메뉴 건너뛰기




Volumn 134, Issue 23, 2012, Pages 9749-9754

Pressure effects on enzyme-catalyzed quantum tunneling events arise from protein-specific structural and dynamic changes

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC AMINES; CONSTANT PRESSURES; DONOR-ACCEPTORS; DYNAMIC CHANGES; ENZYME-CATALYZED REACTIONS; KINETIC ISOTOPE EFFECTS; MOLECULAR DYNAMICS SIMULATIONS; PHENYLETHYLAMINES; PRESSURE AND TEMPERATURE; QUANTUM MECHANICAL; QUANTUM TUNNELING; REACTION COORDINATES; TUNNELING MODELS;

EID: 84862239089     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja3024115     Document Type: Article
Times cited : (23)

References (43)
  • 1
    • 0024573393 scopus 로고
    • Hydrogen Tunneling in Enzyme-Reactions
    • Cha, Y.; Murray, C. J.; Klinman, J. P. Hydrogen Tunneling in Enzyme-Reactions Science 1989, 243, 1325
    • (1989) Science , vol.243 , pp. 1325
    • Cha, Y.1    Murray, C.J.2    Klinman, J.P.3
  • 4
    • 77953692230 scopus 로고    scopus 로고
    • Examining the case for the effect of barrier compression on tunneling, vibrationally enhanced catalysis, catalytic entropy and related issues
    • Kamerlin, S. C. L.; Mavri, J.; Warshel, A. Examining the case for the effect of barrier compression on tunneling, vibrationally enhanced catalysis, catalytic entropy and related issues FEBS Lett. 2010, 584, 2759
    • (2010) FEBS Lett. , vol.584 , pp. 2759
    • Kamerlin, S.C.L.1    Mavri, J.2    Warshel, A.3
  • 5
    • 84857515422 scopus 로고    scopus 로고
    • Good Vibrations in Enzyme Catalysed Reactions
    • Hay, S.; Scrutton, N. S. Good Vibrations in Enzyme Catalysed Reactions Nature Chem. 2012, 4, 161
    • (2012) Nature Chem. , vol.4 , pp. 161
    • Hay, S.1    Scrutton, N.S.2
  • 6
    • 84857542642 scopus 로고    scopus 로고
    • Taking Ockhams razor to enzyme dynamics and catalysis
    • Glowacki, D. R.; Harvey, J. N.; Mulholland, A. J. Taking Ockhams razor to enzyme dynamics and catalysis Nature Chem. 2012, 4, 169
    • (2012) Nature Chem. , vol.4 , pp. 169
    • Glowacki, D.R.1    Harvey, J.N.2    Mulholland, A.J.3
  • 7
    • 77955165990 scopus 로고    scopus 로고
    • Tunneling in enzymatic and nonenzymatic hydrogen transfer reactions
    • Truhlar, D. G. Tunneling in enzymatic and nonenzymatic hydrogen transfer reactions J. Phys. Org. Chem. 2010, 23, 660
    • (2010) J. Phys. Org. Chem. , vol.23 , pp. 660
    • Truhlar, D.G.1
  • 8
    • 0033519723 scopus 로고    scopus 로고
    • Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase
    • Kohen, A.; Cannio, R.; Bartolucci, S.; Klinman, J. P. Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase Nature 1999, 399, 496
    • (1999) Nature , vol.399 , pp. 496
    • Kohen, A.1    Cannio, R.2    Bartolucci, S.3    Klinman, J.P.4
  • 9
    • 0242267579 scopus 로고    scopus 로고
    • Evidence for environmentally coupled hydrogen tunneling during dihydrofolate reductase catalysis
    • Maglia, G.; Allemann, R. K. Evidence for environmentally coupled hydrogen tunneling during dihydrofolate reductase catalysis J. Am. Chem. Soc. 2003, 125, 13372
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13372
    • Maglia, G.1    Allemann, R.K.2
  • 10
    • 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
    • Basran, J.; Harris, R. J.; Sutcliffe, M. J.; Scrutton, N. S. 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. 2003, 278, 43973
    • (2003) J. Biol. Chem. , vol.278 , pp. 43973
    • Basran, J.1    Harris, R.J.2    Sutcliffe, M.J.3    Scrutton, N.S.4
  • 11
    • 0002845355 scopus 로고
    • In; Buncel, E. Lee, C. C. Elsevier, London: Vol
    • Isaacs, N. S. In Isotope Effects in Organic Chemistry; Buncel, E.; Lee, C. C., Eds.; Elsevier, London: 1984; Vol. 6, p 67.
