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Volumn 52, Issue 12, 2013, Pages 2068-2077

Importance of protein dynamics during enzymatic C-H bond cleavage catalysis

Author keywords

[No Author keywords available]

Indexed keywords

C-H BOND CLEAVAGE; CH-BOND ACTIVATION; ENZYME FUNCTIONS; LINK PROTEIN; LIPOXYGENASE-1; PROTEIN DYNAMICS; QUANTUM TUNNELING;

EID: 84875677477     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301504m     Document Type: Article
Times cited : (54)

References (65)
  • 1
    • 84912208190 scopus 로고
    • Chemical achievements and hope for the future
    • Pauling, L. (1948) Chemical achievements and hope for the future Am. Sci. 36, 51-58
    • (1948) Am. Sci. , vol.36 , pp. 51-58
    • Pauling, L.1
  • 2
    • 0033791659 scopus 로고    scopus 로고
    • Critical analysis of antibody catalysis
    • Hilvert, D. (2000) Critical analysis of antibody catalysis Annu. Rev. Biochem. 69, 751-793
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 751-793
    • Hilvert, D.1
  • 6
    • 70350131719 scopus 로고    scopus 로고
    • Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins
    • Schrank, T. P., Bolen, D. W., and Hilser, V. J. (2009) Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins Proc. Natl. Acad. Sci. U.S.A. 106, 16984-16989
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 16984-16989
    • Schrank, T.P.1    Bolen, D.W.2    Hilser, V.J.3
  • 7
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins
    • Hilser, V. J. and Thompson, E. B. (2007) Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins Proc. Natl. Acad. Sci. U.S.A. 104, 8311-8315
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 8311-8315
    • Hilser, V.J.1    Thompson, E.B.2
  • 8
    • 44349104122 scopus 로고    scopus 로고
    • Hydrogen-exchange mass spectrometry reveals activation-induced changes in the conformational mobility of p38α MAP kinase
    • Sours, K. M., Kwok, S. C., Rachidi, T., Lee, T., Ring, A., Hoofnagle, A. N., Resing, K. A., and Ahn, N. G. (2008) Hydrogen-exchange mass spectrometry reveals activation-induced changes in the conformational mobility of p38α MAP kinase J. Mol. Biol. 379, 1075-1093
    • (2008) J. Mol. Biol. , vol.379 , pp. 1075-1093
    • Sours, K.M.1    Kwok, S.C.2    Rachidi, T.3    Lee, T.4    Ring, A.5    Hoofnagle, A.N.6    Resing, K.A.7    Ahn, N.G.8
  • 9
    • 76249122268 scopus 로고    scopus 로고
    • Biochemistry. An ensemble view of allostery
    • Hilser, V. J. (2010) Biochemistry. An ensemble view of allostery Science 327, 653-654
    • (2010) Science , vol.327 , pp. 653-654
    • Hilser, V.J.1
  • 11
    • 71449103005 scopus 로고    scopus 로고
    • Hidden alternative structures of proline isomerase essential for catalysis
    • Fraser, J. S., Clarkson, M. W., Degnan, S. C., Erion, R., Kern, D., and Alber, T. (2009) Hidden alternative structures of proline isomerase essential for catalysis Nature 462, 669-673
    • (2009) Nature , vol.462 , pp. 669-673
    • Fraser, J.S.1    Clarkson, M.W.2    Degnan, S.C.3    Erion, R.4    Kern, D.5    Alber, T.6
  • 12
    • 68049085675 scopus 로고    scopus 로고
    • A 21st century revisionist's view at a turning point in enzymology
    • Nagel, Z. D. and Klinman, J. P. (2009) A 21st century revisionist's view at a turning point in enzymology Nat. Chem. Biol. 5, 543-550
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 543-550
    • Nagel, Z.D.1    Klinman, J.P.2
  • 13
    • 84875665271 scopus 로고    scopus 로고
    • Hydrogen tunneling links protein dynamics to enzyme catalysis
    • press in press
    • Klinman, J. P. and Kohen, A. Hydrogen tunneling links protein dynamics to enzyme catalysis. Annu. Rev. Biochem. 2013, in press in press.
    • (2013) Annu. Rev. Biochem.
