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Volumn 105, Issue 4, 2008, Pages 1146-1151

Enzyme structure and dynamics affect hydrogen tunneling: The impact of a remote side chain (I553) in soybean lipoxygenase-1

Author keywords

Hydrogenic wave function overlap; Protein dynamics

Indexed keywords

HYDROGEN; LIPOOXYGENASE 1; LIPOXYGENASE; UNCLASSIFIED DRUG; IRON; ISOLEUCINE; PROTEIN SUBUNIT; VEGETABLE PROTEIN;

EID: 39549094013     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0710643105     Document Type: Article
Times cited : (140)

References (33)
  • 1
    • 0028864344 scopus 로고
    • Nature of rate-limiting steps in the soybean lipoxygenase-1 reaction
    • Glickman MH, Klinman JP (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.H.1    Klinman, J.P.2
  • 2
    • 0029843150 scopus 로고    scopus 로고
    • Lipoxygenase reaction mechanism: Demonstration that hydrogen abstraction from substrate precedes dioxygen binding during catalytic turnover
    • Glickman MH, Klinman JP (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
  • 3
    • 0028153517 scopus 로고
    • Extremely large isotope effects in the soybean lipoxygenase-linoleic acid reaction
    • Glickman MH, Wiseman JS, Klinman JP (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
  • 4
    • 0027962756 scopus 로고
    • Unusually large deuterium isotope effects in soybean lipoxygenase are not caused by a magnetic isotope effect
    • Hwang CC, Grissom CB (1994) Unusually large deuterium isotope effects in soybean lipoxygenase are not caused by a magnetic isotope effect. J Am Chem Soc 116:795-796.
    • (1994) J Am Chem Soc , vol.116 , pp. 795-796
    • Hwang, C.C.1    Grissom, C.B.2
  • 5
    • 0029964954 scopus 로고    scopus 로고
    • Experimental evidence for extensive tunneling of hydrogen in the lipoxygenase reaction implications for enzyme catalysis
    • Jonsson T, Glickman MH, Sun S, Klinman JP (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
  • 6
    • 0033592315 scopus 로고    scopus 로고
    • The nature of hydrogen transfer in soybean lipoxygenase-1: Separation of primary and secondary isotope effects
    • Rickert K, Klinman JP (1999) The 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.1    Klinman, J.P.2
  • 7
    • 0034811728 scopus 로고    scopus 로고
    • Steric control of oxygenation regiochemistry in soybean lipoxygenase-1
    • Knapp MJ, Seebeck FP, Klinman JP (2001) Steric control of oxygenation regiochemistry in soybean lipoxygenase-1. J Am Chem Soc 123:2931-2932.
    • (2001) J Am Chem Soc , vol.123 , pp. 2931-2932
    • Knapp, M.J.1    Seebeck, F.P.2    Klinman, J.P.3
  • 8
    • 0036301901 scopus 로고    scopus 로고
    • Environmentally coupled hydrogen tunneling: Linking catalysis to dynamics
    • Knapp MJ, Klinman JP (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
  • 9
    • 2442548491 scopus 로고    scopus 로고
    • Proton-coupled electron transfer in soybean lipoxygenase
    • Hatcher E, Soudackov V, Hammes-Schiffer S (2004) Proton-coupled electron transfer in soybean lipoxygenase. J Am Chem Soc 126:5763-5775.
    • (2004) J Am Chem Soc , vol.126 , pp. 5763-5775
    • Hatcher, E.1    Soudackov, V.2    Hammes-Schiffer, S.3
  • 10
    • 33846047459 scopus 로고    scopus 로고
    • Proton-coupled electron transfer in soybean lipoxygenase: Dynamical behavior and temperature dependence of kinetic isotope effects
    • Hatcher E, Soudackov V, Hammes-Schiffer S (2007) Proton-coupled electron transfer in soybean lipoxygenase: Dynamical behavior and temperature dependence of kinetic isotope effects. J Am Chem Soc 129:187-196.
    • (2007) J Am Chem Soc , vol.129 , pp. 187-196
    • Hatcher, E.1    Soudackov, V.2    Hammes-Schiffer, S.3
  • 11
    • 0037328843 scopus 로고    scopus 로고
    • Density-functional investigation on the mechanism of H-atom abstraction by lipoxygenase
    • Lehnert N, Solomon EI (2003) Density-functional investigation on the mechanism of H-atom abstraction by lipoxygenase. J Biol Inorg Chem 8:294-305.
    • (2003) J Biol Inorg Chem , vol.8 , pp. 294-305
    • Lehnert, N.1    Solomon, E.I.2
  • 12
    • 4544316340 scopus 로고    scopus 로고
