메뉴 건너뛰기




Volumn 47, Issue 42, 2008, Pages 11118-11124

Kinetic isotope effects on aromatic and benzylic hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase as probes of chemical mechanism and reactivity

Author keywords

[No Author keywords available]

Indexed keywords

AMINATION; AMINES; AROMATIC COMPOUNDS; AROMATIZATION; CARRIER MOBILITY; CHEMICAL REACTIONS; CHEMICAL REACTIVITY; DEUTERIUM; ENZYMES; HYDROCARBONS; HYDROGEN; HYDROXYLATION; ISOTOPES; ORGANIC ACIDS; OXYGEN; PORPHYRINS; REACTION KINETICS;

EID: 54349093029     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801295w     Document Type: Article
Times cited : (15)

References (48)
  • 1
    • 0033660818 scopus 로고    scopus 로고
    • The aromatic amino acid hydroxylases
    • Purich, D. L, Ed, pp, John Wiley & Sons, Inc, New York
    • Fitzpatrick, P. F. (2000) The aromatic amino acid hydroxylases. In Advances in Enzymology and Related Areas of Molecular Biology (Purich, D. L., Ed.) pp 235-294, John Wiley & Sons, Inc., New York.
    • (2000) Advances in Enzymology and Related Areas of Molecular Biology , pp. 235-294
    • Fitzpatrick, P.F.1
  • 2
    • 0025800443 scopus 로고
    • Phenylketonuria and the phenylalanine hydroxylase gene
    • Eisensmith, R. C., and Woo, S. L. C. (1991) Phenylketonuria and the phenylalanine hydroxylase gene. Mol. Biol. Med. 8, 3-18.
    • (1991) Mol. Biol. Med , vol.8 , pp. 3-18
    • Eisensmith, R.C.1    Woo, S.L.C.2
  • 3
    • 0026015244 scopus 로고
    • Cloning and expression of Chromobacterium violaceum phenylalanine hydroxylase in Escherichia coli and comparison of amino acid sequence with mammalian aromatic amino acid hydroxylases
    • Onishi, A., Liotta, L. J., and Benkovic, S. J. (1991) Cloning and expression of Chromobacterium violaceum phenylalanine hydroxylase in Escherichia coli and comparison of amino acid sequence with mammalian aromatic amino acid hydroxylases. J. Biol. Chem. 266, 18454-18459.
    • (1991) J. Biol. Chem , vol.266 , pp. 18454-18459
    • Onishi, A.1    Liotta, L.J.2    Benkovic, S.J.3
  • 4
    • 0032475980 scopus 로고    scopus 로고
    • Phenylalanine hydroxylase from Chromobacterium violaceum. Uncoupled oxidation of tetrahydropterin and the role of iron in hydroxylation
    • Chen, D., and Frey, P. (1998) Phenylalanine hydroxylase from Chromobacterium violaceum. Uncoupled oxidation of tetrahydropterin and the role of iron in hydroxylation. J. Biol. Chem. 273, 25594-25601.
    • (1998) J. Biol. Chem , vol.273 , pp. 25594-25601
    • Chen, D.1    Frey, P.2
  • 5
    • 0345492036 scopus 로고    scopus 로고
    • Mechanism of aromatic amino acid hydroxylation
    • Fitzpatrick, P. F. (2003) Mechanism of aromatic amino acid hydroxylation. Biochemistry 42, 14083-14091.
    • (2003) Biochemistry , vol.42 , pp. 14083-14091
    • Fitzpatrick, P.F.1
  • 6
    • 0024413420 scopus 로고
    • Evidence for the formation of the 4a-carbinolamine during the tyrosine-dependent oxidation of tetrahydrobiopterin by rat liver phenylalanine hydroxylase
    • Davis, M. D., and Kaufman, S. (1989) Evidence for the formation of the 4a-carbinolamine during the tyrosine-dependent oxidation of tetrahydrobiopterin by rat liver phenylalanine hydroxylase. J. Biol. Chem. 264, 8585-8596.