    • Klinman, J.P.1    Kohen, A.2
  • 14
    • 0032484096 scopus 로고    scopus 로고
    • Single-molecule enzymatic dynamics
    • Liu, H. P., Xun, L., and Xie, X. S. (1998) Single-molecule enzymatic dynamics Science 282, 1877-1882
    • (1998) Science , vol.282 , pp. 1877-1882
    • Liu, H.P.1    Xun, L.2    Xie, X.S.3
  • 15
    • 78751674331 scopus 로고    scopus 로고
    • Seeing the forest for the trees: Fluorescence studies of single enzymes in the context of ensemble experiments
    • Tan, Y. W. and Yang, H. (2011) Seeing the forest for the trees: Fluorescence studies of single enzymes in the context of ensemble experiments Phys. Chem. Chem. Phys. 13, 1709-1721
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 1709-1721
    • Tan, Y.W.1    Yang, H.2
  • 17
    • 62249181529 scopus 로고    scopus 로고
    • An integrated model for enzyme catalysis emerges from studies of hydrogen tunneling
    • Klinman, J. P. (2009) An integrated model for enzyme catalysis emerges from studies of hydrogen tunneling Chem. Phys. Lett. 471, 179-193
    • (2009) Chem. Phys. Lett. , vol.471 , pp. 179-193
    • Klinman, J.P.1
  • 18
    • 0022004980 scopus 로고
    • Electron transfer in chemistry and biology
    • Marcus, R. A. and Sutin, N. (1985) Electron transfer in chemistry and biology Biochim. Biophys. Acta 811, 265-322
    • (1985) Biochim. Biophys. Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 19
    • 0024573393 scopus 로고
    • Hydrogen tunneling in enzyme reactions
    • Cha, Y., Murray, C. J., and Klinman, J. P. (1989) Hydrogen tunneling in enzyme reactions Science 243, 1325-1330
    • (1989) Science , vol.243 , pp. 1325-1330
    • Cha, Y.1    Murray, C.J.2    Klinman, J.P.3
  • 20
    • 0010884753 scopus 로고
    • On the theory of oxidation-reduction reactions involving electron transfer
    • Marcus, R. A. (1956) On the theory of oxidation-reduction reactions involving electron transfer J. Chem. Phys. 24, 966-978
    • (1956) J. Chem. Phys. , vol.24 , pp. 966-978
    • Marcus, R.A.1
  • 21
    • 0033305793 scopus 로고    scopus 로고
    • Proton and hydrogen atom tunnelling in hydrolytic and redox enzyme catalysis
    • Kuznetsov, A. M. and Ulstrup, J. (1999) Proton and hydrogen atom tunnelling in hydrolytic and redox enzyme catalysis Can. J. Chem. 77, 1085-1096
    • (1999) Can. J. Chem. , vol.77 , pp. 1085-1096
    • Kuznetsov, A.M.1    Ulstrup, J.2
  • 22
    • 0036301901 scopus 로고    scopus 로고
    • Environmentally coupled hydrogen tunneling: Linking catalysis to dynamics
    • Knapp, M. J. and Klinman, J. P. (2002) Environmentally coupled hydrogen tunneling: Linking catalysis to dynamics Eur. J. Biochem. 269, 3113-3121
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3113-3121
    • Knapp, M.J.1    Klinman, J.P.2
  • 23
    • 0028153517 scopus 로고
    • Extremely large isotope effects in the soybean lipoxygenase-linoleic acid reaction
    • Glickman, M. H., Wiseman, J. S., and Klinman, J. P. (1994) Extremely large isotope effects in the soybean lipoxygenase-linoleic acid reaction J. Am. Chem. Soc. 116, 793-794
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 793-794
    • Glickman, M.H.1    Wiseman, J.S.2    Klinman, J.P.3
  • 25
    • 0033576983 scopus 로고    scopus 로고
    • Large competitive kinetic isotope effects in human 15-lipoxygenase catalysis measured by a novel HPLC method
    • Lewis, E. R., Johansen, E., and Holman, T. R. (1999) Large competitive kinetic isotope effects in human 15-lipoxygenase catalysis measured by a novel HPLC method J. Am. Chem. Soc. 121, 1395-1396
