메뉴 건너뛰기




Volumn 25, Issue 9, 2000, Pages 405-408

Enzyme catalysis: Over-the-barrier or through-the-barrier?

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ENERGY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME BINDING; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN MODIFICATION; QUANTUM MECHANICS; SHORT SURVEY; THERMODYNAMICS;

EID: 0034283867     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(00)01642-X     Document Type: Short Survey
Times cited : (56)

References (30)
  • 2
    • 0024298964 scopus 로고    scopus 로고
    • How do enzymes work?
    • Kraut J. How do enzymes work? Science. 242:1998;533-540.
    • (1998) Science , vol.242 , pp. 533-540
    • Kraut, J.1
  • 3
    • 0030093768 scopus 로고    scopus 로고
    • The potential of catalytic antibodies
    • Kirby A.J. The potential of catalytic antibodies. Acta Chem. Scand. 50:1996;203-210.
    • (1996) Acta Chem. Scand. , vol.50 , pp. 203-210
    • Kirby, A.J.1
  • 6
    • 33947547892 scopus 로고
    • Molecular architecture and biological reactions
    • Pauling L. Molecular architecture and biological reactions. Chem. Eng. News. 24:1946;1375-1377.
    • (1946) Chem. Eng. News , vol.24 , pp. 1375-1377
    • Pauling, L.1
  • 7
    • 0029782456 scopus 로고    scopus 로고
    • A perspective on biological catalysis
    • Cannon W.R.et al. A perspective on biological catalysis. Nat. Struct. Biol. 3:1996;821-833.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 821-833
    • Cannon, W.R.1
  • 8
    • 0001173909 scopus 로고
    • Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering
    • Leatherbarrow RJ.et al. Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering. Proc. Natl. Acad. Sci. U. S. A. 82:1985;7840-7844.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 7840-7844
    • Leatherbarrow, RJ.1
  • 9
    • 0032475870 scopus 로고    scopus 로고
    • Enzyme catalytic power minireview series
    • Neet K. Enzyme catalytic power minireview series. J. Biol. Chem. 273:1998;25527-25528.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25527-25528
    • Neet, K.1
  • 10
    • 0032475836 scopus 로고    scopus 로고
    • The low barrier hydrogen bond in enzymatic catalysis
    • Cleland W.et al. The low barrier hydrogen bond in enzymatic catalysis. J. Biol. Chem. 273:1998;25529-25532.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25529-25532
    • Cleland, W.1
  • 11
    • 0032500555 scopus 로고    scopus 로고
    • Solvation, reorganisation energy, and biological catalysis
    • Cannon W., Benkovic S. Solvation, reorganisation energy, and biological catalysis. J. Biol. Chem. 273:1998;26257-26260.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26257-26260
    • Cannon, W.1    Benkovic, S.2
  • 12
    • 0032538627 scopus 로고    scopus 로고
    • Electrostatic origin of the catalytic power of enzymes and the role of preorganized active sites
    • Warshel A. Electrostatic origin of the catalytic power of enzymes and the role of preorganized active sites. J. Biol. Chem. 273:1998;27035-27038.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27035-27038
    • Warshel, A.1
  • 13
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and the diffusion model of chemical reactions
    • Kramers H.A. Brownian motion in a field of force and the diffusion model of chemical reactions. Physica (Utrecht). 7:1940;284-304.
    • (1940) Physica (Utrecht) , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 14
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • Marcus R.A., Sutin N. Electron transfers in chemistry and biology. Biochim. Biophys. Acta. 811:1985;265-316.
    • (1985) Biochim. Biophys. Acta , vol.811 , pp. 265-316
    • Marcus, R.A.1    Sutin, N.2
  • 15
    • 0028954039 scopus 로고
    • Hydrogen tunneling in enzyme catalysis
    • Bahnson B.J., Klinman J.P. Hydrogen tunneling in enzyme catalysis. Methods Enzymol. 249:1995;373-397.
    • (1995) Methods Enzymol. , vol.249 , pp. 373-397
    • Bahnson, B.J.1    Klinman, J.P.2
  • 16
    • 0024573393 scopus 로고
    • Hydrogen tunneling in enzyme reactions
    • Cha Y.et al. Hydrogen tunneling in enzyme reactions. Science. 243:1989;1325-1330.
    • (1989) Science , vol.243 , pp. 1325-1330
    • Cha, Y.1
  • 17
    • 0024379962 scopus 로고