    • (1989) J. Biol. Chem , vol.264 , pp. 8585-8596
    • Davis, M.D.1    Kaufman, S.2
  • 8
    • 0034636184 scopus 로고    scopus 로고
    • Mutation of serine 395 of tyrosine hydroxylase decouples oxygen-oxygen bond cleavage and tyrosine hydroxylation
    • Ellis, H. R., Daubner, S. C., and Fitzpatrick, P. F. (2000) Mutation of serine 395 of tyrosine hydroxylase decouples oxygen-oxygen bond cleavage and tyrosine hydroxylation. Biochemistry 39, 4174-4181.
    • (2000) Biochemistry , vol.39 , pp. 4174-4181
    • Ellis, H.R.1    Daubner, S.C.2    Fitzpatrick, P.F.3
  • 10
    • 3643061399 scopus 로고    scopus 로고
    • A mechanism for hydroxylation by tyrosine hydroxylase based on partitioning of substituted phenylalanines
    • Hillas, P. J., and Fitzpatrick, P. F. (1996) A mechanism for hydroxylation by tyrosine hydroxylase based on partitioning of substituted phenylalanines. Biochemistry 35, 6969-6975.
    • (1996) Biochemistry , vol.35 , pp. 6969-6975
    • Hillas, P.J.1    Fitzpatrick, P.F.2
  • 11
    • 0036310665 scopus 로고    scopus 로고
    • Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: Similar fold, different stability and reaction rates
    • Erlandsen, H., Kim, J. Y., Patch, M. G., Han, A., Volner, A., Abu-Omar, M. M., and Stevens, R. C. (2002) Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: Similar fold, different stability and reaction rates. J. Mol. Biol. 320, 645-661.
    • (2002) J. Mol. Biol , vol.320 , pp. 645-661
    • Erlandsen, H.1    Kim, J.Y.2    Patch, M.G.3    Han, A.4    Volner, A.5    Abu-Omar, M.M.6    Stevens, R.C.7
  • 12
    • 0031010420 scopus 로고    scopus 로고
    • Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited diseases
    • Goodwill, K. E., Sabatier, C., Marks, C., Raag, R., Fitzpatrick, P. F., and Stevens, R. C. (1997) Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited diseases. Nat. Struct. Biol. 4, 578-585.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 578-585
    • Goodwill, K.E.1    Sabatier, C.2    Marks, C.3    Raag, R.4    Fitzpatrick, P.F.5    Stevens, R.C.6
  • 13
    • 0031303781 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria
    • Erlandsen, H., Fusetti, F., Martinez, A., Hough, E., Flatmark, T., and Stevens, R. C. (1997) Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria. Nat. Struct. Biol. 4, 995-1000.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 995-1000
    • Erlandsen, H.1    Fusetti, F.2    Martinez, A.3    Hough, E.4    Flatmark, T.5    Stevens, R.C.6
  • 14
    • 0037465514 scopus 로고    scopus 로고
    • Characterization of metal ligand mutants of tyrosine hydroxylase: Insights into the plasticity of a 2-histidine-1-carboxylate triad
    • Fitzpatrick, P. F., Ralph, E. C., Ellis, H. R., Willmon, O. J., and Daubner, S. C. (2003) Characterization of metal ligand mutants of tyrosine hydroxylase: Insights into the plasticity of a 2-histidine-1-carboxylate triad. Biochemistry 42, 2081-2088.
    • (2003) Biochemistry , vol.42 , pp. 2081-2088
    • Fitzpatrick, P.F.1    Ralph, E.C.2    Ellis, H.R.3    Willmon, O.J.4    Daubner, S.C.5
  • 15
    • 44949192686 scopus 로고    scopus 로고
    • Characterization of metal ligand mutants of phenylalanine hydroxylase: Insights into the plasticity of a 2-histidine-1-carboxylate triad
    • Li, J., and Fitzpatrick, P. F. (2008) Characterization of metal ligand mutants of phenylalanine hydroxylase: Insights into the plasticity of a 2-histidine-1-carboxylate triad. Arch. Biochem. Biophys. 475, 164-168.
