메뉴 건너뛰기




Volumn 77, Issue 4, 1999, Pages 2184-2190

Enzyme dynamics and activity: Time-scale dependence of dynamical transitions in glutamate dehydrogenase solution

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMATE DEHYDROGENASE;

EID: 0032863425     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77058-X     Document Type: Article
Times cited : (81)

References (31)
  • 3
    • 0033051987 scopus 로고    scopus 로고
    • Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature
    • Cordone, L., M. Ferrand, E. Vitrano, and G. Zaccai. 1999. Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature. Biophys. J. 76:1043-1047.
    • (1999) Biophys. J. , vol.76 , pp. 1043-1047
    • Cordone, L.1    Ferrand, M.2    Vitrano, E.3    Zaccai, G.4
  • 4
    • 0025333959 scopus 로고
    • Temperature dependence of the low frequency dynamics of myoglobin
    • Cusack, S., and W. Doster. 1990. Temperature dependence of the low frequency dynamics of myoglobin. Biophys. J. 58:243-251.
    • (1990) Biophys. J. , vol.58 , pp. 243-251
    • Cusack, S.1    Doster, W.2
  • 5
    • 0029977715 scopus 로고    scopus 로고
    • The denaturation and degradation of stable enzymes at high temperatures
    • Daniel, R. M., M. Dines, and H. H. Petach. 1997. The denaturation and degradation of stable enzymes at high temperatures. Biochem. J. 317: 1-11.
    • (1997) Biochem. J. , vol.317 , pp. 1-11
    • Daniel, R.M.1    Dines, M.2    Petach, H.H.3
  • 7
    • 0026700192 scopus 로고
    • Protein dynamics. Vibrational coupling, spectral broadening mechanisms, and anharmonicity effects in carbonmonoxy heme proteins studied by the temperature dependence of the Soret band lineshape
    • Di Pace, A., A. Cupane, M. Leone, E. Vitrano, and L. Cordone. 1992. Protein dynamics. Vibrational coupling, spectral broadening mechanisms, and anharmonicity effects in carbonmonoxy heme proteins studied by the temperature dependence of the Soret band lineshape. Biophys. J. 63:475-484.
    • (1992) Biophys. J. , vol.63 , pp. 475-484
    • Di Pace, A.1    Cupane, A.2    Leone, M.3    Vitrano, E.4    Cordone, L.5
  • 8
    • 0024976853 scopus 로고
    • Dynamical transition of myoglobin revealed by inelastic neutron scattering
    • Doster, W., S. C. Cusack, and W. Petry. 1989. Dynamical transition of myoglobin revealed by inelastic neutron scattering. Nature. 337: 754-756.
    • (1989) Nature , vol.337 , pp. 754-756
    • Doster, W.1    Cusack, S.C.2    Petry, W.3
  • 9
    • 0027491027 scopus 로고
    • Thermal motions and function of bacteriorhodopsin in purple membranes: Effects of temperature and hydration studied by neutron scattering
    • Ferrand, M., A. J. Dianoux, W. Petry, and G. Zaccai. 1993. Thermal motions and function of bacteriorhodopsin in purple membranes: effects of temperature and hydration studied by neutron scattering. Proc. Natl. Acad. Sci. USA. 90:9668-9672.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9668-9672
    • Ferrand, M.1    Dianoux, A.J.2    Petry, W.3    Zaccai, G.4
  • 11
    • 36849142809 scopus 로고
    • New looks at protein motions
    • Frauenfelder, H. 1989. New looks at protein motions. Nature 338: 623-624.
    • (1989) Nature , vol.338 , pp. 623-624
    • Frauenfelder, H.1
