, P. Moore, M.L. Klein, Metadynamics as a tool for exploring free energy landscapes of chemical reactions, Acc. Chem. Res. 39 (2006) 73-81.
    • (2006) Acc. Chem. Res. , vol.39 , pp. 73-81
    • Ensing, B.1    De Vivo, M.2    Liu, Z.W.3    Moore, P.4    Klein, M.L.5
  • 76
    • 0028455053 scopus 로고
    • Targeted molecular dynamics: A new approach for searching pathways of conformational transitions
    • J. Schlitter, M. Engels, P. Kruger, Targeted molecular dynamics: a new approach for searching pathways of conformational transitions, J. Mol. Graphics Modell. 12 (1994) 84-89.
    • (1994) J. Mol. Graphics Modell. , vol.12 , pp. 84-89
    • Schlitter, J.1    Engels, M.2    Kruger, P.3
  • 79
    • 0034655949 scopus 로고    scopus 로고
    • The morph server: A standardized system for analyzing and visualizing macromolecular motions in a database framework
    • W.G. Krebs, M. Gerstein, The morph server: a standardized system for analyzing and visualizing macromolecular motions in a database framework, Nucleic Acids Res. 28 (2000) 1665-1675. (Pubitemid 30199298)
    • (2000) Nucleic Acids Research , vol.28 , Issue.8 , pp. 1665-1675
    • Krebs, W.G.1    Gerstein, M.2
  • 81
    • 46449096932 scopus 로고    scopus 로고
    • Vibrational excitation through tug-of-war inelastic collisions
    • DOI 10.1038/nature07079, PII NATURE07079
    • S.J. Greaves, E. Wrede, N.T. Goldberg, J. Zhang, D.J. Miller, R.N. Zare, Vibrational excitation through tug-of-war inelastic collisions, Nature 454 (2008) 88-91. (Pubitemid 351931981)
    • (2008) Nature , vol.454 , Issue.7200 , pp. 88-91
    • Greaves, S.J.1    Wrede, E.2    Goldberg, N.T.3    Zhang, J.4    Miller, D.J.5    Zare, R.N.6
  • 82
    • 0035707451 scopus 로고    scopus 로고
    • Dynamics of biochemical and biophysical reactions: Insight from computer simulations
    • A. Warshel, W.W. Parson, Dynamics of biochemical and biophysical reactions: insight from computer simulations, Q. Rev. Biophys. 34 (2001) 563-679. (Pubitemid 34127275)
    • (2001) Quarterly Reviews of Biophysics , vol.34 , Issue.4 , pp. 563-679
    • Warshel, A.1    Parson, W.W.2
  • 83
    • 33646935697 scopus 로고    scopus 로고
    • Dynamical contributions to enzyme catalysis: Critical tests of a popular hypothesis
    • M.H.M. Olsson, W.W. Parson, A. Warshel, Dynamical contributions to enzyme catalysis: Critical tests of a popular hypothesis, Chem. Rev. (2006) 1737-1756.
    • (2006) Chem. Rev. , pp. 1737-1756
    • Olsson, M.H.M.1    Parson, W.W.2    Warshel, A.3
  • 84
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate
    • DOI 10.1038/35090602
    • D.J. Vocadlo, G.J. Davies, R. Laine, S.G. Withers, Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate, Nature 412 (2001) 835-838. (Pubitemid 32801467)
    • (2001) Nature , vol.412 , Issue.6849 , pp. 835-838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 85
    • 52449116184 scopus 로고    scopus 로고
    • QM/MM simulations predict a covalent intermediate in the hen egg white lysozyme reaction with its natural substrate
    • A.L. Bowman, I.M. Grant, A.J. Mulholland, QM/MM simulations predict a covalent intermediate in the hen egg white lysozyme reaction with its natural substrate, Chem. Commun. (2008) 4425-4427.
    • (2008) Chem. Commun. , pp. 4425-4427
    • Bowman, A.L.1    Grant, I.M.2    Mulholland, A.J.3
  • 87
    • 0027023534 scopus 로고
    • Simulation analysis of triosephosphate isomerase: Conformational transition and catalysis
    • M. Karplus, J.D. Evanseck, D. Joseph, P.A. Bash, M.J. Field, Simulation analysis of triosephosphate isomerase: conformational transition and catalysis, Faraday Discuss. 93 (1992) 239-248.
    • (1992) Faraday Discuss. , vol.93 , pp. 239-248
    • Karplus, M.1    Evanseck, J.D.2    Joseph, D.3    Bash, P.A.4    Field, M.J.5
  • 88
    • 0024282745 scopus 로고
    • Triosephosphate isomerase: Removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism
    • E.B. Nickbarg, R.C. Davenport, G.A. Petsko, J.R. Knowles, Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism, Biochemistry 27 (1988) 5948-5960.
    • (1988) Biochemistry , vol.27 , pp. 5948-5960
    • Nickbarg, E.B.1    Davenport, R.C.2    Petsko, G.A.3    Knowles, J.R.4
  • 89
    • 0038305457 scopus 로고    scopus 로고
    • Quantum chemical studies of radical-containing enzymes
    • F. Himo, P.E.M. Siegbahn, Quantum chemical studies of radical-containing enzymes, Chem. Rev. 103 (2003) 2421-2456.
    • (2003) Chem. Rev. , vol.103 , pp. 2421-2456
    • Himo, F.1    Siegbahn, P.E.M.2
  • 90
    • 67649476220 scopus 로고    scopus 로고
    • Recent developments of the quantum chemical cluster approach for modeling enzyme reactions
    • P.E.M. Siegbahn, F. Himo, Recent developments of the quantum chemical cluster approach for modeling enzyme reactions, J. Biol. Inorg. Chem. 14 (2009) 643-651.
    • (2009) J. Biol. Inorg. Chem. , vol.14 , pp. 643-651
    • Siegbahn, P.E.M.1    Himo, F.2
  • 91
    • 25444523794 scopus 로고    scopus 로고
    • QM/MM modelling of oleamide hydrolysis in fatty acid amide hydrolase (FAAH) reveals a newmechanism of nucleophile activation
    • A. Lodola, M. Mor, J.C. Hermann, G. Tarzia, D. Piomelli, A.J. Mulholland, QM/MM modelling of oleamide hydrolysis in fatty acid amide hydrolase (FAAH) reveals a newmechanism of nucleophile activation, Chem. Commun. 10 (2005) 4399-4401.
    • (2005) Chem. Commun. , vol.10 , pp. 4399-4401
    • Lodola, A.1    Mor, M.2    Hermann, J.C.3    Tarzia, G.4    Piomelli, D.5    Mulholland, A.J.6
  • 92
    • 77949868796 scopus 로고    scopus 로고
    • Investigations of enzyme-catalysed reactions with combined quantum mechanics/molecular mechanics (QM/MM) methods
    • K.E. Ranaghan, A.J. Mulholland, Investigations of enzyme-catalysed reactions with combined quantum mechanics/molecular mechanics (QM/MM) methods, Int. Rev. Phys. Chem. 29 (2010) 65-133.
    • (2010) Int. Rev. Phys. Chem. , vol.29 , pp. 65-133
    • Ranaghan, K.E.1    Mulholland, A.J.2
  • 93
    • 60349127442 scopus 로고    scopus 로고
    • QM/MM Methods for biomolecular systems
    • H.M. Senn, W. Thiel, QM/MM Methods for biomolecular systems, Angew. Chem. Int. Edit. 48 (2009) 1198-1229.
    • (2009) Angew. Chem. Int. Edit. , vol.48 , pp. 1198-1229
    • Senn, H.M.1    Thiel, W.2
  • 94
    • 0017100947 scopus 로고
    • Theoretical studies of enzymic reactions: Dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme
    • A. Warshel, M. Levitt, Theoretical studies of enzymic reactions: Dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme, J. Mol. Biol. 103 (1976) 227-249.
    • (1976) J. Mol. Biol. , vol.103 , pp. 227-249
    • Warshel, A.1    Levitt, M.2
  • 96
    • 78149341694 scopus 로고    scopus 로고
    • Inclusion of Dispersion Effects Significantly Improves Accuracy of Calculated Reaction Barriers for Cytochrome P450 Catalyzed Reaction
    • R. Lonsdale, J.N. Harvey, A.J. Mulholland, Inclusion of Dispersion Effects Significantly Improves Accuracy of Calculated Reaction Barriers for Cytochrome P450 Catalyzed Reaction, J. Phys. Chem. Letts. 1 (2010) 3232-3237.
    • (2010) J. Phys. Chem. Letts. , vol.1 , pp. 3232-3237
    • Lonsdale, R.1    Harvey, J.N.2    Mulholland, A.J.3
  • 97
    • 38349061612 scopus 로고    scopus 로고
    • Toward accurate barriers for enzymatic reactions: QM/MM case study on p-hydroxybenzoate hydroxylase
    • R.A. Mata, H.J. Werner, S. Thiel, W. Thiel, Toward accurate barriers for enzymatic reactions: QM/MM case study on p-hydroxybenzoate hydroxylase, J. Chem. Phys. 128 (2008) 4867-4875.