    • (2008) Arch. Biochem. Biophys , vol.475 , pp. 164-168
    • Li, J.1    Fitzpatrick, P.F.2
  • 16
    • 0036915347 scopus 로고    scopus 로고
    • Use of a tyrosine hydroxylase mutant enzyme with reduced metal affinity allows detection of activity with cobalt in place of iron
    • Ellis, H. R., McCusker, K. P., and Fitzpatrick, P. (2002) Use of a tyrosine hydroxylase mutant enzyme with reduced metal affinity allows detection of activity with cobalt in place of iron. Arch. Biochem. Biophys. 408, 305-307.
    • (2002) Arch. Biochem. Biophys , vol.408 , pp. 305-307
    • Ellis, H.R.1    McCusker, K.P.2    Fitzpatrick, P.3
  • 17
    • 0020048381 scopus 로고
    • Phenylalanine hydroxylase. Correlation of the iron content with activity and the preparation and reconstitution of the apoenzyme
    • Gottschall, D. W., Dietrich, R. F., and Benkovic, S. J. (1982) Phenylalanine hydroxylase. Correlation of the iron content with activity and the preparation and reconstitution of the apoenzyme. J. Biol. Chem. 257, 845-849.
    • (1982) J. Biol. Chem , vol.257 , pp. 845-849
    • Gottschall, D.W.1    Dietrich, R.F.2    Benkovic, S.J.3
  • 18
    • 0024324003 scopus 로고
    • The metal requirement of rat tyrosine hydroxylase
    • Fitzpatrick, P. F. (1989) The metal requirement of rat tyrosine hydroxylase. Biochem. Biophys. Res. Commun. 161, 211-215.
    • (1989) Biochem. Biophys. Res. Commun , vol.161 , pp. 211-215
    • Fitzpatrick, P.F.1
  • 19
    • 0032524864 scopus 로고    scopus 로고
    • Expression and characterization of the catalytic core of tryptophan hydroxylase
    • Moran, G. R., Daubner, S. C., and Fitzpatrick, P. F. (1998) Expression and characterization of the catalytic core of tryptophan hydroxylase. J. Biol. Chem. 273, 12259-12266.
    • (1998) J. Biol. Chem , vol.273 , pp. 12259-12266
    • Moran, G.R.1    Daubner, S.C.2    Fitzpatrick, P.F.3
  • 20
    • 0023038339 scopus 로고
    • Phenylalanine hydroxylase from Chromobacterium violaceum is a copper-containing monooxygenase. Kinetics of the reductive activation of the enzyme
    • Pember, S. O., Villafranca, J. J., and Benkovic, S. J. (1986) Phenylalanine hydroxylase from Chromobacterium violaceum is a copper-containing monooxygenase. Kinetics of the reductive activation of the enzyme. Biochemistry 25, 6611-6619.
    • (1986) Biochemistry , vol.25 , pp. 6611-6619
    • Pember, S.O.1    Villafranca, J.J.2    Benkovic, S.J.3
  • 21
    • 0029047711 scopus 로고
    • Mechanism of metal-independent hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase
    • Carr, R. T., Balasubramanian, S., Hawkins, P. C. D., and Benkovic, S. J. (1995) Mechanism of metal-independent hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase. Biochemistry 34, 7525-7532.
    • (1995) Biochemistry , vol.34 , pp. 7525-7532
    • Carr, R.T.1    Balasubramanian, S.2    Hawkins, P.C.D.3    Benkovic, S.J.4
  • 22
    • 0025804515 scopus 로고
    • Hydroxylation of 4-methylphenylalanine by rat liver phenylalanine hydroxylase
    • Siegmund, H.-U., and Kaufman, S. (1991) Hydroxylation of 4-methylphenylalanine by rat liver phenylalanine hydroxylase. J. Biol. Chem. 266, 2903-2910.