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 1395-1396
    • Lewis, E.R.1    Johansen, E.2    Holman, T.R.3
  • 26
    • 50249166700 scopus 로고    scopus 로고
    • Evidence for protein radical-mediated nuclear tunneling in fatty acid α-oxygenase
    • Gupta, A., Mukherjee, A., Matsui, K., and Roth, J. P. (2008) Evidence for protein radical-mediated nuclear tunneling in fatty acid α-oxygenase J. Am. Chem. Soc. 130, 11274-11275
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11274-11275
    • Gupta, A.1    Mukherjee, A.2    Matsui, K.3    Roth, J.P.4
  • 27
    • 80053465271 scopus 로고    scopus 로고
    • Hydrogen tunneling steps in cyclooxygenase-2 catalysis
    • Danish, H. H., Doncheva, I. S., and Roth, J. P. (2011) Hydrogen tunneling steps in cyclooxygenase-2 catalysis J. Am. Chem. Soc. 133, 15846-15849
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 15846-15849
    • Danish, H.H.1    Doncheva, I.S.2    Roth, J.P.3
  • 28
    • 0032557580 scopus 로고    scopus 로고
    • Manganese lipoxygenase: Discovery of a bis-allylic hydroperoxide as product and intermediate in a lipoxygenase reaction
    • Hamberg, M., Su, C., and Oliw, E. (1998) Manganese lipoxygenase: Discovery of a bis-allylic hydroperoxide as product and intermediate in a lipoxygenase reaction J. Biol. Chem. 273, 13080-13088
    • (1998) J. Biol. Chem. , vol.273 , pp. 13080-13088
    • Hamberg, M.1    Su, C.2    Oliw, E.3
  • 29
    • 84866530943 scopus 로고    scopus 로고
    • Novel insights into cyclooxygenases, linoleate diol synthases, and lipoxygenases from deuterium kinetic isotope effects and oxidation of substrate analogs
    • Hoffmann, I., Hamberg, M., Lindh, R., and Oliw, E. H. (2012) Novel insights into cyclooxygenases, linoleate diol synthases, and lipoxygenases from deuterium kinetic isotope effects and oxidation of substrate analogs Biochim. Biophys. Acta 1821, 1508-1517
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 1508-1517
    • Hoffmann, I.1    Hamberg, M.2    Lindh, R.3    Oliw, E.H.4
  • 30
    • 0033592315 scopus 로고    scopus 로고
    • Nature of hydrogen transfer in soybean lipoxygenase 1: Separation of primary and secondary isotope effects
    • Rickert, K. W. and Klinman, J. P. (1999) Nature of hydrogen transfer in soybean lipoxygenase 1: Separation of primary and secondary isotope effects Biochemistry 38, 12218-12228
    • (1999) Biochemistry , vol.38 , pp. 12218-12228
    • Rickert, K.W.1    Klinman, J.P.2
  • 31
    • 0029843150 scopus 로고    scopus 로고
    • Lipoxygenase reaction mechanism: Demonstration that hydrogen abstraction from substrate precedes dioxygen binding during catalytic turnover
    • Glickman, M. H. and Klinman, J. P. (1996) Lipoxygenase reaction mechanism: Demonstration that hydrogen abstraction from substrate precedes dioxygen binding during catalytic turnover Biochemistry 35, 12882-12892
    • (1996) Biochemistry , vol.35 , pp. 12882-12892
    • Glickman, M.H.1    Klinman, J.P.2
  • 33
    • 0028864344 scopus 로고
    • Nature of rate-limiting steps in the soybean lipoxygenase-1 reaction
    • Glickman, M. and Klinman, J. P. (1995) Nature of rate-limiting steps in the soybean lipoxygenase-1 reaction Biochemistry 34, 14077-14092
    • (1995) Biochemistry , vol.34 , pp. 14077-14092
    • Glickman, M.1    Klinman, J.P.2
  • 34
    • 0029964954 scopus 로고    scopus 로고
    • Experimental evidence for extensive tunneling of hydrogen in the lipoxygenase reaction: Implications for enzyme catalysis
    • Jonsson, T., Glickman, M. H., Sun, S., and Klinman, J. P. (1996) Experimental evidence for extensive tunneling of hydrogen in the lipoxygenase reaction: Implications for enzyme catalysis J. Am. Chem. Soc. 118, 10319-10320