    • (2008) J. Chem. Phys. , vol.128 , pp. 4867-4875
    • Mata, R.A.1    Werner, H.J.2    Thiel, S.3    Thiel, W.4
  • 98
    • 77956092555 scopus 로고    scopus 로고
    • Testing high-level QM/MM methods for modeling enzyme reactions: Acetyl-CoA deprotonation in citrate synthase
    • M.W. Van Der Kamp, J. Zurek, F.R. Manby, J.N. Harvey, A.J. Mulholland, Testing high-level QM/MM methods for modeling enzyme reactions: acetyl-CoA deprotonation in citrate synthase, J. Phys. Chem. B 114 (2010) 11303-11314.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 11303-11314
    • Van Der Kamp, M.W.1    Zurek, J.2    Manby, F.R.3    Harvey, J.N.4    Mulholland, A.J.5
  • 99
    • 0346726109 scopus 로고    scopus 로고
    • How Enzymes Work: Analysis by Modern Rate Theory and Computer Simulations
    • DOI 10.1126/science.1088172
    • M. Garcia-Viloca, J. Gao, M. Karplus, D.G. Truhlar, How enzymes work: Analysis by modern rate theory and computer simulations, Science 303 (2004) 186-195. (Pubitemid 38057561)
    • (2004) Science , vol.303 , Issue.5655 , pp. 186-195
    • Garcia-Viloca, M.1    Gao, J.2    Karplus, M.3    Truhlar, D.G.4
  • 100
    • 33748613208 scopus 로고    scopus 로고
    • Multidimensional tunneling, recrossing, and the transmission coefficient for enzymatic reactions
    • DOI 10.1021/cr050308e
    • J.Z. Pu, J. Gao, D. Truhlar, Multidimensional tunneling, recrossing, and the transmission coefficient for enzymatic reactions, Chem. Rev. 106 (2006) 3140-3169. (Pubitemid 44376930)
    • (2006) Chemical Reviews , vol.106 , Issue.8 , pp. 3140-3169
    • Pu, J.1    Gao, J.2    Truhlar, D.G.3
  • 101
    • 1842531419 scopus 로고    scopus 로고
    • Pivotal Role of Gly 121 in Dihydrofolate Reductase from Escherichia coli: The Altered Structure of A Mutant Enzyme May Form the Basis of Its Diminished Catalytic Performance
    • DOI 10.1021/bi036164k
    • R.S. Swanwick, P.J. Shrimpton, R.K. Allemann, Pivotal role of Gly 121 in dihydrofolate reductase from Escherichia coli: The altered structure of a mutant enzyme may form the basis of its diminished catalytic performance, Biochemistry 43 (2004) 4119-4127. (Pubitemid 38445631)
    • (2004) Biochemistry , vol.43 , Issue.14 , pp. 4119-4127
    • Swanwick, R.S.1    Shrimpton, P.J.2    Allemann, R.K.3
  • 102
    • 0035940264 scopus 로고    scopus 로고
    • Energetics and dynamics of enzymatic reactions
    • J. Villa, A. Warshel, Energetics and dynamics of enzymatic reactions, J. Phys. Chem. B 105 (2001) 7887-7907.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 7887-7907
    • Villa, J.1    Warshel, A.2
  • 103
    • 0344924796 scopus 로고    scopus 로고
    • Comment on "Effect of Active Site Mutation Phe93 -> Trp in the Horse Liver Alcohol Dehydrogenase Enzyme on Catalysis: A Molecular Dynamics Study"
    • A. Warshel, J. Villa-Freixa, Comment on "Effect of Active Site Mutation Phe93 -> Trp in the Horse Liver Alcohol Dehydrogenase Enzyme on Catalysis: A Molecular Dynamics Study", J. Phys. Chem. B 107 (2003) 12370-12371.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 12370-12371
    • Warshel, A.1    Villa-Freixa, J.2
  • 104
    • 33644825853 scopus 로고    scopus 로고
    • Testing the nature of the Lambda (1520)-resonance in proton-induced production
    • L. Roca, C. Hanhart, E. Oset, U.G. Meissner, Testing the nature of the Lambda (1520)-resonance in proton-induced production, Eur. Phys. J. A 27 (2006) 373-380.
    • (2006) Eur. Phys. J. A , vol.27 , pp. 373-380
    • Roca, L.1    Hanhart, C.2    Oset, E.3    Meissner, U.G.4
  • 105
    • 77956545132 scopus 로고    scopus 로고
    • Theoretical study of the temperature dependence of dynamic effects in thymidylate synthase
    • N. Kanaan, M. Roca, I. Tunon, S. Marti, V. Moliner, Theoretical study of the temperature dependence of dynamic effects in thymidylate synthase, Phys. Chem. Chem. Phys. 12 (2010) 11657-11664.
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 11657-11664
    • Kanaan, N.1    Roca, M.2    Tunon, I.3    Marti, S.4    Moliner, V.5
  • 106
    • 33748365234 scopus 로고    scopus 로고
    • Transition state theory can be used in studies of enzyme catalysis: Lessons from simulations of tunnelling and dynamical effects in lipoxygenase and other systems
    • DOI 10.1098/rstb.2006.1880
    • M.H.M. Olsson, J. Mavri, A. Warshel, Transition state theory can be used in studies of enzyme catalysis: lessons from simulations of tunnelling and dynamical effects in lipoxygenase and other systems, Phil. Trans. R. Soc. B 361 (2006) 1417-1432. (Pubitemid 44338501)
    • (2006) Philosophical Transactions of the Royal Society B: Biological Sciences , vol.361 , Issue.1472 , pp. 1417-1432
    • Olsson, M.H.M.1    Mavri, J.2    Warshel, A.3
  • 107
    • 44949134134 scopus 로고    scopus 로고
    • Dynamic effects on reaction rates in a Michael addition catalyzed by chalcone isomerase. Beyond the frozen environment approach
    • DOI 10.1021/ja801156y
    • J.J. Ruiz-Pernia, I. Tunon, V. Moliner, J.T. Hynes, M. Roca, Dynamic effects on reaction rates in a Michael addition catalyzed by chalcone isomerase. Beyond the frozen environment approach, J. Am. Chem. Soc. 130 (2008) 7477-7488. (Pubitemid 351813242)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.23 , pp. 7477-7488
    • Ruiz-Pernia, J.J.1    Tunon, I.2    Moliner, V.3    Hynes, J.T.4    Roca, M.5
  • 108
    • 38749105097 scopus 로고    scopus 로고
    • Using grote-hynes theory to quantify dynamical effects on the reaction rate of enzymatic processes. The case of methyltransferases
    • DOI 10.1021/jp077660b
    • R. Castillo, M. Roca, A. Soriano, V. Moliner, I. Tunon, Using Grote-Hynes theory to quantify dynamical effects on the reaction rate of enzymatic processes. The case of methyltransferases, J. Phys. Chem. B 112 (2008) 529-534. (Pubitemid 351184626)
    • (2008) Journal of Physical Chemistry B , vol.112 , Issue.2 , pp. 529-534
    • Castillo, R.1    Roca, M.2    Soriano, A.3    Moliner, V.4    Tunon, I.5
  • 110
    • 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 (1989) 3537-3558.
    • (1989) J. Chem. Phys. , vol.90 , pp. 3537-3558
    • Gertner, B.J.1    Wilson, K.R.2    Hynes, J.T.3
  • 111
    • 33748274620 scopus 로고
    • Non-equilibrium solvation dynamics in solution reactions
    • G. Vanderzwan, J.T. Hynes, Non-equilibrium solvation dynamics in solution reactions, J. Chem. Phys. 78 (1983) 4174-4185.
    • (1983) J. Chem. Phys. , vol.78 , pp. 4174-4185
    • Vanderzwan, G.1    Hynes, J.T.2
  • 112
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and the diffusion model of chemical reactions
    • H.A. Kramers, Brownian motion in a field of force and the diffusion model of chemical reactions, Physica 7 (1940) 284-304.
    • (1940) Physica , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 113
    • 1242307783 scopus 로고    scopus 로고
    • Vibrationally Enhanced Hydrogen Tunneling in the Escherichia coli Thymidylate Synthase Catalyzed Reaction
    • DOI 10.1021/bi036124g
    • N. Agrawal, B. Hong, C. Mihai, A. Kohen, Vibrationally enhanced hydrogen tunneling in the Escherichia coli thymidylate synthase catalyzed reaction, Biochemistry 43 (2004) 1998-2006. (Pubitemid 38233262)
    • (2004) Biochemistry , vol.43 , Issue.7 , pp. 1998-2006
    • Agrawal, N.1    Hong, B.2    Mihai, C.3    Kohen, A.4
  • 114
    • 0000205312 scopus 로고    scopus 로고
    • Enzyme Catalysis: Beyond Classical Paradigms
    • A. Kohen, J.P. Klinman, Enzyme catalysis: Beyond classical paradigms, Acc. Chem. Res. 31 (1998) 397-404. (Pubitemid 128474600)
    • (1998) Accounts of Chemical Research , vol.31 , Issue.7 , pp. 397-404
    • Kohen, A.1    Klinman, J.P.2
  • 117
    • 62249181529 scopus 로고    scopus 로고
    • An integrated model for enzyme catalysis emerges from studies of hydrogen tunneling
    • J.P. Klinman, An integrated model for enzyme catalysis emerges from studies of hydrogen tunneling, Chem. Phys. Lett. 471 (2009) 179-193.