  • 12
    • 0018793861 scopus 로고
    • Temperature-dependent x-ray diffraction as a probe of protein structural dynamics
    • Frauenfelder, H., G. A. Petsko, and D. Tsernoglou. 1979. Temperature-dependent x-ray diffraction as a probe of protein structural dynamics. Nature. 280:558-563.
    • (1979) Nature , vol.280 , pp. 558-563
    • Frauenfelder, H.1    Petsko, G.A.2    Tsernoglou, D.3
  • 13
    • 0027333040 scopus 로고
    • L-glutamate dehydrogenase: Distribution, properties and mechanism
    • R. D.R. C.
    • Hudson, R. D.,R. D.R. C. and R. M. Daniel. 1993. L-Glutamate dehydrogenase: distribution, properties and mechanism. Comp. Biochem. Physiol. 106:767-792.
    • (1993) Comp. Biochem. Physiol. , vol.106 , pp. 767-792
    • Hudson, R.D.1    Daniel, R.M.2
  • 14
    • 0029016560 scopus 로고
    • Steady state kinetics of the glutamate dehydrogenase from an archaebacterial extreme thermophile, isolate AN1
    • Hudson, R. C., and R. M. Daniel. 1995. Steady state kinetics of the glutamate dehydrogenase from an archaebacterial extreme thermophile, isolate AN1. Biochim. Biophys. Acta. 1250:60-68.
    • (1995) Biochim. Biophys. Acta , vol.1250 , pp. 60-68
    • Hudson, R.C.1    Daniel, R.M.2
  • 15
    • 0027431229 scopus 로고
    • Glutamate dehydrogenase from the extremely thermophilic archaebacterial isolate, AN1
    • Hudson, R. C., L. D. Ruttersmith, and R. M. Daniel. 1993. Glutamate dehydrogenase from the extremely thermophilic archaebacterial isolate, AN1. Biochim. Biophys. Acta. 1202:244-250.
    • (1993) Biochim. Biophys. Acta , vol.1202 , pp. 244-250
    • Hudson, R.C.1    Ruttersmith, L.D.2    Daniel, R.M.3
  • 16
    • 0002131341 scopus 로고
    • Evidence for conformational and diffusional mean square displacements in frozen aqueous solution of myogloblin
    • Keller, H., and P. G. Debrunner. 1980. Evidence for conformational and diffusional mean square displacements in frozen aqueous solution of myogloblin. Phys. Rev. Lett. 45:68-67.
    • (1980) Phys. Rev. Lett. , vol.45 , pp. 68-167
    • Keller, H.1    Debrunner, P.G.2
  • 17
    • 0000988129 scopus 로고
    • Protein dynamics from Mossbauer spectra: The temperature dependence
    • Knapp, E. W., S. F. Fischer, and F. Parak. 1982. Protein dynamics from Mossbauer spectra: the temperature dependence. J. Phys. Chem. 86: 5042-5047.
    • (1982) J. Phys. Chem. , vol.86 , pp. 5042-5047
    • Knapp, E.W.1    Fischer, S.F.2    Parak, F.3
  • 18
    • 0344863187 scopus 로고    scopus 로고
    • Thermal motions in bacteriorhodopsin at different hydration levels studied by neutron scattering: Correlation with kinetics and light-induced conformational changes
    • Lehnert, U., V. Réat, M. Weik, G. Zaccai, and C. Pfister. 1998. Thermal motions in bacteriorhodopsin at different hydration levels studied by neutron scattering: correlation with kinetics and light-induced conformational changes. Biophys. J. 75:1945-1952.
    • (1998) Biophys. J. , vol.75 , pp. 1945-1952
    • Lehnert, U.1    Réat, V.2    Weik, M.3    Zaccai, G.4    Pfister, C.5
  • 19
    • 0030004479 scopus 로고    scopus 로고
    • Structural fluctuations of myoglobin from normal-modes, Mossbauer, Raman, and absorption spectroscopy