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10319-10320
    • Jonsson, T.1    Glickman, M.H.2    Sun, S.3    Klinman, J.P.4
  • 35
    • 0019330801 scopus 로고
    • Kinetic and chemical mechanisms of yeast formate dehydrogenase
    • Blanchard, J. S. and Cleland, W. W. (1980) Kinetic and chemical mechanisms of yeast formate dehydrogenase Biochemistry 19, 3543-3550
    • (1980) Biochemistry , vol.19 , pp. 3543-3550
    • Blanchard, J.S.1    Cleland, W.W.2
  • 36
    • 0033519723 scopus 로고    scopus 로고
    • Enzyme dynamics and hydrogen tunneling in a thermophilic alcohol dehydrogenase
    • Kohen, A., Cannio, R., Bartolucci, S., and Klinman, J. P. (1999) Enzyme dynamics and hydrogen tunneling in a thermophilic alcohol dehydrogenase Nature 399, 496-499
    • (1999) Nature , vol.399 , pp. 496-499
    • Kohen, A.1    Cannio, R.2    Bartolucci, S.3    Klinman, J.P.4
  • 37
    • 77955127137 scopus 로고    scopus 로고
    • A new model for the origin of kinetic hydrogen isotope effects
    • Klinman, J. P. (2010) A new model for the origin of kinetic hydrogen isotope effects J. Phys. Org. Chem. 23, 606-612
    • (2010) J. Phys. Org. Chem. , vol.23 , pp. 606-612
    • Klinman, J.P.1
  • 38
    • 79851479815 scopus 로고    scopus 로고
    • Investigating inner-sphere reorganization via secondary kinetic isotope effects in the C-H cleavage reaction catalyzed by soybean lipoxygenase: Tunneling in the substrate backbone as well as the transferred hydrogen
    • Meyer, M. P. and Klinman, J. P. (2011) Investigating inner-sphere reorganization via secondary kinetic isotope effects in the C-H cleavage reaction catalyzed by soybean lipoxygenase: Tunneling in the substrate backbone as well as the transferred hydrogen J. Am. Chem. Soc. 133, 430-439
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 430-439
    • Meyer, M.P.1    Klinman, J.P.2
  • 39
    • 33748613208 scopus 로고    scopus 로고
    • Multidimensional tunneling, recrossing, and the transmission coefficient for enzymatic reactions
    • Pu, J., Gao, J., and Truhlar, D. (2006) Multidimensional tunneling, recrossing, and the transmission coefficient for enzymatic reactions Chem. Rev. 106, 3140-3169
    • (2006) Chem. Rev. , vol.106 , pp. 3140-3169
    • Pu, J.1    Gao, J.2    Truhlar, D.3
  • 40
    • 48149093014 scopus 로고    scopus 로고
    • Hydrogen tunneling in an enzyme active site: A quantum wavepacket dynamical perspective
    • Iyengar, S. S., Sumner, I., and Jakowski, J. (2008) Hydrogen tunneling in an enzyme active site: A quantum wavepacket dynamical perspective J. Phys. Chem. B 112, 7601-7613
    • (2008) J. Phys. Chem. B , vol.112 , pp. 7601-7613
    • Iyengar, S.S.1    Sumner, I.2    Jakowski, J.3
  • 41
    • 84868243079 scopus 로고    scopus 로고
    • Quantum variational transition state theory for hydrogen tunneling in enzyme catalysis
    • Pollak, E. (2012) Quantum variational transition state theory for hydrogen tunneling in enzyme catalysis J. Phys. Chem. B 116, 12966-12971
    • (2012) J. Phys. Chem. B , vol.116 , pp. 12966-12971
    • Pollak, E.1
  • 42
    • 0037123216 scopus 로고    scopus 로고
    • Temperature-dependent isotope effects in soybean lipoxygenase-1: Correlating hydrogen tunneling with protein dynamics
    • Knapp, M. J., Rickert, K., and Klinman, J. P. (2002) Temperature- dependent isotope effects in soybean lipoxygenase-1: Correlating hydrogen tunneling with protein dynamics J. Am. Chem. Soc. 124, 3865-3874