    • Hydrogen abstraction by soybean lipoxygenase-1: Density-functional theory study on active site models in terms of Gibbs free energies
    • Tejero I, Eriksson LA, Gonzalez-Lafont A, Marquet J, Lluch JM (2004) Hydrogen abstraction by soybean lipoxygenase-1: Density-functional theory study on active site models in terms of Gibbs free energies. J Phys Chem B 108:13831-13838.
    • (2004) J Phys Chem B , vol.108 , pp. 13831-13838
    • Tejero, I.1    Eriksson, L.A.2    Gonzalez-Lafont, A.3    Marquet, J.4    Lluch, J.M.5
  • 13
    • 1542317813 scopus 로고    scopus 로고
    • Manganese(II) Zero-field interaction in cambialistic and manganese superoxide dismutases and its relationship to the structure of the metal binding site
    • Olsson MHM, Siegbahn PEM, Warshel A (2004) Manganese(II) Zero-field interaction in cambialistic and manganese superoxide dismutases and its relationship to the structure of the metal binding site. J Am Chem Soc 126:2820-2828.
    • (2004) J Am Chem Soc , vol.126 , pp. 2820-2828
    • Olsson, M.H.M.1    Siegbahn, P.E.M.2    Warshel, A.3
  • 14
    • 1842763785 scopus 로고    scopus 로고
    • Temperature dependence of kinetic isotope effects for enzymatic carbon-hydrogen bond cleavage
    • Siebrand W, Smedarchina Z (2004) Temperature dependence of kinetic isotope effects for enzymatic carbon-hydrogen bond cleavage. J Phys Chem B 108:4185-4195.
    • (2004) J Phys Chem B , vol.108 , pp. 4185-4195
    • Siebrand, W.1    Smedarchina, Z.2
  • 15
    • 0037123216 scopus 로고    scopus 로고
    • Temperature-dependent isotope effects in soybean lipoxygenase-1: Correlating hydrogen tunneling with protein dynamics
    • Knapp MJ, Rickert K, Klinman JP (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
  • 16
    • 28644449439 scopus 로고    scopus 로고
    • Modeling temperature dependent kinetic isotope effects for hydrogen transfer in a series of soybean lipoxygenase mutants: The effect of anharmonicity upon transfer distance
    • Meyer M, Klinman JP (2005) Modeling temperature dependent kinetic isotope effects for hydrogen transfer in a series of soybean lipoxygenase mutants: The effect of anharmonicity upon transfer distance. Chem Phys 319:283-296.
    • (2005) Chem Phys , vol.319 , pp. 283-296
    • Meyer, M.1    Klinman, J.P.2
  • 17
    • 0026707687 scopus 로고
    • Vibrationally enhanced tunneling as a mechanism for enzymatic hydrogen transfer
    • Bruno WJ, Bialek W (1992) Vibrationally enhanced tunneling as a mechanism for enzymatic hydrogen transfer. Biophys J 63:689-699.
    • (1992) Biophys J , vol.63 , pp. 689-699
    • Bruno, W.J.1    Bialek, W.2
  • 18
    • 33748902041 scopus 로고    scopus 로고
    • The role of tunneling in enzyme catalysis of C-H activation
    • Klinman JP (2006) The role of tunneling in enzyme catalysis of C-H activation. Biochim Biophys Acta 1757:981-987.
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 981-987
    • Klinman, J.P.1
  • 19
    • 0000205312 scopus 로고    scopus 로고
    • Enzyme catalysis: Beyond classical paradigms
    • Kohen A, Klinman JP (1998) Enzyme catalysis: Beyond classical paradigms. Acc Chem Res 31:397-404.
    • (1998) Acc Chem Res , vol.31 , pp. 397-404
    • Kohen, A.1    Klinman, J.P.2
  • 21
    • 0033519723 scopus 로고    scopus 로고
    • Enzyme dynamics and hydrogen tunneling in a thermophilic alcohol dehydrogenase
    • Kohen A, Cannio R, Bartolucci S, Klinman JP (1999) (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
  • 22
    • 3042709505 scopus 로고    scopus 로고
    • Thermal-activated protein mobility and its correlation with catalysis in thermophilic alcohol dehydrogenase
    • Liang Z-X, Lee T, Resing KA, Ahn NG, Klinman JP (2004) Thermal-activated protein mobility and its correlation with catalysis in thermophilic alcohol dehydrogenase. Proc Natl Acad Sci USA 101:9556-9561.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9556-9561
    • Liang, Z.-X.1    Lee, T.2    Resing, K.A.3    Ahn, N.G.4    Klinman, J.P.5
  • 23
    • 33748601471 scopus 로고    scopus 로고
    • Tunneling and dynamics in enzymatic hydride transfer
    • Nagel Z, Klinman JP (2006) Tunneling and dynamics in enzymatic hydride transfer. Chem Rev 106:3095-3118.
    • (2006) Chem Rev , vol.106 , pp. 3095-3118