    • (2009) Chem. Phys. Lett. , vol.471 , pp. 179-193
    • Klinman, J.P.1
  • 118
    • 68049093016 scopus 로고    scopus 로고
    • Enzymatic transition states and dynamic motion in barrier crossing
    • S.D. Schwartz, V.L. Schramm, Enzymatic transition states and dynamic motion in barrier crossing, Nat. Chem. Biol. 5 (2009) 552-559.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 552-559
    • Schwartz, S.D.1    Schramm, V.L.2
  • 119
    • 76149097495 scopus 로고    scopus 로고
    • A Stationary-Wave Model of Enzyme Catalysis
    • C. Canepa, A Stationary-Wave Model of Enzyme Catalysis, J. Comput. Chem. 31 (2010) 343-350.
    • (2010) J. Comput. Chem. , vol.31 , pp. 343-350
    • Canepa, C.1
  • 120
    • 0034644411 scopus 로고    scopus 로고
    • A quantum mechanical/molecular mechanical study of the hydroxylation of phenol and halogenated derivatives by phenol hydroxylase
    • L. Ridder, A.J. Mulholland, I.M.C.M. Rietjens, J. Vervoort, A quantum mechanical/molecular mechanical study of the hydroxylation of phenol and halogenated derivatives by phenol hydroxylase, J. Am. Chem. Soc. 122 (2000) 8728-8738.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8728-8738
    • Ridder, L.1    Mulholland, A.J.2    Rietjens, I.M.C.M.3    Vervoort, J.4
  • 121
    • 77952355806 scopus 로고    scopus 로고
    • Role of conformation transitions in adenylate kinase
    • author reply E72
    • M. Karplus, Role of conformation transitions in adenylate kinase, Proc. Natl. Acad. Sci. USA 107 (2010) E718 author reply E72.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107
    • Karplus, M.1
  • 122
    • 77952340641 scopus 로고    scopus 로고
    • Reply to Karplus: Conformational dynamics have no role in the chemical step
    • S.C.L. Kamerlin, A. Warshel, Reply to Karplus: Conformational dynamics have no role in the chemical step, Proc. Natl. Acad. Sci. USA 107 (2010) E72-E.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107
    • Kamerlin, S.C.L.1    Warshel, A.2
  • 123
    • 70350453758 scopus 로고    scopus 로고
    • Enzyme millisecond conformational dynamics do not catalyze the chemical step
    • A.V. Pisliakov, J. Cao, S.C.L. Kamerlin, A. Warshel, Enzyme millisecond conformational dynamics do not catalyze the chemical step, Proc. Natl. Acad. Sci. USA 106 (2009) 17359-17364.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 17359-17364
    • Pisliakov, A.V.1    Cao, J.2    Kamerlin, S.C.L.3    Warshel, A.4
  • 124
    • 38749105098 scopus 로고    scopus 로고
    • Two-dimensional reaction free energy surfaces of catalytic reaction: Effects of protein conformational dynamics on enzyme catalysis
    • W. Min, X.S. Xie, B. Bagchi, Two-dimensional reaction free energy surfaces of catalytic reaction: effects of protein conformational dynamics on enzyme catalysis, J. Phys. Chem. B 112 (2008) 454-466.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 454-466
    • Min, W.1    Xie, X.S.2    Bagchi, B.3
  • 125
    • 0029927729 scopus 로고    scopus 로고
    • Mutagenesis study of active site residues in chorismate mutase from bacillus subtilis
    • S.T. Cload, D.R. Liu, R.M. Pastor, P.G. Schultz, Mutagenesis study of active site residues in chorismate mutase from bacillus subtilis, J. Am. Chem. Soc. 118 (1996) 1787-1788.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 1787-1788
    • Cload, S.T.1    Liu, D.R.2    Pastor, R.M.3    Schultz, P.G.4
  • 126
    • 0029928213 scopus 로고    scopus 로고
    • Is chorismate mutase a prototypic entropy trap? - Activation parameters for the Bacillus subtilis enzyme
    • DOI 10.1016/0040-4039(96)00338-3
    • P. Kast, M. Asif-Ullah, D. Hilvert, Is chorismate mutase a prototypic entropy trap? - Activation parameters for the Bacillus subtilis enzyme, Tetrahedron Lett. 37 (1996) 2691-2694. (Pubitemid 26126379)
    • (1996) Tetrahedron Letters , vol.37 , Issue.16 , pp. 2691-2694
    • Kast, P.1    Asif-Ullah, M.2    Hilvert, D.3
  • 127
    • 0142052240 scopus 로고    scopus 로고
    • Selective stabilization of the chorismate mutase transition state by a positively charged hydrogen bond donor
    • DOI 10.1021/ja0341992
    • A. Kienhofer, P. Kast, D. Hilvert, Selective stabilization of the chorismate mutase transition state by a positively charged hydrogen bond donor, J. Am. Chem. Soc. 125 (2003) 3206-3207. (Pubitemid 36512450)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.11 , pp. 3206-3207
    • Kienhofer, A.1    Kast, P.2    Hilvert, D.3
  • 128
    • 0000167881 scopus 로고
    • Insights into chorismate mutase catalysis from a combined QM/MM simulation of the enzyme reaction
    • P.D. Lyne, A.J. Mulholland, W.G. Richards, Insights into chorismate mutase catalysis from a combined QM/MM simulation of the enzyme reaction, J. Am. Chem. Soc. 117 (1995) 11345-11350.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11345-11350
    • Lyne, P.D.1    Mulholland, A.J.2    Richards, W.G.3
  • 129
    • 0037153275 scopus 로고    scopus 로고
    • Reaction mechanism of chorismate mutase studied by the combined potentials of quantum mechanics and molecular mechanics
    • Y.S. Lee, S.E. Worthington, M. Krauss, B.R. Brooks, Reaction mechanism of chorismate mutase studied by the combined potentials of quantum mechanics and molecular mechanics, J. Phys. Chem. B 106 (2002) 12059-12065.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 12059-12065
    • Lee, Y.S.1    Worthington, S.E.2    Krauss, M.3    Brooks, B.R.4
  • 130
    • 0041429611 scopus 로고    scopus 로고
    • Apparent NAC effect in chorismate mutase reflects electrostatic transition state stabilization
    • DOI 10.1021/ja0356481
    • M. Strajbl, A. Shurki, M. Kato, A. Warshel, Apparent NAC effect in chorismate mutase reflects electrostatic transition state stabilization, J. Am. Chem. Soc. 125 (2003) 10228-10237. (Pubitemid 37022233)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.34 , pp. 10228-10237
    • Strajbl, M.1    Shurki, A.2    Kato, M.3    Warshel, A.4
  • 131
    • 0346885688 scopus 로고    scopus 로고
    • A DFT-based QM-MM approach designed for the treatment of large molecular systems: Application to chorismate mutase
    • A. Crespo, D.A. Scherlis, M.A. Marti, P. Ordejon, A.E. Roitberg, D.A. Estrin, A DFT-based QM-MM approach designed for the treatment of large molecular systems: application to chorismate mutase, J. Phys. Chem. 107 (2003) 13728-13736.
    • (2003) J. Phys. Chem. , vol.107 , pp. 13728-13736
    • Crespo, A.1    Scherlis, D.A.2    Marti, M.A.3    Ordejon, P.4    Roitberg, A.E.5    Estrin, D.A.6
  • 132
    • 18244376600 scopus 로고    scopus 로고
    • Investigation of ligand binding and protein dynamics in Bacillus subtilis chorismate mutase by transverse relaxation optimized spectroscopy-nuclear magnetic resonance
    • DOI 10.1021/bi0474259
    • A. Eletsky, A. Kienhofer, D. Hilvert, K. Pervushin, Investigation of ligand binding and protein dynamics in bacillus subtilis chorismate mutase by transverse relaxation optimized spectroscopy nuclear magnetic resonance, Biochemistry 44 (2005) 6788-6799. (Pubitemid 40632397)
    • (2005) Biochemistry , vol.44 , Issue.18 , pp. 6788-6799
    • Eletsky, A.1    Kienhofer, A.2    Hilvert, D.3    Pervushin, K.4
  • 133
  • 134
    • 27644492410 scopus 로고    scopus 로고
    • Multiple high-level QM/MM reaction paths demonstrate transition-state stabilization in chorismate mutase: Correlation of barrier height with transition-state stabilization
    • F. Claeyssens, K.E. Ranaghan, F.R. Manby, J.N. Harvey, A.J. Mulholland, Multiple high-level QM/MM reaction paths demonstrate transition-state stabilization in chorismate mutase: correlation of barrier height with transition-state stabilization, Chem. Commun. (2005) 5068-5070.