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3865-3874
    • Knapp, M.J.1    Rickert, K.2    Klinman, J.P.3
  • 43
    • 84867514524 scopus 로고    scopus 로고
    • Hydrogen donor-acceptor fluctuations from kinetic isotope effects: A phenomenological model
    • Roston, D., Cheatum, C. M., and Kohen, A. (2012) Hydrogen donor-acceptor fluctuations from kinetic isotope effects: A phenomenological model Biochemistry 51, 6860-6870
    • (2012) Biochemistry , vol.51 , pp. 6860-6870
    • Roston, D.1    Cheatum, C.M.2    Kohen, A.3
  • 44
    • 39549094013 scopus 로고    scopus 로고
    • Enzyme structure and dynamics affect hydrogen tunneling: The impact of a remote side chain (I553) in soybean lipoxygenase-1
    • 19562 (Correction)
    • Meyer, M. P., Tomchick, D. R., and Klinman, J. P. (2008) Enzyme structure and dynamics affect hydrogen tunneling: The impact of a remote side chain (I553) in soybean lipoxygenase-1 Proc. Natl. Acad. Sci. U.S.A. 105, 1146-1151, 19562 (Correction)
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 1146-1151
    • Meyer, M.P.1    Tomchick, D.R.2    Klinman, J.P.3
  • 45
    • 84865800398 scopus 로고    scopus 로고
    • Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis
    • Xu, S., Mueser, T. C., Marnett, L. J., and Funk, M. O. J. (2012) Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis Structure 20, 1490-1497
    • (2012) Structure , vol.20 , pp. 1490-1497
    • Xu, S.1    Mueser, T.C.2    Marnett, L.J.3    Funk, M.O.J.4
  • 47
    • 84856247363 scopus 로고    scopus 로고
    • Effects of the donor-acceptor distance and dynamics on hydride tunneling in the dihydrofolate reductase catalyzed reaction
    • Stojkovic, V., Perissinotti, L. L., Willmer, D., Benkovic, S. J., and Kohen, A. (2012) Effects of the donor-acceptor distance and dynamics on hydride tunneling in the dihydrofolate reductase catalyzed reaction J. Am. Chem. Soc. 134, 1738-1745
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 1738-1745
    • Stojkovic, V.1    Perissinotti, L.L.2    Willmer, D.3    Benkovic, S.J.4    Kohen, A.5
  • 48
    • 84861379052 scopus 로고    scopus 로고
    • Active site hydrophobic residues impact hydrogen tunneling differently in thermophilic alcohol dehydrogenase at optimal versus nonoptimal temperatures
    • Nagel, Z. D., Meadows, C. W., Dong, M., Bahnson, B. J., and Klinman, J. P. (2012) Active site hydrophobic residues impact hydrogen tunneling differently in thermophilic alcohol dehydrogenase at optimal versus nonoptimal temperatures Biochemistry 51, 4147-4156
    • (2012) Biochemistry , vol.51 , pp. 4147-4156
    • Nagel, Z.D.1    Meadows, C.W.2    Dong, M.3    Bahnson, B.J.4    Klinman, J.P.5
  • 49
    • 77952523308 scopus 로고    scopus 로고
    • Impact of distal mutation on hydrogen transfer interface and substrate conformation in soybean lipoxygenase
    • Edwards, S. J., Soudackov, A. V., and Hammes-Schiffer, S. (2010) Impact of distal mutation on hydrogen transfer interface and substrate conformation in soybean lipoxygenase J. Phys. Chem. B 114, 6653-6660
    • (2010) J. Phys. Chem. B , vol.114 , pp. 6653-6660
    • Edwards, S.J.1    Soudackov, A.V.2    Hammes-Schiffer, S.3
  • 50
    • 84857542642 scopus 로고    scopus 로고
    • Taking Ockham's razor to enzyme dynamics and catalysis
    • Glowacki, D. R., Harvey, J. N., and Mulholland, A. J. (2012) Taking Ockham's razor to enzyme dynamics and catalysis Nat. Chem. 4, 169-176
    • (2012) Nat. Chem. , vol.4 , pp. 169-176
    • Glowacki, D.R.1    Harvey, J.N.2    Mulholland, A.J.3
  • 51
    • 3042709505 scopus 로고    scopus 로고