    • (1984) Isotope Effects in Organic Chemistry , vol.6 , pp. 67
    • Isaacs, N.S.1
  • 12
    • 33748341301 scopus 로고    scopus 로고
    • Unusual origins of isotope effects in enzyme-catalysed reactions
    • Northrop, D. B. Unusual origins of isotope effects in enzyme-catalysed reactions Phil. Trans. Royal Soc. B 2006, 361, 1341
    • (2006) Phil. Trans. Royal Soc. B , vol.361 , pp. 1341
    • Northrop, D.B.1
  • 13
    • 0017398625 scopus 로고
    • Pressure effects on proton tunnelling
    • Isaacs, N. S.; Javaid, K.; Rannala, E. Pressure Effects on Proton Tunnelling Nature 1977, 268, 372 (Pubitemid 8142011)
    • (1977) Nature , vol.268 , Issue.5618 , pp. 372
    • Isaacs, N.S.1    Javaid, K.2    Rannala, E.3
  • 14
    • 0033553158 scopus 로고    scopus 로고
    • Effects of high pressure on isotope effects and hydrogen tunneling
    • Northrop, D. B. Effects of high pressure on isotope effects and hydrogen tunneling J. Am. Chem. Soc. 1999, 121, 3521
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 3521
    • Northrop, D.B.1
  • 15
    • 33846307373 scopus 로고    scopus 로고
    • Promoting motions in enzyme catalysis probed by pressure studies of kinetic isotope effects
    • Hay, S.; Sutcliffe, M. J.; Scrutton, N. S. Promoting motions in enzyme catalysis probed by pressure studies of kinetic isotope effects Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 507
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 507
    • Hay, S.1    Sutcliffe, M.J.2    Scrutton, N.S.3
  • 16
    • 51849095467 scopus 로고    scopus 로고
    • Incorporation of hydrostatic pressure into models of hydrogen tunneling highlights a role for pressure-modulated promoting vibrations
    • Hay, S.; Scrutton, N. S. Incorporation of hydrostatic pressure into models of hydrogen tunneling highlights a role for pressure-modulated promoting vibrations Biochemistry 2008, 47, 9880
    • (2008) Biochemistry , vol.47 , pp. 9880
    • Hay, S.1    Scrutton, N.S.2
  • 17
    • 72249089538 scopus 로고    scopus 로고
    • Evidence to support the hypothesis that promoting vibrations enhance the rate of an enzyme catalyzed H-tunneling reaction
    • Pudney, C. R.; Hay, S.; Levy, C.; Pang, J. Y.; Sutcliffe, M. J.; Leys, D.; Scrutton, N. S. Evidence to support the hypothesis that promoting vibrations enhance the rate of an enzyme catalyzed H-tunneling reaction J. Am. Chem. Soc. 2009, 131, 17072
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 17072
    • Pudney, C.R.1    Hay, S.2    Levy, C.3    Pang, J.Y.4    Sutcliffe, M.J.5    Leys, D.6    Scrutton, N.S.7
  • 19
    • 0037171123 scopus 로고    scopus 로고
    • Effects of high pressure on enzymatic activity
    • Northrop, D. B. Effects of high pressure on enzymatic activity Biochim. Biophys. Acta 2002, 1595, 71
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 71
    • Northrop, D.B.1
  • 20
    • 77955165989 scopus 로고    scopus 로고
    • Probing active site geometry using high pressure and secondary isotope effects in an enzyme-catalysed 'deep' H-tunneling reaction
    • Hay, S.; Pudney, C. R.; Sutcliffe, M. J.; Scrutton, N. S. Probing active site geometry using high pressure and secondary isotope effects in an enzyme-catalysed 'deep' H-tunneling reaction J. Phys. Org. Chem. 2010, 23, 696
    • (2010) J. Phys. Org. Chem. , vol.23 , pp. 696
    • Hay, S.1    Pudney, C.R.2    Sutcliffe, M.J.3    Scrutton, N.S.4
  • 22
    • 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
    • Johannissen, L. O.; Hay, S.; Scrutton, N. S.; Sutcliffe, M. J. 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 2007, 111, 2631