    • (2005) Chem. Commun. , pp. 5068-5070
    • Claeyssens, F.1    Ranaghan, K.E.2    Manby, F.R.3    Harvey, J.N.4    Mulholland, A.J.5
  • 135
    • 23244446189 scopus 로고    scopus 로고
    • A definitive mechanism for chorismate mutase
    • DOI 10.1021/bi050886p
    • X. Zhang, T.C. Bruice, A Definitive Mechanism for chorismate mutase, Biochemistry 44 (2005) 10443-10448. (Pubitemid 41098220)
    • (2005) Biochemistry , vol.44 , Issue.31 , pp. 10443-10448
    • Zhang, X.1    Zhang, X.2    Bruice, T.C.3
  • 137
    • 2342565009 scopus 로고    scopus 로고
    • Transition state stabilization and substrate strain in enzyme catalysis: Ab initio QM/MM modelling of the chorismate mutase reaction
    • K.E. Ranaghan, L. Ridder, B. Szefczyk, A. Sokalski, H.J. C. and A.J. Mulholland, Transition state stabilization and substrate strain in enzyme catalysis: ab initio QM/MM modelling of the chorismate mutase reaction, Org. Biomol. Chem. 2 (2004) 968-980.
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 968-980
    • Ranaghan, K.E.1    Ridder, L.2    Szefczyk, B.3    Sokalski, A.4    C, H.J.5    Mulholland, A.J.6
  • 138
    • 18744400238 scopus 로고    scopus 로고
    • Multiple-steering QM-MM calculation of the free energy profile in chorismate mutase
    • DOI 10.1021/ja0452830
    • A. Crespo, M.A. Marti, D.A. Estrin, A.E. Roitberg, Multiple-steering QMMM calculation of the free energy profile in chorismate mutase, J. Am. Chem. Soc. 127 (2005) 6940-6941. (Pubitemid 40676708)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.19 , pp. 6940-6941
    • Crespo, A.1    Marti, M.A.2    Estrin, D.A.3    Roitberg, A.E.4
  • 139
    • 33644508642 scopus 로고    scopus 로고
    • All electron quantum chemical calculation of the entire enzyme system confirms a collective catalytic device in the chorismate mutase reaction
    • T. Ishida, D.G. Fedorov, K. Kitaura, All electron quantum chemical calculation of the entire enzyme system confirms a collective catalytic device in the chorismate mutase reaction, J. Phys. Chem. B 110 (2005) 1457-1463.
    • (2005) J. Phys. Chem. B , vol.110 , pp. 1457-1463
    • Ishida, T.1    Fedorov, D.G.2    Kitaura, K.3
  • 141
    • 0038634537 scopus 로고    scopus 로고
    • Comparison of formation of reactive conformers (NACs) for the Claisen rearrangement of chorismate to prephenate in water and in the E. coli mutase: The efficiency of the enzyme catalysis
    • DOI 10.1021/ja0210648
    • S. Hur, T.C. Bruice, Comparison of formation of reactive conformers (NACs) for the Claisen rearrangement of chorismate to prephenate in water and in the E-coli mutase: The efficiency of the enzyme catalysis, J. Am. Chem. Soc. 125 (2003) 5964-5972. (Pubitemid 36592919)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.19 , pp. 5964-5972
    • Hur, S.1    Bruice, T.C.2
  • 142
    • 0001138032 scopus 로고    scopus 로고
    • The conformational equilibrium of chorismate in solution: Implications for the mechanism of the non-enzymic and the enzyme-catalyzed rearrangement of chorismate to prephenate
    • S.D. Copley, J.R. Knowles, The conformational equilibrium of chorismate in solution: implications for the mechanism of the non-enzymic and the enzyme-catalyzed rearrangement of chorismate to prephenate, J. Am. Chem. Soc. 109 (2002) 5008-5013.
    • (2002) J. Am. Chem. Soc. , vol.109 , pp. 5008-5013
    • Copley, S.D.1    Knowles, J.R.2
  • 143
    • 2942739060 scopus 로고    scopus 로고
    • Conformational effects in enzyme catalysis: QM/MM free energy calculation of the NAC contribution in chorismate mutase
    • K.E. Ranaghan, A.J. Mulholland, Conformational effects in enzyme catalysis: QM/MM free energy calculation of the NAC contribution in chorismate mutase, Chem. Commun. (2004) 1238-1239.
    • (2004) Chem. Commun. , pp. 1238-1239
    • Ranaghan, K.E.1    Mulholland, A.J.2
  • 144
    • 10344265555 scopus 로고    scopus 로고
    • Differential transition-state stabilization in enzyme catalysis: Quantum chemical analysis of interactions in the chorismate mutase reaction and prediction of the optimal catalytic field
    • DOI 10.1021/ja049376t
    • B. Szefczyk, A.J. Mulholland, K.E. Ranaghan, W.A. Sokalski, Differential transitionstate stabilization in enzyme catalysis: quantum chemical analysis of interactions in the chorismate mutase reaction and prediction of the optimal catalytic field, J. Am. Chem. Soc. 126 (2004) 16148-16159. (Pubitemid 39627626)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.49 , pp. 16148-16159
    • Szefczyk, B.1    Mulholland, A.J.2    Ranaghan, K.E.3    Sokalski, W.A.4
  • 145
    • 2342565009 scopus 로고    scopus 로고
    • Transition state stabilization and substrate strain in enzyme catalysis: Ab initio QM/MM modelling of the chorismate mutase reaction
    • K.E. Ranaghan, L. Ridder, B. Szefczyk, W.A. Sokalski, J.C. Hermann, A.J. Mulholland, Transition state stabilization and substrate strain in enzyme catalysis: ab initio QM/MM modelling of the chorismate mutase reaction, Org. Biomol. Chem. 2 (2004) 968-980.
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 968-980
    • Ranaghan, K.E.1    Ridder, L.2    Szefczyk, B.3    Sokalski, W.A.4    Hermann, J.C.5    Mulholland, A.J.6
  • 146
    • 33846413566 scopus 로고    scopus 로고
    • Conformational effects in enzyme catalysis: Reaction via a high energy conformation in fatty acid amide hydrolase
    • DOI 10.1529/biophysj.106.098434
    • A. Lodola, M. Mor, J. Zurek, G. Tarzia, D. Piomelli, J.N. Harvey, A.J. Mulholland, Conformational Effects in Enzyme Catalysis: Reaction via a high energy conformation in fatty acid amide hydrolase, Biophys. J. 92 (2007) L20-L22. (Pubitemid 46145768)
    • (2007) Biophysical Journal , vol.92 , Issue.2
    • Lodola, A.1    Mor, M.2    Zurek, J.3    Tarzia, G.4    Piomelli, D.5    Harvey, J.N.6    Mulholland, A.J.7
  • 147
    • 77956595530 scopus 로고    scopus 로고
    • Structural fluctuations in enzyme-catalyzed reactions: Determinants of reactivity in fatty acid amide hydrolase from multivariate statistical analysis of quantum mechanics/molecular mechanics paths
    • A. Lodola, J. Sirirak, N. Fey, S. Rivara, M.Mor, A.J.Mulholland, Structural fluctuations in enzyme-catalyzed reactions: determinants of reactivity in fatty acid amide hydrolase from multivariate statistical analysis of quantum mechanics/molecular mechanics paths, J. Chem. Theory Comput. 6 (2010) 2948-2960.
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 2948-2960
    • Lodola, A.1    Sirirak, J.2    Fey, N.3    Rivara, S.4    Mor, M.5    Mulholland, A.J.6
  • 148
    • 0345303765 scopus 로고    scopus 로고
    • Anandamide hydrolysis: A new target for anti-anxiety drugs?
    • DOI 10.1016/j.molmed.2003.09.005
    • S. Gaetani, V. Cuomo, D. Piomelli, Anandamide hydrolysis: a new target for anti-anxiety drugs? Trends Mol. Med. 9 (2003) 474-478. (Pubitemid 37464283)
    • (2003) Trends in Molecular Medicine , vol.9 , Issue.11 , pp. 474-478
    • Gaetani, S.1    Cuomo, V.2    Piomelli, D.3
  • 153
    • 4744354729 scopus 로고    scopus 로고
    • Cyclohexylcarbamic acid 3′- or 4′-substituted biphenyl-3-yl esters as fatty acid amide hydrolase inhibitors: Synthesis, quantitative structure - activity relationships, and molecular modeling studies
    • M. Mor, S. Rivara, A. Lodola, P.V. Plazzi, G. Tarzia, A. Duranti, A. Tontini, G. Piersanti, S. Kathuria, D. Piomelli, Cyclohexylcarbamic acid 3′- or 4′-substituted biphenyl-3-yl esters as fatty acid amide hydrolase inhibitors: synthesis, quantitative structure - activity relationships, and molecular modeling studies, J. Med. Chem. 47 (2004) 4998-5008.