    • (1991) J. Biol. Chem , vol.266 , pp. 2903-2910
    • Siegmund, H.-U.1    Kaufman, S.2
  • 23
    • 28444448357 scopus 로고    scopus 로고
    • Intrinsic isotope effects on benzylic hydroxylation by the aromatic amino acid hydroxylases: Evidence for hydrogen tunneling, coupled motion, and similar reactivities
    • Pavon, J. A., and Fitzpatrick, P. F. (2005) Intrinsic isotope effects on benzylic hydroxylation by the aromatic amino acid hydroxylases: Evidence for hydrogen tunneling, coupled motion, and similar reactivities. J. Am. Chem. Soc. 127, 16414-16415.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 16414-16415
    • Pavon, J.A.1    Fitzpatrick, P.F.2
  • 24
    • 0028039678 scopus 로고
    • Kinetic isotope effects on hydroxylation of ring-deuterated phenylalanines by tyrosine hydroxylase provide evidence against partitioning of an arene oxide intermediate
    • Fitzpatrick, P. F. (1994) Kinetic isotope effects on hydroxylation of ring-deuterated phenylalanines by tyrosine hydroxylase provide evidence against partitioning of an arene oxide intermediate. J. Am. Chem. Soc. 116, 1133-1134.
    • (1994) J. Am. Chem. Soc , vol.116 , pp. 1133-1134
    • Fitzpatrick, P.F.1
  • 25
    • 0037165727 scopus 로고    scopus 로고
    • Intrinsic deuterium isotope effects on benzylic hydroxylation by tyrosine hydroxylase
    • Frantom, P. A., Pongdee, R., Sulikowski, G. A., and Fitzpatrick, P. F. (2002) Intrinsic deuterium isotope effects on benzylic hydroxylation by tyrosine hydroxylase. J. Am. Chem. Soc. 124, 4202-4203.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 4202-4203
    • Frantom, P.A.1    Pongdee, R.2    Sulikowski, G.A.3    Fitzpatrick, P.F.4
  • 26
    • 0030568905 scopus 로고    scopus 로고
    • Characterization of the active site iron in tyrosine hydroxylase: Redox states of the iron
    • Ramsey, A. J., Hillas, P. J., and Fitzpatrick, P. F. (1996) Characterization of the active site iron in tyrosine hydroxylase: Redox states of the iron. J. Biol. Chem. 271, 24395-24400.
    • (1996) J. Biol. Chem , vol.271 , pp. 24395-24400
    • Ramsey, A.J.1    Hillas, P.J.2    Fitzpatrick, P.F.3
  • 27
    • 0025336708 scopus 로고
    • Mechanism of phenylalanine regulation of phenylalanine hydroxylase
    • Shiman, R., Jones, S. H., and Gray, D. W. (1990) Mechanism of phenylalanine regulation of phenylalanine hydroxylase. J. Biol. Chem. 265, 11633-11642.
    • (1990) J. Biol. Chem , vol.265 , pp. 11633-11642
    • Shiman, R.1    Jones, S.H.2    Gray, D.W.3
  • 28
    • 0030848479 scopus 로고    scopus 로고
    • Characterization of chimeric pterin dependent hydroxylases: Contributions of the regulatory domains of tyrosine and phenylalanine hydroxylase to substrate specificity
    • Daubner, S. C., Hillas, P. J., and Fitzpatrick, P. F. (1997) Characterization of chimeric pterin dependent hydroxylases: Contributions of the regulatory domains of tyrosine and phenylalanine hydroxylase to substrate specificity. Biochemistry 36, 11574-11582.
    • (1997) Biochemistry , vol.36 , pp. 11574-11582
    • Daubner, S.C.1    Hillas, P.J.2    Fitzpatrick, P.F.3
  • 29
    • 33748496877 scopus 로고    scopus 로고
    • Insights into the catalytic mechanisms of phenylalanine and tryptophan hydroxylase from kinetic isotope effects on aromatic hydroxylation
    • Pavon, J. A., and Fitzpatrick, P. F. (2006) Insights into the catalytic mechanisms of phenylalanine and tryptophan hydroxylase from kinetic isotope effects on aromatic hydroxylation. Biochemistry 45, 11030-11037.
    • (2006) Biochemistry , vol.45 , pp. 11030-11037
    • Pavon, J.A.1    Fitzpatrick, P.F.2
  • 30
    • 0023239093 scopus 로고
    • Phenylalanine 4-monooxygenase from Chromobacterium violaceum
    • Fujisawa, H., and Nakata, H. (1987) Phenylalanine 4-monooxygenase from Chromobacterium violaceum. Methods Enzymol. 142, 44-49.