    • (2007) J. Phys. Chem. B , vol.111 , pp. 2631
    • Johannissen, L.O.1    Hay, S.2    Scrutton, N.S.3    Sutcliffe, M.J.4
  • 24
    • 74049100280 scopus 로고    scopus 로고
    • Barrier compression and its contribution to both classical and quantum mechanical aspects of enzyme catalysis
    • Hay, S.; Johannissen, L.; Sutcliffe, M. J.; Scrutton, N. S. Barrier compression and its contribution to both classical and quantum mechanical aspects of enzyme catalysis Biophys. J. 2010, 98, 121
    • (2010) Biophys. J. , vol.98 , pp. 121
    • Hay, S.1    Johannissen, L.2    Sutcliffe, M.J.3    Scrutton, N.S.4
  • 25
    • 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
    • Johannissen, L. O.; Scrutton, N. S.; Sutcliffe, M. J. 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. Royal. Soc. Interface 2008, 5, S225
    • (2008) J. Royal. Soc. Interface , vol.5 , pp. 225
    • Johannissen, L.O.1    Scrutton, N.S.2    Sutcliffe, M.J.3
  • 26
    • 0000109395 scopus 로고
    • Thermodynamics of the association and the pressure dissociation of oligomeric proteins
    • Weber, G. Thermodynamics of the association and the pressure dissociation of oligomeric proteins J. Phys. Chem. 1993, 97, 7108
    • (1993) J. Phys. Chem. , vol.97 , pp. 7108
    • Weber, G.1
  • 28
    • 74049100280 scopus 로고    scopus 로고
    • Barrier compression and its contribution to both classical and quantum mechanical aspects of enzyme catalysis
    • Hay, S.; Johannissen, L. O.; Sutcliffe, M. J.; Scrutton, N. S. Barrier compression and its contribution to both classical and quantum mechanical aspects of enzyme catalysis Biophys. J. 2010, 98, 121
    • (2010) Biophys. J. , vol.98 , pp. 121
    • Hay, S.1    Johannissen, L.O.2    Sutcliffe, M.J.3    Scrutton, N.S.4
  • 29
    • 79951913324 scopus 로고    scopus 로고
    • How does pressure affect barrier compression and isotope effects in an enzymatic hydrogen tunneling reaction?
    • Johannissen, L. O.; Scrutton, N. S.; Sutcliffe, M. J. How does pressure affect barrier compression and isotope effects in an enzymatic hydrogen tunneling reaction? Angew. Chem., Int. Ed. 2011, 50, 2129
    • (2011) Angew. Chem., Int. Ed. , vol.50 , pp. 2129
    • Johannissen, L.O.1    Scrutton, N.S.2    Sutcliffe, M.J.3
  • 30
    • 0037012441 scopus 로고    scopus 로고
    • Identification of a protein-promoting vibration in the reaction catalyzed by horse liver alcohol dehydrogenase
    • Caratzoulas, S.; Mincer, J. S.; Schwartz, S. D. Identification of a protein-promoting vibration in the reaction catalyzed by horse liver alcohol dehydrogenase J. Am. Chem. Soc. 2002, 124, 3270
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3270
    • Caratzoulas, S.1    Mincer, J.S.2    Schwartz, S.D.3
  • 31
    • 77957205244 scopus 로고    scopus 로고
    • Do dynamic effects play a significant role in enzymatic catalysis? A theoretical analysis of formate dehydrogenase
    • Roca, M.; Oliva, M.; Castillo, R.; Moliner, V.; Tunon, I. Do dynamic effects play a significant role in enzymatic catalysis? A theoretical analysis of formate dehydrogenase Chem.-Eur. J. 2010, 16, 11399
    • (2010) Chem.-Eur. J. , vol.16 , pp. 11399
    • Roca, M.1    Oliva, M.2    Castillo, R.3    Moliner, V.4    Tunon, I.5
  • 33
    • 33846047459 scopus 로고    scopus 로고
    • Proton-coupled electron transfer in soybean lipoxygenase: Dynamical behavior and temperature dependence of kinetic isotope effects
    • Hatcher, E.; Soudackov, A. V.; Hammes-Schiffer, S. Proton-coupled electron transfer in soybean lipoxygenase: Dynamical behavior and temperature dependence of kinetic isotope effects J. Am. Chem. Soc. 2007, 129, 187