    • (2004) J. Med. Chem. , vol.47 , pp. 4998-5008
    • Mor, M.1    Rivara, S.2    Lodola, A.3    Plazzi, P.V.4    Tarzia, G.5    Duranti, A.6    Tontini, A.7    Piersanti, G.8    Kathuria, S.9    Piomelli, D.10
  • 155
    • 0035859446 scopus 로고    scopus 로고
    • Internal enzyme motions as a source of catalytic activity: Rate-promoting vibrations and hydrogen tunneling
    • D. Antoniou, S.D. Schwartz, Internal enzyme motions as a source of catalytic activity: Rate-promoting vibrations and hydrogen tunneling, J. Phys. Chem. B 105 (2001) 5553-5558.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 5553-5558
    • Antoniou, D.1    Schwartz, S.D.2
  • 156
    • 0035794224 scopus 로고    scopus 로고
    • Importance of barrier shape in enzyme-catalyzed reactions - Vibrationally assisted hydrogen tunneling in tryptophan tryptophylquinone-dependent amine dehydrogenases
    • J. Basran, S. Patel, M.J. Sutcliffe, N.S. Scrutton, Importance of barrier shape in enzyme-catalyzed reactions - Vibrationally assisted hydrogen tunneling in tryptophan tryptophylquinone-dependent amine dehydrogenases, J. Biol. Chem. 276 (2001) 6234-6242.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6234-6242
    • Basran, J.1    Patel, S.2    Sutcliffe, M.J.3    Scrutton, N.S.4
  • 157
    • 0242582914 scopus 로고    scopus 로고
    • H-tunneling in the multiple H-transfers of the catalytic cycle of morphinone reductase and in the reductive half-reaction of the homologous pentaerythritol tetranitrate reductase
    • J. Basran, R.J. Harris, M.J. Sutcliffe, N.S. Scrutton, H-tunneling in the multiple H-transfers of the catalytic cycle of morphinone reductase and in the reductive half-reaction of the homologous pentaerythritol tetranitrate reductase, J. Biol. Chem. 278 (2003) 43973-43982.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43973-43982
    • Basran, J.1    Harris, R.J.2    Sutcliffe, M.J.3    Scrutton, N.S.4
  • 160
    • 0037188007 scopus 로고    scopus 로고
    • Nuclear quantum effects and enzyme dynamics in dihydrofolate reductase catalysis
    • P.K. Agarwal, S.R. Billeter, S. Hammes-Schiffer, Nuclear quantum effects and enzyme dynamics in dihydrofolate reductase catalysis, J. Phys. Chem. B 106 (2002) 3283-3293.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 3283-3293
    • Agarwal, P.K.1    Billeter, S.R.2    Hammes-Schiffer, S.3
  • 161
    • 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 (2003) 366-371.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 366-371
    • Mincer, J.S.1    Schwartz, S.D.2
  • 162
    • 2342448523 scopus 로고    scopus 로고
    • Rate-promoting vibrations and coupled hydrogen-electron transfer reactions in the condensed phase: A model for enzymic catalysis
    • J.S. Mincer, S.D. Schwartz, Rate-promoting vibrations and coupled hydrogen-electron transfer reactions in the condensed phase: A model for enzymic catalysis, J. Chem. Phys. 120 (2004) 7755-7760.
    • (2004) J. Chem. Phys. , vol.120 , pp. 7755-7760
    • Mincer, J.S.1    Schwartz, S.D.2
  • 163
    • 34047264783 scopus 로고    scopus 로고
    • Proton tunneling in aromatic amine dehydrogenase is driven by a short-range sub-picosecond promoting vibration: Consistency of simulation and theory with experiment
    • L.O. Johannissen, S. Hay, N.S. Scrutton, M.J. Sutcliffe, Proton tunneling in aromatic amine dehydrogenase is driven by a short-range sub-picosecond promoting vibration: Consistency of simulation and theory with experiment, J. Phys. Chem. B 111 (2007) 2631-2638.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 2631-2638
    • Johannissen, L.O.1    Hay, S.2    Scrutton, N.S.3    Sutcliffe, M.J.4
  • 164
    • 58749097088 scopus 로고    scopus 로고
    • The enzyme aromatic amine dehydrogenase induces a substrate conformation crucial for promoting vibration that significantly reduces the effective potential energy barrier to proton transfer
    • L.O. Johannissen, N.S. Scrutton, M.J. Sutcliffe, The enzyme aromatic amine dehydrogenase induces a substrate conformation crucial for promoting vibration that significantly reduces the effective potential energy barrier to proton transfer, J. R. Soc. Interface 5 (2008) 225-232.
    • (2008) J. R. Soc. Interface , vol.5 , pp. 225-232
    • Johannissen, L.O.1    Scrutton, N.S.2    Sutcliffe, M.J.3
  • 167
    • 0043236031 scopus 로고    scopus 로고
    • The first experimental test of the hypothesis that enzymes have evolved to enhance hydrogen tunneling
    • DOI 10.1021/ja030120h
    • K.M. Doll, B.R. Bender, R.G. Finke, The first experimental test of the hypothesis that enzymes have evolved to enhance hydrogen tunneling, J. Am. Chem. Soc. 125 (2003) 10877-10884. (Pubitemid 37087545)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.36 , pp. 10877-10884
    • Doll, K.M.1    Bender, B.R.2    Finke, R.G.3
  • 168
    • 0040193886 scopus 로고
    • Simulations of quantum-mechanical corrections for rate constants of hydride-transfer reactions in enzymes and solutions
    • J.K. Hwang, Z.T. Chu, A. Yadav, A. Warshel, Simulations of quantum-mechanical corrections for rate constants of hydride-transfer reactions in enzymes and solutions, J. Phys. Chem. 95 (1991) 8445-8448.
    • (1991) J. Phys. Chem. , vol.95 , pp. 8445-8448
    • Hwang, J.K.1    Chu, Z.T.2    Yadav, A.3    Warshel, A.4
  • 169
    • 0029951263 scopus 로고    scopus 로고
    • How important are quantum mechanical nuclear motions in enzyme catalysis?
    • J.K. Hwang, A. Warshel, How important are quantum mechanical nuclear motions in enzyme catalysis? J. Am. Chem. Soc. 118 (1996) 11745-11751.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11745-11751
    • Hwang, J.K.1    Warshel, A.2
  • 170
    • 1542317813 scopus 로고    scopus 로고
    • Simulations of the Large Kinetic Isotope Effect and the Temperature Dependence of the Hydrogen Atom Transfer in Lipoxygenase
    • DOI 10.1021/ja037233l
    • M.H. Olsson, P.E. Siegbahn, A. Warshel, Simulations of the large kinetic isotope effect and the temperature dependence of the hydrogen atom transfer in lipoxygenase, J. Am. Chem. Soc. 126 (2004) 2820-2828. (Pubitemid 38314288)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.9 , pp. 2820-2828
    • Olsson, M.H.M.1    Siegbahn, P.E.M.2    Warshel, A.3
  • 171
    • 77955140052 scopus 로고    scopus 로고
    • Quantum catalysis? A comment on tunnelling contributions for catalysed and uncatalysed reactions
    • I.H. Williams, Quantum catalysis? A comment on tunnelling contributions for catalysed and uncatalysed reactions, J. Phys. Org. Chem. 23 (2010) 685-689.
    • (2010) J. Phys. Org. Chem. , vol.23 , pp. 685-689
    • Williams, I.H.1
  • 172
    • 0000115857 scopus 로고    scopus 로고
    • Quantum mechanical tunneling in methylamine dehydrogenase
    • DOI 10.1016/S0009-2614(01)00921-6, PII S0009261401009216
    • C. Alhambra, M.L. Sanchez, J. Corchado, J. Gao, D.G. Truhlar, Quantum mechanical tunneling in methylamine dehydrogenase, Chem. Phys. Lett. 347 (2001) 512-518. (Pubitemid 33628552)
    • (2001) Chemical Physics Letters , vol.347 , Issue.4-6 , pp. 512-518
    • Alhambra, C.1    Luz, S.M.2    Corchado, J.3    Gao, J.4    Truhlar, D.G.5
  • 174
    • 0035892157 scopus 로고    scopus 로고
    • Canonical variational theory for enzyme kinetics with the protein mean force and multidimensional quantum mechanical tunneling dynamics. Theory and application to liver alcohol dehydrogenase
    • DOI 10.1021/jp0120312
    • C. Alhambra, J. Corchado, M.L. Sanchez, M. Garcia-Viloca, J. Gao, D.G. Truhlar, Canonical variational theory for enzyme kinetics with the protein mean force and multidimensional quantum mechanical tunneling dynamics. Theory and application to liver alcohol dehydrogenase, J. Phys. Chem. B 105 (2001) 11326-11340. (Pubitemid 35338485)
    • (2001) Journal of Physical Chemistry B , vol.105 , Issue.45 , pp. 11326-11340
    • Alhambra, C.1    Corchado, J.2    Sanchez, M.L.3    Garcia-Viloca, M.4    Gao, J.5    Truhlar, D.G.6
  • 175
    • 0037035975 scopus 로고    scopus 로고
    • Calculations of hydrogen tunnelling and enzyme catalysis: A comparison of liver alcohol dehydrogenase, methylamine dehydrogenase and soybean lipoxygenase
    • G. Tresadern, J.P.Mcnamara,M.Mohr, H.Wang,N.A. Burton, I.H. Hillier, Calculations of hydrogen tunnelling and enzyme catalysis: a comparison of liver alcohol dehydrogenase, methylamine dehydrogenase and soybean lipoxygenase, Chem. Phys. Lett. 358 (2002) 489-494.