    • Thermal-activated protein mobility and its correlation with catalysis in thermophilic alcohol dehydrogenase
    • Liang, Z.-X., Lee, T., Resing, K. A., Ahn, N. G., and Klinman, J. P. (2004) Thermal-activated protein mobility and its correlation with catalysis in thermophilic alcohol dehydrogenase Proc. Natl. Acad. Sci. U.S.A. 101, 9556-9561
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 9556-9561
    • Liang, Z.-X.1    Lee, T.2    Resing, K.A.3    Ahn, N.G.4    Klinman, J.P.5
  • 52
    • 50849111095 scopus 로고    scopus 로고
    • Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis
    • Boehr, D. D., Dyson, H. J., and Wright, P. E. (2008) Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis Biochemistry 47, 9227-9233
    • (2008) Biochemistry , vol.47 , pp. 9227-9233
    • Boehr, D.D.1    Dyson, H.J.2    Wright, P.E.3
  • 53
    • 84255214322 scopus 로고    scopus 로고
    • Protein dynamics and enzymatic chemical barrier passage
    • Antoniou, D. and Schwartz, S. D. (2011) Protein dynamics and enzymatic chemical barrier passage J. Phys. Chem. B 115, 15147-15158
    • (2011) J. Phys. Chem. B , vol.115 , pp. 15147-15158
    • Antoniou, D.1    Schwartz, S.D.2
  • 54
    • 79960580073 scopus 로고    scopus 로고
    • Impaired protein conformational landscapes as revealed in anomalous Arrhenius prefactors
    • Nagel, Z. D., Dong, M., Bahnson, B. J., and Klinman, J. P. (2011) Impaired protein conformational landscapes as revealed in anomalous Arrhenius prefactors Proc. Natl. Acad. Sci. U.S.A. 108, 10520-10525
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 10520-10525
    • Nagel, Z.D.1    Dong, M.2    Bahnson, B.J.3    Klinman, J.P.4
  • 58
    • 0019349208 scopus 로고
    • The expression of isotope effects on enzyme-catalyzed reactions
    • Northrop, D. B. (1981) The expression of isotope effects on enzyme-catalyzed reactions Annu. Rev. Biochem. 50, 103-131
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 103-131
    • Northrop, D.B.1
  • 59
    • 0000261827 scopus 로고
    • Deuterium isotope effects on outer-sphere electron transfer reactions
    • Buhks, E., Bixon, M., and Jortner, J. (1981) Deuterium isotope effects on outer-sphere electron transfer reactions J. Phys. Chem. 85, 3763-3766
    • (1981) J. Phys. Chem. , vol.85 , pp. 3763-3766
    • Buhks, E.1    Bixon, M.2    Jortner, J.3
  • 62
    • 0015101706 scopus 로고
    • Entropic contributions to rate accelerations in enzymic and intramolecular reactions and chelate effect
    • Page, M. I. and Jencks, W. P. (1971) Entropic contributions to rate accelerations in enzymic and intramolecular reactions and chelate effect Proc. Natl. Acad. Sci. U.S.A. 68, 1678-1683
    • (1971) Proc. Natl. Acad. Sci. U.S.A. , vol.68 , pp. 1678-1683
    • Page, M.I.1    Jencks, W.P.2
  • 63
    • 0142091405 scopus 로고    scopus 로고
    • The near attack conformation approach to the study of the chorismate to prephenate reaction
    • Hur, S. and Bruice, T. C. (2003) The near attack conformation approach to the study of the chorismate to prephenate reaction Proc. Natl. Acad. Sci. U.S.A. 100, 12015-12020
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 12015-12020
    • Hur, S.1    Bruice, T.C.2
  • 65
    • 77955127137 scopus 로고    scopus 로고
    • A new model for the origin of kinetic hydrogen isotope effects
    • Klinman, J. P. (2010) A new model for the origin of kinetic hydrogen isotope effects J. Phys. Org. Chem. 23, 606-612
    • (2010) J. Phys. Org. Chem. , vol.23 , pp. 606-612
    • Klinman, J.P.1


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