    • (1987) Methods Enzymol , vol.142 , pp. 44-49
    • Fujisawa, H.1    Nakata, H.2
  • 31
    • 0037262644 scopus 로고    scopus 로고
    • Order of substrate binding in bacterial phenylalanine hydroxylase and its mechanistic implication for pterin-dependent oxygenases
    • Volner, A., Zoidakis, J., and Abu-Omar, M. M. (2003) Order of substrate binding in bacterial phenylalanine hydroxylase and its mechanistic implication for pterin-dependent oxygenases. J. Biol. Inorg. Chem. 8, 121-128.
    • (2003) J. Biol. Inorg. Chem , vol.8 , pp. 121-128
    • Volner, A.1    Zoidakis, J.2    Abu-Omar, M.M.3
  • 32
    • 0021682831 scopus 로고
    • The activation of rat liver phenylalanine hydroxylase by limited proteolysis, lysolecithin, and tocopherol phosphate. Changes in conformation and catalytic properties
    • Abita, J.-P., Parniak, M., and Kaufman, S. (1984) The activation of rat liver phenylalanine hydroxylase by limited proteolysis, lysolecithin, and tocopherol phosphate. Changes in conformation and catalytic properties. J. Biol. Chem. 259, 14560-14566.
    • (1984) J. Biol. Chem , vol.259 , pp. 14560-14566
    • Abita, J.-P.1    Parniak, M.2    Kaufman, S.3
  • 34
    • 0346434118 scopus 로고    scopus 로고
    • Uncoupled forms of tyrosine hydroxylase unmask kinetic isotope effects on chemical steps
    • Frantom, P. A., and Fitzpatrick, P. F. (2003) Uncoupled forms of tyrosine hydroxylase unmask kinetic isotope effects on chemical steps. J. Am. Chem. Soc. 125, 16190-16191.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 16190-16191
    • Frantom, P.A.1    Fitzpatrick, P.F.2
  • 35
    • 33748505959 scopus 로고    scopus 로고
    • Isotope effects from partitioning of intermediates in enzyme-catalyzed hydroxylation reactions
    • Kohen, A, and Limbach, H, Eds, pp, Marcel Dekker, Inc, New York
    • Fitzpatrick, P. F. (2005) Isotope effects from partitioning of intermediates in enzyme-catalyzed hydroxylation reactions. In Isotope Effects in Chemistry and Biology (Kohen, A., and Limbach, H., Eds.) pp 861-873, Marcel Dekker, Inc., New York.
    • (2005) Isotope Effects in Chemistry and Biology , pp. 861-873
    • Fitzpatrick, P.F.1
  • 36
    • 0033168713 scopus 로고    scopus 로고
    • Hydrogen tunneling in biology
    • Kohen, A., and Klinman, J. P. (1999) Hydrogen tunneling in biology. Chem. Biol. 6, 191-198.
    • (1999) Chem. Biol , vol.6 , pp. 191-198
    • Kohen, A.1    Klinman, J.P.2
  • 37
    • 0023651141 scopus 로고
    • Organization and evolution of the rat tyrosine hydroxylase gene
    • Brown, E. R., Coker, G. T., III., and O'Malley, K. L. (1987) Organization and evolution of the rat tyrosine hydroxylase gene. Biochemistry 26, 5208-5212.
    • (1987) Biochemistry , vol.26 , pp. 5208-5212
    • Brown, E.R.1    Coker III, G.T.2    O'Malley, K.L.3
  • 38
    • 0023393590 scopus 로고
    • Full-length cDNA for rabbit tryptophan hydroxylase: Functional domains and evolution of aromatic amino acid hydroxylases
    • Grenett, H. E., Ledley, F. D., Reed, L. L., and Woo, S. L. C. (1987) Full-length cDNA for rabbit tryptophan hydroxylase: Functional domains and evolution of aromatic amino acid hydroxylases. Proc. Natl. Acad. Sci. U.S.A. 84, 5530-5534.