    • (2002) Chem. Phys. Lett. , vol.358 , pp. 489-494
    • Tresadern, G.1    Mcnamara, J.P.2    Mohr, M.3    Wang, H.4    Burton, N.A.5    Hillier, I.H.6
  • 176
    • 0037472678 scopus 로고    scopus 로고
    • Hydride transfer catalyzed by xylose isomerase: Mechanism and quantum effects
    • M. Garcia-Viloca, C. Alhambra, D.G. Truhlar, J.L. Gao, Hydride transfer catalyzed by xylose isomerase: Mechanism and quantum effects, J. Comput. Chem. 24 (2003) 177-190.
    • (2003) J. Comput. Chem. , vol.24 , pp. 177-190
    • Garcia-Viloca, M.1    Alhambra, C.2    Truhlar, D.G.3    Gao, J.L.4
  • 178
    • 0344391945 scopus 로고    scopus 로고
    • Reaction-Path Energetics and Kinetics of the Hydride Transfer Reaction Catalyzed by Dihydrofolate Reductase
    • DOI 10.1021/bi034824f
    • M. Garcia-Viloca, D.G. Truhlar, J. Gao, Reaction-path energetics and kinetics of the hydride transfer reaction catalyzed by dihydrofolate reductase, Biochemistry 42 (2003) 13558-13575. (Pubitemid 37444907)
    • (2003) Biochemistry , vol.42 , Issue.46 , pp. 13558-13575
    • Garcia-Viloca, M.1    Truhlar, D.G.2    Gao, J.3
  • 179
    • 19944416878 scopus 로고    scopus 로고
    • Small temperature dependence of the kinetic isotope effect for the hydride transfer reaction catalyzed by Escherichia coli dihydrofolate reductase
    • J.Z. Pu, S.H. Ma, J.L. Gao, D.G. Truhlar, Small temperature dependence of the kinetic isotope effect for the hydride transfer reaction catalyzed by Escherichia coli dihydrofolate reductase, J. Phys. Chem. B 109 (2005) 8551-8556.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 8551-8556
    • Pu, J.Z.1    Ma, S.H.2    Gao, J.L.3    Truhlar, D.G.4
  • 180
    • 34047242540 scopus 로고    scopus 로고
    • Tunneling and classical paths for proton transfer in an enzyme reaction dominated by tunneling: Oxidation of tryptamine by aromatic amine dehydrogenase
    • L. Masgrau, K.E. Ranaghan, N.S. Scrutton, A.J. Mulholland, M.J. Sutcliffe, Tunneling and classical paths for proton transfer in an enzyme reaction dominated by tunneling: oxidation of tryptamine by aromatic amine dehydrogenase, J. Phys. Chem. B 111 (2007) 3032-3047.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 3032-3047
    • Masgrau, L.1    Ranaghan, K.E.2    Scrutton, N.S.3    Mulholland, A.J.4    Sutcliffe, M.J.5
  • 181
    • 1842839777 scopus 로고    scopus 로고
    • Quantum-classical simulation methods for hydrogen transfer in enzymes: A case study of dihydrofolate reductase
    • DOI 10.1016/j.sbi.2004.03.008, PII S0959440X04000429
    • S. Hammes-Schiffer, Quantum-classical simulation methods for hydrogen transfer in enzymes: a case study of dihydrofolate reductase, Curr. Opin. Struct. Biol. 14 (2004) 192-201. (Pubitemid 38490786)
    • (2004) Current Opinion in Structural Biology , vol.14 , Issue.2 , pp. 192-201
    • Hammes-Schiffer, S.1
  • 182
    • 33748354485 scopus 로고    scopus 로고
    • The role of enzyme dynamics and tunnelling in catalysing hydride transfer: Studies of distal mutants of dihydrofolate reductase
    • L. Wang, N.M. Goodey, S.J. Benkovic, A. Kohen, The role of enzyme dynamics and tunnelling in catalysing hydride transfer: studies of distal mutants of dihydrofolate reductase, 1307-1315Philos. Trans.R. Soc. London Biol. 361 (2006).
    • (2006) Philos. Trans.R. Soc. London Biol. , vol.361 , pp. 1307-1315
    • Wang, L.1    Goodey, N.M.2    Benkovic, S.J.3    Kohen, A.4
  • 183
    • 1842763785 scopus 로고    scopus 로고
    • Temperature dependence of kinetic isotope effects for enzymatic carbon-hydrogen bond cleavage
    • W. Siebrand, Z. Smedarchina, Temperature dependence of kinetic isotope effects for enzymatic carbon-hydrogen bond cleavage, J. Phys. Chem. B 108 (2004) 4185-4195.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 4185-4195
    • Siebrand, W.1    Smedarchina, Z.2
  • 186
    • 77949829432 scopus 로고    scopus 로고
    • Computer simulations of quantum tunnelling in enzyme-catalysed hydrogen transfer reactions
    • K.E. Ranaghan, A.J. Mulholland, Computer simulations of quantum tunnelling in enzyme-catalysed hydrogen transfer reactions, Interdiscip. Sci. 2 (2010) 78-97.
    • (2010) Interdiscip. Sci. , vol.2 , pp. 78-97
    • Ranaghan, K.E.1    Mulholland, A.J.2
  • 187
    • 0031443372 scopus 로고    scopus 로고
    • Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant
    • DOI 10.1021/bi9716231
    • C.E. Cameron, S.J. Benkovic, Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant, Biochemistry 36 (1997) 15792-15800. (Pubitemid 28027379)
    • (1997) Biochemistry , vol.36 , Issue.50 , pp. 15792-15800
    • Cameron, C.E.1    Benkovic, S.J.2
  • 188
    • 6344294816 scopus 로고    scopus 로고
    • The coupling of structural fluctuations to hydride transfer in dihydrofolate reductase
    • I.F. Thorpe, C.L. Brooks, The coupling of structural fluctuations to hydride transfer in dihydrofolate reductase, Proteins: Struct. Funct. and Bioinf. 57 (2004) 444-457.
    • (2004) Proteins: Struct. Funct. and Bioinf. , vol.57 , pp. 444-457
    • Thorpe, I.F.1    Brooks, C.L.2
  • 189
    • 25144458498 scopus 로고    scopus 로고
    • Conformational substates modulate hydride transfer in dihydrofolate reductase
    • DOI 10.1021/ja053558l
    • I.F. Thorpe, C.L. Brooks, Conformational substates modulate hydride transfer in dihydrofolate reductase, J. Am. Chem. Soc. 127 (2005) 12997-13006. (Pubitemid 41339185)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.37 , pp. 12997-13006
    • Thorpe, I.F.1    Brooks III, C.L.2
  • 190
    • 34249104188 scopus 로고    scopus 로고
    • The catalytic effect of dihydrofolate reductase and its mutants is determined by reorganization energies
    • DOI 10.1021/bi700201w
    • H.B. Liu, A. Warshel, The catalytic effect of dihydrofolate reductase and its mutants is determined by reorganization energies, Biochemistry 46 (2007) 6011-6025. (Pubitemid 46799163)
    • (2007) Biochemistry , vol.46 , Issue.20 , pp. 6011-6025
    • Liu, H.1    Warshel, A.2
  • 191
    • 0037123216 scopus 로고    scopus 로고
    • Temperature-dependent isotope effects in soybean Lipoxygenase-1: Correlating hydrogen tunneling with protein dynamics
    • DOI 10.1021/ja012205t
    • 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 (2002) 3865-3874. (Pubitemid 34310901)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.15 , pp. 3865-3874
    • Knapp, M.J.1    Rickert, K.2    Klinman, J.P.3
  • 192
    • 46949108866 scopus 로고    scopus 로고
    • A chemical understanding for the enhanced hydrogen tunnelling in hydroperoxidation of linoleic acid catalysed by soybean lipoxygenase-1
    • M. Barroso, L.G. Arnaut, S.J. Formosinho, A chemical understanding for the enhanced hydrogen tunnelling in hydroperoxidation of linoleic acid catalysed by soybean lipoxygenase-1, J. Phys. Org. Chem. 21 (2008) 659-665.