    • Nagel, Z.1    Klinman, J.P.2
  • 24
    • 33750441144 scopus 로고    scopus 로고
    • Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase
    • Wang L, Goodey NM, Benkovic SJ, Kohen A (2006) Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase. Proc Natl Acad Sci USA 103:15753-15758.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 15753-15758
    • Wang, L.1    Goodey, N.M.2    Benkovic, S.J.3    Kohen, A.4
  • 25
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • Marcus RA, Sutin N (1985) (1985) Electron transfers 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
  • 26
    • 0033305793 scopus 로고    scopus 로고
    • Proton and hydrogen atom tunneling in hydrolytic and redox enzyme catalysis
    • Kuznetsov AM, Ulstrup J (1999) Proton and hydrogen atom tunneling 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
  • 27
    • 33748216903 scopus 로고
    • Electron-transfer reactions in chemistry: Theory and experiment (Nobel lecture)
    • Marcus RA (1993) Electron-transfer reactions in chemistry: Theory and experiment (Nobel lecture). Angew Chem Int Ed Eng 32:1111-1121.
    • (1993) Angew Chem Int Ed Eng , vol.32 , pp. 1111-1121
    • Marcus, R.A.1
  • 28
    • 0038408766 scopus 로고    scopus 로고
    • Spectroscopic characterization of soybean lipoxygenase-1 mutants: The role of second coordination sphere residues in the regulation of enzyme activity
    • Schenk G, Neidig ML, Zhow J, Holman TR, Solomon EI (2003) Spectroscopic characterization of soybean lipoxygenase-1 mutants: The role of second coordination sphere residues in the regulation of enzyme activity. Biochemistry 42:7294-7302.
    • (2003) Biochemistry , vol.42 , pp. 7294-7302
    • Schenk, G.1    Neidig, M.L.2    Zhow, J.3    Holman, T.R.4    Solomon, E.I.5
  • 29
    • 0043236031 scopus 로고    scopus 로고
    • The first experimental test of the hypothesis that enzymes have evolved to enhance hydrogen tunneling
    • Doll KM, Bender BR, Lin Y, Finke RG (2003) The first experimental test of the hypothesis that enzymes have evolved to enhance hydrogen tunneling. J Am Chem Soc 125:10877-10884.
    • (2003) J Am Chem Soc , vol.125 , pp. 10877-10884
    • Doll, K.M.1    Bender, B.R.2    Lin, Y.3    Finke, R.G.4
  • 30
    • 0042905762 scopus 로고    scopus 로고
    • A compelling experimental test of the hypothesis that enzymes have evolved to enhance quantum mechanical tunneling in hydrogen transfer reactions: The beta-neopentylcobalamin system combined with prior adocobalamin data
    • Doll KM, Finke RG (2003) A compelling experimental test of the hypothesis that enzymes have evolved to enhance quantum mechanical tunneling in hydrogen transfer reactions: The beta-neopentylcobalamin system combined with prior adocobalamin data. Inorg Chem 42:4849-4856.
    • (2003) Inorg Chem , vol.42 , pp. 4849-4856
    • Doll, K.M.1    Finke, R.G.2
  • 31
    • 0141732235 scopus 로고    scopus 로고
    • Enzyme tunneling idea questioned: Comparison of H-transfer reactions with and without enzyme shows no enhanced tunneling
    • Kemsley J (2003) Enzyme tunneling idea questioned: Comparison of H-transfer reactions with and without enzyme shows no enhanced tunneling. Chem Eng News 81:29-30.
    • (2003) Chem Eng News , vol.81 , pp. 29-30
    • Kemsley, J.1
  • 32
    • 0037045257 scopus 로고    scopus 로고
    • C-H bond activation by a ferric methoxide complex: Modeling the rate-determining step in the mechanism of lipoxygenase
    • Goldsmith CR, Jonas RT, Stack DP (2002) C-H bond activation by a ferric methoxide complex: Modeling the rate-determining step in the mechanism of lipoxygenase. J Am Chem Soc 124:83-96.
    • (2002) J Am Chem Soc , vol.124 , pp. 83-96
    • Goldsmith, C.R.1    Jonas, R.T.2    Stack, D.P.3
  • 33
    • 0035954384 scopus 로고    scopus 로고
    • Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1
    • Tomchick DR, Phan P, Cymborowski M, Minor W, Holman TR (2001) Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1. Biochemistry 40:7509-7517.
    • (2001) Biochemistry , vol.40 , pp. 7509-7517
    • Tomchick, D.R.1    Phan, P.2    Cymborowski, M.3    Minor, W.4    Holman, T.R.5


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