    • Evidence that protium and deuterium undergo significant tunneling in the reaction catalysed by bovine serum amine oxidase
    • Grant K.L., Klinman J.P. Evidence that protium and deuterium undergo significant tunneling in the reaction catalysed by bovine serum amine oxidase. Biochemistry. 28:1989;6597-6605.
    • (1989) Biochemistry , vol.28 , pp. 6597-6605
    • Grant, K.L.1    Klinman, J.P.2
  • 18
    • 0028601412 scopus 로고
    • Hydrogen tunneling in the flavoenzyme monoamine oxidase B
    • Jonsson T.et al. Hydrogen tunneling in the flavoenzyme monoamine oxidase B. Biochemistry. 33:1994;14871-14878.
    • (1994) Biochemistry , vol.33 , pp. 14871-14878
    • Jonsson, T.1
  • 19
    • 0031025267 scopus 로고    scopus 로고
    • Effects of protein glycosylation on catalysis: Changes in hydrogen tunneling and enthalpy of activation in the glucose oxidase reaction
    • Kohen A.et al. Effects of protein glycosylation on catalysis: changes in hydrogen tunneling and enthalpy of activation in the glucose oxidase reaction. Biochemistry. 36:1997;2603-2611.
    • (1997) Biochemistry , vol.36 , pp. 2603-2611
    • Kohen, A.1
  • 20
    • 0029964954 scopus 로고    scopus 로고
    • Experimental evidence for extensive tunneling of hydrogen in the lipoxygenase reaction: Implications for enzyme catalysis
    • Jonsson T.et al. Experimental evidence for extensive tunneling of hydrogen in the lipoxygenase reaction: implications for enzyme catalysis. J. Am. Chem. Soc. 118:1996;10319-10320.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10319-10320
    • Jonsson, T.1
  • 21
    • 0000234681 scopus 로고
    • Hydrogen tunneling in condensed media
    • Suarez A., Silbey R. Hydrogen tunneling in condensed media. J. Chem. Phys. 94:1991;4809-4816.
    • (1991) J. Chem. Phys. , vol.94 , pp. 4809-4816
    • Suarez, A.1    Silbey, R.2
  • 22
    • 0026707687 scopus 로고
    • Vibrationally enhanced tunneling as a mechanism for enzymatic hydrogen transfer
    • Bruno W.J., Bialek W. Vibrationally enhanced tunneling as a mechanism for enzymatic hydrogen transfer. Biophys. J. 63:1992;689-699.
    • (1992) Biophys. J. , vol.63 , pp. 689-699
    • Bruno, W.J.1    Bialek, W.2
  • 23
    • 0033537697 scopus 로고    scopus 로고
    • Enzymatic H-transfer requires vibration-driven extreme tunnelling
    • Basran J.et al. Enzymatic H-transfer requires vibration-driven extreme tunnelling. Biochemistry. 38:1999;3218-3222.
    • (1999) Biochemistry , vol.38 , pp. 3218-3222
    • Basran, J.1
  • 24
    • 0034097153 scopus 로고    scopus 로고
    • Effect of pressure on deuterium isotope effects of yeast alcohol dehydrogenase: Evidence for mechanical models of catalysis
    • Northrop D.B., Cho Y.K. Effect of pressure on deuterium isotope effects of yeast alcohol dehydrogenase: evidence for mechanical models of catalysis. Biochemistry. 39:2000;2406-2412.
    • (2000) Biochemistry , vol.39 , pp. 2406-2412
    • Northrop, D.B.1    Cho, Y.K.2
  • 26
    • 0033568523 scopus 로고    scopus 로고
    • New insights into enzyme catalysis: Ground state tunnelling driven by protein dynamics
    • Scrutton N.S.et al. New insights into enzyme catalysis: ground state tunnelling driven by protein dynamics. Eur. J. Biochem. 264:1999;666-671.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 666-671
    • Scrutton, N.S.1
  • 27
    • 0033168713 scopus 로고    scopus 로고
    • Hydrogen tunneling in biology
    • Kohen A., Klinman J.P. Hydrogen tunneling in biology. Chem. Biol. 6:1999;R191-R198.
    • (1999) Chem. Biol. , vol.6 , pp. 191-R198
    • Kohen, A.1    Klinman, J.P.2
  • 28
    • 0033519723 scopus 로고    scopus 로고
    • Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase
    • Kohen A.et al. Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase. Nature. 399:1999;496-499.
    • (1999) Nature , vol.399 , pp. 496-499
    • Kohen, A.1
  • 29
    • 0034673186 scopus 로고    scopus 로고
    • Kinetic studies of the mechanism of C-H bond breakage by the heterotetrameric sarcosine oxidase of Arthrobacter sp. 1-IN
    • Harris R.J.et al. Kinetic studies of the mechanism of C-H bond breakage by the heterotetrameric sarcosine oxidase of Arthrobacter sp. 1-IN. Biochemistry. 39:2000;1189-1198.
    • (2000) Biochemistry , vol.39 , pp. 1189-1198
    • Harris, R.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.