    • (2008) J. Phys. Org. Chem. , vol.21 , pp. 659-665
    • Barroso, M.1    Arnaut, L.G.2    Formosinho, S.J.3
  • 194
    • 33846047459 scopus 로고    scopus 로고
    • Proton-coupled electron transfer in soybean lipoxygenase: Dynamical behavior and temperature dependence of kinetic isotope effects
    • DOI 10.1021/ja0667211
    • E. Hatcher, A.V. Soudackov, S. Hammes-Schiffer, Proton-coupled electron transfer in soybean lipoxygenase: Dynamical behavior and temperature dependence of kinetic isotope effects, J. Am. Chem. Soc. 129 (2007) 187-196. (Pubitemid 46068274)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.1 , pp. 187-196
    • Hatcher, E.1    Soudackov, A.V.2    Hammes-Schiffer, S.3
  • 195
    • 48149093014 scopus 로고    scopus 로고
    • Hydrogen tunneling in an enzyme active site: A quantum wavepacket dynamical perspective
    • S.S. Iyengar, I. Sumner, J. Jakowski, Hydrogen tunneling in an enzyme active site: A quantum wavepacket dynamical perspective, J. Phys. Chem. B 112 (2008) 7601-7613.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 7601-7613
    • Iyengar, S.S.1    Sumner, I.2    Jakowski, J.3
  • 196
    • 0029964954 scopus 로고    scopus 로고
    • Experimental evidence for extensive tunneling of hydrogen in the lipoxygenase reaction: Implications for enzyme catalysis
    • DOI 10.1021/ja961827p, PII S0002786396018276
    • T. Jonsson, M.H. Glickman, S.J. Sun, J.P. Klinman, Experimental evidence for extensive tunneling of hydrogen in the lipoxygenase reaction: Implications for enzyme catalysis, J. Am. Chem. Soc. 118 (1996) 10319-10320. (Pubitemid 26375225)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.42 , pp. 10319-10320
    • Jonsson, T.1    Glickman, M.H.2    Sun, S.3    Klinman, J.P.4
  • 197
    • 0037328843 scopus 로고    scopus 로고
    • Density-functional investigation on the mechanism of H-atom abstraction by lipoxygenase
    • N. Lehnert, E.I. Solomon, Density-functional investigation on the mechanism of H-atom abstraction by lipoxygenase, J. Biol. Inorg. Chem. 8 (2003) 294-305. (Pubitemid 36236138)
    • (2003) Journal of Biological Inorganic Chemistry , vol.8 , Issue.3 , pp. 294-305
    • Lehnert, N.1    Solomon, E.I.2
  • 198
    • 44949221121 scopus 로고    scopus 로고
    • Simulation of tunneling in enzyme catalysis by combining a biased propagation approach and the quantum classical pathmethod: Application to lipoxygenase
    • J. Mavri, H.B. Liu, M.H.M. Olsson, A. Warshel, Simulation of tunneling in enzyme catalysis by combining a biased propagation approach and the quantum classical pathmethod: Application to lipoxygenase, J. Phys. Chem. B 112 (2008) 5950-5954.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 5950-5954
    • Mavri, J.1    Liu, H.B.2    Olsson, M.H.M.3    Warshel, A.4
  • 199
    • 58049192859 scopus 로고    scopus 로고
    • Enzyme structure and dynamics affect hydrogen tunneling: The impact of a remote side chain (I553) in soybean lipoxygenase-1 (vol 105, pg 1146, 2008)
    • M.P. Meyer, D.R. Tomchick, J.P. Klinman, Enzyme structure and dynamics affect hydrogen tunneling: The impact of a remote side chain (I553) in soybean lipoxygenase-1 (vol 105, pg 1146, 2008), Proc. Natl. Acad. Sci. USA 105 (2008) 19562.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19562
    • Meyer, M.P.1    Tomchick, D.R.2    Klinman, J.P.3
  • 200
    • 1542317813 scopus 로고    scopus 로고
    • Simulations of the Large Kinetic Isotope Effect and the Temperature Dependence of the Hydrogen Atom Transfer in Lipoxygenase
    • DOI 10.1021/ja037233l
    • M.H.M. Olsson, P.E.M. Siegbahn, A. Warshel, Simulations of the large kinetic isotope effect and the temperature dependence of the hydrogen Atom transfer in lipoxygenase, J. Am. Chem. Soc. 126 (2004) 2820-2828. (Pubitemid 38314288)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.9 , pp. 2820-2828
    • Olsson, M.H.M.1    Siegbahn, P.E.M.2    Warshel, A.3
  • 201
    • 0036971585 scopus 로고    scopus 로고
    • Direct dynamics calculations of reaction rate and kinetic isotope effects in enzyme catalysed reactions
    • G. Tresadern, S. Nunez, P.F. Faulder, H. Wang, I.H. Hillier, N.A. Burton, Direct dynamics calculations of reaction rate and kinetic isotope effects in enzyme catalysed reactions, Faraday Discuss. 122 (2003) 223-242.
    • (2003) Faraday Discuss. , vol.122 , pp. 223-242
    • Tresadern, G.1    Nunez, S.2    Faulder, P.F.3    Wang, H.4    Hillier, I.H.5    Burton, N.A.6
  • 202
    • 1542377623 scopus 로고    scopus 로고
    • Extreme tunnelling in methylamine dehydrogenase revealed by hybrid QM/MM calculations: Potential energy surface profile for methylamine and ethanolamine substrates and kinetic isotope effect values
    • G. Tresadern, H. Wang, P.F. Faulder, N.A. Burton, I.H. Hillier, Extreme tunnelling in methylamine dehydrogenase revealed by hybrid QM/MM calculations: potential energy surface profile for methylamine and ethanolamine substrates and kinetic isotope effect values, Mol. Phys. 101 (2003) 2775-2784.
    • (2003) Mol. Phys. , vol.101 , pp. 2775-2784
    • Tresadern, G.1    Wang, H.2    Faulder, P.F.3    Burton, N.A.4    Hillier, I.H.5
  • 204
    • 69949116013 scopus 로고    scopus 로고
    • Evaluation of the kinetic isotope effect in methylamine dehydrogenase using the wave function propagation approach
    • G. Pierdominici-Sottile, J. Palma, Evaluation of the kinetic isotope effect in methylamine dehydrogenase using the wave function propagation approach, Chem. Phys. 363 (2009) 59-64.
    • (2009) Chem. Phys. , vol.363 , pp. 59-64
    • Pierdominici-Sottile, G.1    Palma, J.2
  • 205
    • 0035928796 scopus 로고    scopus 로고
    • Backbone dynamics in dihydrofolate reductase complexes: Role of loop flexibility in the catalytic mechanism
    • DOI 10.1021/bi010621k
    • M.J. Osborne, J. Schnell, S.J. Benkovic, H.J. Dyson, P.E. Wright, Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism, Biochemistry 40 (2001) 9846-9859. (Pubitemid 32769533)
    • (2001) Biochemistry , vol.40 , Issue.33 , pp. 9846-9859
    • Osborne, M.J.1    Schnell, J.2    Benkovic, S.J.3    Dyson, H.J.4    Wright, P.E.5
  • 206
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • DOI 10.1021/bi962337c
    • M.R. Sawaya, J. Kraut, Loop and subdomain movements in the mechanism of escherichia coli dihydrofolate reductase: crystallographic evidence, Biochemistry 36 (1997) 586-603. (Pubitemid 27057006)
    • (1997) Biochemistry , vol.36 , Issue.3 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 208
    • 0242267579 scopus 로고    scopus 로고
    • Evidence for Environmentally Coupled Hydrogen Tunneling during Dihydrofolate Reductase Catalysis
    • DOI 10.1021/ja035692g
    • G. Maglia, R.K. Allemann, Evidence for environmentally coupled hydrogen tunneling during dihydrofolate reductase catalysis, J. Am. Chem. Soc. 125 (2003) 13372-13373. (Pubitemid 37352119)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.44 , pp. 13372-13373
    • Maglia, G.1    Allemann, R.K.2
  • 209
    • 33646254850 scopus 로고    scopus 로고
    • Dynamics of immobilized and native Escherichia coli dihydrofolate reductase by quasielastic neutron scattering
    • M. Tehei, J.C. Smith, C. Monk, J. Ollivier, M. Oettl, V. Kurkal, J.L. Finney, R.M. Daniel, Dynamics of immobilized and native Escherichia coli dihydrofolate reductase by quasielastic neutron scattering, Biophys. J. 90 (2006) 1090-1097.
    • (2006) Biophys. J. , vol.90 , pp. 1090-1097
    • Tehei, M.1    Smith, J.C.2    Monk, C.3    Ollivier, J.4    Oettl, M.5    Kurkal, V.6    Finney, J.L.7    Daniel, R.M.8
  • 210
    • 0037459224 scopus 로고    scopus 로고
    • Importance of substrate and cofactor polarization in the active site of dihydrofolate reductase
    • M. Garcia-Viloca, D.G. Truhlar, J.L. Gao, Importance of substrate and cofactor polarization in the active site of dihydrofolate reductase, J. Mol. Biol. 327 (2003) 549-560.
    • (2003) J. Mol. Biol. , vol.327 , pp. 549-560
    • Garcia-Viloca, M.1    Truhlar, D.G.2    Gao, J.L.3
  • 211
    • 0023668190 scopus 로고
    • Construction and evaluation of the kinetic scheme associated with dihydrofolate-reductase from escherichia-Coli
    • C.A. Fierke, K.A. Johnson, S.J. Benkovic, Construction and evaluation of the kinetic scheme associated with dihydrofolate-reductase from escherichia-Coli, Biochemistry 26 (1987) 4085-4092.
    • (1987) Biochemistry , vol.26 , pp. 4085-4092
    • Fierke, C.A.1    Johnson, K.A.2    Benkovic, S.J.3
  • 212
    • 0023748631 scopus 로고
    • Mechanism of the reaction catalyzed by dihydrofolate-reductase from escherichia-coli - PH and deuterium-isotope effects with NADPH as the variable substrate
    • J.F. Morrison, S.R. Stone, Mechanism of the reaction catalyzed by dihydrofolate-reductase from escherichia-coli - pH and deuterium-isotope effects with NADPH as the variable substrate, Biochemistry 27 (1988) 5499-5506.