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 187
    • Hatcher, E.1    Soudackov, A.V.2    Hammes-Schiffer, S.3
  • 34
    • 0030817281 scopus 로고    scopus 로고
    • Large kinetic isotope effects in enzymatic proton transfer and the role of substrate oscillations
    • Antoniou, D.; Schwartz, S. D. Large kinetic isotope effects in enzymatic proton transfer and the role of substrate oscillations Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 12360
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12360
    • Antoniou, D.1    Schwartz, S.D.2
  • 35
    • 0033305793 scopus 로고    scopus 로고
    • Proton and hydrogen atom tunnelling in hydrolytic and redox enzyme catalysis
    • Kuznetsov, A. M.; Ulstrup, J. Proton and hydrogen atom tunnelling in hydrolytic and redox enzyme catalysis Can. J. Chem. 1999, 77, 1085
    • (1999) Can. J. Chem. , vol.77 , pp. 1085
    • Kuznetsov, A.M.1    Ulstrup, J.2
  • 36
    • 0037123216 scopus 로고    scopus 로고
    • Temperature-dependent isotope effects in soybean lipoxygenase-1: Correlating hydrogen tunneling with protein dynamics
    • Knapp, M. J.; Rickert, K.; Klinman, J. P. Temperature-dependent isotope effects in soybean lipoxygenase-1: Correlating hydrogen tunneling with protein dynamics J. Am. Chem. Soc. 2002, 124, 3865
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3865
    • Knapp, M.J.1    Rickert, K.2    Klinman, J.P.3
  • 37
    • 22944452805 scopus 로고    scopus 로고
    • Quantum and dynamical effects of proton donor-acceptor vibrational motion in nonadiabatic proton-coupled electron transfer reactions
    • Soudackov, A.; Hatcher, E.; Hammes-Schiffer, S. Quantum and dynamical effects of proton donor-acceptor vibrational motion in nonadiabatic proton-coupled electron transfer reactions J. Chem. Phys. 2005, 122.
    • (2005) J. Chem. Phys. , vol.122
    • Soudackov, A.1    Hatcher, E.2    Hammes-Schiffer, S.3
  • 38
    • 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. P.; Klinman, J. P. 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. 2005, 319, 283
    • (2005) Chem. Phys. , vol.319 , pp. 283
    • Meyer, M.P.1    Klinman, J.P.2
  • 40
    • 28044447627 scopus 로고    scopus 로고
    • Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis
    • Hothi, P.; Khadra, K. A.; Combe, J. P.; Leys, D.; Scrutton, N. S. Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis FEBS J. 2005, 272, 5894
    • (2005) FEBS J. , vol.272 , pp. 5894
    • Hothi, P.1    Khadra, K.A.2    Combe, J.P.3    Leys, D.4    Scrutton, N.S.5
  • 41
    • 67650500988 scopus 로고    scopus 로고
    • CHARMM: The Biomolecular Simulation Program
    • Brooks, B. R. CHARMM: The Biomolecular Simulation Program J. Comput. Chem. 2009, 30, 1545
    • (2009) J. Comput. Chem. , vol.30 , pp. 1545
    • Brooks, B.R.1
  • 42
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell, A. D. All-atom empirical potential for molecular modeling and dynamics studies of proteins J. Phys. Chem. B 1998, 102, 3586
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586
    • MacKerell, A.D.1
  • 43
    • 33748614305 scopus 로고    scopus 로고
    • Computational and theoretical methods to explore the relation between enzyme dynamics and catalysis
    • Antoniou, D.; Basner, J.; Nunez, S.; Schwartz, S. D. Computational and theoretical methods to explore the relation between enzyme dynamics and catalysis Chem. Rev. 2006, 106, 3170
    • (2006) Chem. Rev. , vol.106 , pp. 3170
    • Antoniou, D.1    Basner, J.2    Nunez, S.3    Schwartz, S.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.