    • (1987) Proc. Natl. Acad. Sci. U.S.A , vol.84 , pp. 5530-5534
    • Grenett, H.E.1    Ledley, F.D.2    Reed, L.L.3    Woo, S.L.C.4
  • 39
    • 0037159254 scopus 로고    scopus 로고
    • Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin
    • Wang, L., Erlandsen, H., Haavik, J., Knappskog, P. M., and Stevens, R. C. (2002) Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin. Biochemistry 41, 12569-12574.
    • (2002) Biochemistry , vol.41 , pp. 12569-12574
    • Wang, L.1    Erlandsen, H.2    Haavik, J.3    Knappskog, P.M.4    Stevens, R.C.5
  • 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
    • 0037125529 scopus 로고    scopus 로고
    • Hydrogen tunneling in peptidylglycine α-hydroxylating monooxygenase
    • Francisco, W. A., Knapp, M. J., Blackburn, N. J., and Klinman, J. P. (2002) Hydrogen tunneling in peptidylglycine α-hydroxylating monooxygenase. J. Am. Chem. Soc. 124, 8194-8195.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 8194-8195
    • Francisco, W.A.1    Knapp, M.J.2    Blackburn, N.J.3    Klinman, J.P.4
  • 44
    • 0036305396 scopus 로고    scopus 로고
    • Hydrogen tunneling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes
    • Sutcliffe, M. J., and Scrutton, N. S. (2002) Hydrogen tunneling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes. Eur. J. Biochem. 269, 3096-3102.
    • (2002) Eur. J. Biochem , vol.269 , pp. 3096-3102
    • Sutcliffe, M.J.1    Scrutton, N.S.2
  • 45
    • 33748367252 scopus 로고    scopus 로고
    • Arrhenius curves of hydrogen transfers: Tunnel effects, isotope effects and effects of pre-equilibria
    • Limbach, H.-H., Lopez, J. M., and Kohen, A. (2006) Arrhenius curves of hydrogen transfers: Tunnel effects, isotope effects and effects of pre-equilibria. Philos. Trans. R. Soc. London, Ser. B 361, 1399-1415.
    • (2006) Philos. Trans. R. Soc. London, Ser. B , vol.361 , pp. 1399-1415
    • Limbach, H.-H.1    Lopez, J.M.2    Kohen, A.3
  • 46
    • 33748344518 scopus 로고    scopus 로고
    • Linking protein structure and dynamics to catalysis: The role of hydrogen tunnelling
    • Klinman, J. P. (2006) Linking protein structure and dynamics to catalysis: The role of hydrogen tunnelling. Philos. Trans. R. Soc. London, Ser. B 361, 1323-1331.
    • (2006) Philos. Trans. R. Soc. London, Ser. B , vol.361 , pp. 1323-1331
    • Klinman, J.P.1
  • 47
    • 34547456661 scopus 로고    scopus 로고
    • Origin of the temperature dependence of isotope effects in enzymatic reactions: The case of dihydrofolate reductase
    • Liu, H., and Warshel, A. (2007) Origin of the temperature dependence of isotope effects in enzymatic reactions: The case of dihydrofolate reductase. J. Phys. Chem. B 111, 7852-7861.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 7852-7861
    • Liu, H.1    Warshel, A.2
  • 48
    • 39449086415 scopus 로고    scopus 로고
    • Atomistic insight into the origin of the temperature-dependence of kinetic isotope effects and H-tunnelling in enzyme systems is revealed through combined experimental studies and biomolecular simulation
    • Hay, S., Pudney, C., Hothi, P., Johannissen, L. O., Masgrau, L., Pang, J., Leys, D., Sutcliffe, M. J., and Scrutton, N. S. (2008) Atomistic insight into the origin of the temperature-dependence of kinetic isotope effects and H-tunnelling in enzyme systems is revealed through combined experimental studies and biomolecular simulation. Biochem. Soc. Trans. 36, 16-21.
    • (2008) Biochem. Soc. Trans , vol.36 , pp. 16-21
    • Hay, S.1    Pudney, C.2    Hothi, P.3    Johannissen, L.O.4    Masgrau, L.5    Pang, J.6    Leys, D.7    Sutcliffe, M.J.8    Scrutton, N.S.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.