    • (1988) Biochemistry , vol.27 , pp. 5499-5506
    • Morrison, J.F.1    Stone, S.R.2
  • 213
    • 0028049327 scopus 로고
    • Dynamics of a flexible loop in dihydrofolate reductase from Escherichia coli and its implication for catalysis
    • C.J. Falzone, P.E. Wright, S.J. Benkovic, Dynamics of a flexible loop in dihydrofolate reductase from Escherichia coli and its implication for catalysis, Biochemistry 33 (1994) 439-442. (Pubitemid 24048085)
    • (1994) Biochemistry , vol.33 , Issue.2 , pp. 439-442
    • Falzone, C.J.1    Wright, P.E.2    Benkovic, S.J.3
  • 214
    • 0033955055 scopus 로고    scopus 로고
    • Protein dynamics in enzymatic catalysis: Exploration of dihydrofolate reductase
    • DOI 10.1021/ja9913838
    • J.L. Radkiewicz, C.L. Brooks, Protein dynamics in enzymatic catalysis: Exploration of dihydrofolate reductase, J. Am. Chem. Soc. 122 (2000) 225-231. (Pubitemid 30061051)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.2 , pp. 225-231
    • Radkiewicz, J.L.1    Brooks III, C.L.2
  • 215
    • 0028037407 scopus 로고
    • Nonadditivity of mutational effects at the folate binding site of Escherichia coli dihydrofolate reductase
    • DOI 10.1021/bi00204a020
    • Z. Huang, C.R. Wagner, S.J. Benkovic, Nonadditivity of mutational effects at the folate binding-sote of Esherichia-coli dihydrofolate reductase, Biochemistry 33 (1994) 11576-11585. (Pubitemid 24330091)
    • (1994) Biochemistry , vol.33 , Issue.38 , pp. 11576-11585
    • Huang, Z.1    Wagner, C.R.2    Benkovic, S.J.3
  • 216
    • 0028828696 scopus 로고
    • Molecular-basis for nonadditive mutational effects in Escherichia-coli dihydrofolate reductase
    • C.R. Wagner, Z. Huang, S.F. Singleton, S.J. Benkovic, Molecular-basis for nonadditive mutational effects in Escherichia-coli dihydrofolate reductase, Biochemistry 34 (1995) 15671-15680.
    • (1995) Biochemistry , vol.34 , pp. 15671-15680
    • Wagner, C.R.1    Huang, Z.2    Singleton, S.F.3    Benkovic, S.J.4
  • 217
    • 0034737320 scopus 로고    scopus 로고
    • The crystal structure of dihydrofolate reductase from Thermotoga maritima: Molecular features of thermostability
    • T. Dams, G. Auerbach, G. Bader, U. Jacob, T. Ploom, R. Huber, R. Jaenicke, The crystal structure of dihydrofolate reductase from Thermotoga maritima: Molecular features of thermostability, J. Mol. Biol. 297 (2000) 659-672.
    • (2000) J. Mol. Biol. , vol.297 , pp. 659-672
    • Dams, T.1    Auerbach, G.2    Bader, G.3    Jacob, U.4    Ploom, T.5    Huber, R.6    Jaenicke, R.7
  • 219
    • 0027483247 scopus 로고
    • Deuterium kinetic isotope effect and stopped-flow kinetic studies of the quinoprotein methylamine dehydrogenase
    • H.B. Brooks, L.H. Jones, V.L. Davidson, Deuterium kinetic isotope effect and stopped-flow kinetic-studies of the quinoprotein methylamine dehydrogenase, Biochemistry 32 (1993) 2725-2729. (Pubitemid 23090663)
    • (1993) Biochemistry , vol.32 , Issue.10 , pp. 2725-2729
    • Brooks, H.B.1    Jones, L.H.2    Davidson, V.L.3
  • 222
    • 77953289373 scopus 로고    scopus 로고
    • Optimal control design of laser pulses for mode specific vibrational excitation in an enzyme-substrate complex
    • Q. Ren, K.E. Ranaghan, A.J. Mulholland, J.N. Harvey, F.R. Manby, G.G. Balint-Kurti, Optimal control design of laser pulses for mode specific vibrational excitation in an enzyme-substrate complex, Chem. Phys. Lett. 491 (2010) 230-236.
    • (2010) Chem. Phys. Lett. , vol.491 , pp. 230-236
    • Ren, Q.1    Ranaghan, K.E.2    Mulholland, A.J.3    Harvey, J.N.4    Manby, F.R.5    Balint-Kurti, G.G.6
  • 223
    • 36749104477 scopus 로고
    • Solution of the Schrödinger-equation by a spectral method. 2. Vibrational-energy levels of triatomic-molecules
    • M.D. Feit, J.A. Fleck, Solution of the Schrödinger-equation by a spectral method. 2. Vibrational-energy levels of triatomic-molecules, J. Chem. Phys. 78 (1983) 301-308.
    • (1983) J. Chem. Phys. , vol.78 , pp. 301-308
    • Feit, M.D.1    Fleck, J.A.2
  • 224
    • 22944434892 scopus 로고    scopus 로고
    • Quantum control of molecular motion including electronic polarization effects with a two-stage toolkit
    • G.G. Balint-Kurti, F.R. Manby, Q.H. Ren, M. Artamonov, T.S. Ho, H. Rabitz, Quantum control of molecular motion including electronic polarization effects with a two-stage toolkit, J. Chem. Phys. 122 (2005).
    • (2005) J. Chem. Phys. , vol.122
    • Balint-Kurti, G.G.1    Manby, F.R.2    Ren, Q.H.3    Artamonov, M.4    Ho, T.S.5    Rabitz, H.6
  • 225
    • 34547649017 scopus 로고    scopus 로고
    • Quantum control of molecular vibrational and rotational excitations in a homonuclear diatomic molecule: A full three-dimensional treatment with polarization forces
    • Q.H. Ren, G.G. Balint-Kurti, F.R. Manby, M. Artamonov, T.S. Ho, H. Rabitz, Quantum control of molecular vibrational and rotational excitations in a homonuclear diatomic molecule: A full three-dimensional treatment with polarization forces, J. Chem. Phys. 124 (2006).
    • (2006) J. Chem. Phys. , vol.124
    • Ren, Q.H.1    Balint-Kurti, G.G.2    Manby, F.R.3    Artamonov, M.4    Ho, T.S.5    Rabitz, H.6
  • 226
    • 39649096055 scopus 로고    scopus 로고
    • Chiral cyclohexane based fluorescent chemosensors for enantiomeric discrimination of aspartate
    • A.M. Costero, M. Colera, P. Gavina, S. Gil, M. Kubinyi, K. Pal, M. Kallay, Chiral cyclohexane based fluorescent chemosensors for enantiomeric discrimination of aspartate, Tetrahedron 64 (2008) 3217-3224.
    • (2008) Tetrahedron , vol.64 , pp. 3217-3224
    • Costero, A.M.1    Colera, M.2    Gavina, P.3    Gil, S.4    Kubinyi, M.5    Pal, K.6    Kallay, M.7
  • 227
    • 78650159036 scopus 로고    scopus 로고
    • Comment on "Astationary-wave model of enzyme catalysis" by Carlo Canepa
    • R. Lonsdale, J.N.Harvey, F.R.Manby, A.J.Mulholland, Comment on "Astationary-wave model of enzyme catalysis" by Carlo Canepa, J. Comput. Chem. 32 (2011) 368-369.
    • (2011) J. Comput. Chem. , vol.32 , pp. 368-369
    • Lonsdale, R.1    Harvey, J.N.2    Manby, F.R.3    Mulholland, A.J.4
  • 228
    • 77955127388 scopus 로고    scopus 로고
    • An analysis of all the relevant facts and arguments indicates that enzyme catalysis does not involve large contributions from nuclear tunneling
    • S.C.L. Kamerlin, A. Warshel, An analysis of all the relevant facts and arguments indicates that enzyme catalysis does not involve large contributions from nuclear tunneling, J. Phys. Org. Chem. 23 (2010) 677-684.
    • (2010) J. Phys. Org. Chem. , vol.23 , pp. 677-684
    • Kamerlin, S.C.L.1    Warshel, A.2
  • 229
    • 77951226274 scopus 로고    scopus 로고
    • At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis?
    • S.C.L. Kamerlin, A. Warshel, At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis? Proteins: Struct. Funct. Bioinf. 78 (2010) 1339-1375.
    • (2010) Proteins: Struct. Funct. Bioinf. , vol.78 , pp. 1339-1375
    • Kamerlin, S.C.L.1    Warshel, A.2
  • 230
    • 38049031723 scopus 로고    scopus 로고
    • The effect of temperature on enzyme activity: New insights and their implications
    • R.M. Daniel, M.J. Danson, R. Eisenthal, C.K. Lee, M.E. Peterson, The effect of temperature on enzyme activity: new insights and their implications, Extremophiles 12 (2008) 51-59.
    • (2008) Extremophiles , vol.12 , pp. 51-59
    • Daniel, R.M.1    Danson, M.J.2    Eisenthal, R.3    Lee, C.K.4    Peterson, M.E.5
  • 232
    • 0031662567 scopus 로고    scopus 로고
    • Structure, function and stability of enzymes from the Archaea
    • M.J. Danson, D.W. Hough, Structure, function and stability of enzymes from the Archaea, Trends Microbiol. 6 (1998) 307-314.
    • (1998) Trends Microbiol. , vol.6 , pp. 307-314
    • Danson, M.J.1    Hough, D.W.2


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