    • Melchers, B., E. W. Knapp, F. Parak, L. Cordone, A. Cupane, and M. Leone. 1996. Structural fluctuations of myoglobin from normal-modes, Mossbauer, Raman, and absorption spectroscopy. Biophys. J. 70: 2092-2099.
    • (1996) Biophys. J. , vol.70 , pp. 2092-2099
    • Melchers, B.1    Knapp, E.W.2    Parak, F.3    Cordone, L.4    Cupane, A.5    Leone, M.6
  • 20
    • 0028812131 scopus 로고    scopus 로고
    • The effect of low temperatures on enzyme activity
    • More, R., R. M. Daniel, and H. H. Petach. 1996. The effect of low temperatures on enzyme activity. Biochem. J. 305:17-20.
    • (1996) Biochem. J. , vol.305 , pp. 17-20
    • More, R.1    Daniel, R.M.2    Petach, H.H.3
  • 21
    • 0019135979 scopus 로고
    • Evidence for a correlation between the photo induced electron transfer and dynamic properties of the chromatophore membranes from Rhodospirillum rubrum
    • Parak, F., E. N. Frolov, A. A. Kononenko, R. L. Mossbauer, V. I. Goldonskii, and A. G. Rubin. 1980. Evidence for a correlation between the photo induced electron transfer and dynamic properties of the chromatophore membranes from Rhodospirillum rubrum. FEBS Lett. 117: 368-372.
    • (1980) FEBS Lett. , vol.117 , pp. 368-372
    • Parak, F.1    Frolov, E.N.2    Kononenko, A.A.3    Mossbauer, R.L.4    Goldonskii, V.I.5    Rubin, A.G.6
  • 22
    • 0020333863 scopus 로고
    • Protein dynamics: Mossbauer spectroscopy on deoxymyoglobin crystals
    • Parak, F., E. W. Knapp, and D. Kucheida. 1982. Protein dynamics: Mossbauer spectroscopy on deoxymyoglobin crystals. J. Mol. Biol. 161: 177-194.
    • (1982) J. Mol. Biol. , vol.161 , pp. 177-194
    • Parak, F.1    Knapp, E.W.2    Kucheida, D.3
  • 23
    • 0032548990 scopus 로고    scopus 로고
    • Influence of antiviral compound on the temperature dependence of viral protein flexibility and packing
    • Phelps, D. K., P. J. Rossky, and C. B. Post. 1998. Influence of antiviral compound on the temperature dependence of viral protein flexibility and packing. J. Mol. Biol. 276:331-337.
    • (1998) J. Mol. Biol. , vol.276 , pp. 331-337
    • Phelps, D.K.1    Rossky, P.J.2    Post, C.B.3
  • 24
    • 0026720247 scopus 로고
    • Crystalline ribonuclease A loses function below the dynamical transition at 220K
    • Rassmussen, B. F., A. M. Stock, D. Ringe, and G. A. Petsko. 1992. Crystalline ribonuclease A loses function below the dynamical transition at 220K. Nature. 357:523-424.
    • (1992) Nature , vol.357 , pp. 523-1424
    • Rassmussen, B.F.1    Stock, A.M.2    Ringe, D.3    Petsko, G.A.4
  • 25
    • 0032574723 scopus 로고    scopus 로고
    • Dynamics of different functional parts of bacteriorhodopsin: H-2H labelling and neutron scattering
    • Réat, V., H. Patzelt, M. Ferrand, C. Pfister, D. Oesterhelt, and G. Zaccai. 1998. Dynamics of different functional parts of bacteriorhodopsin: H-2H labelling and neutron scattering. Proc. Natl. Acad. Sci. USA. 95: 4970-4975.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4970-4975
    • Réat, V.1    Patzelt, H.2    Ferrand, M.3    Pfister, C.4    Oesterhelt, D.5    Zaccai, G.6
  • 26
    • 0002943198 scopus 로고    scopus 로고
    • Functional dynamics in purple membrane
    • S. Cusack, H. Buttner, M. Ferrand, P. Langan, and P. Timmins, editors. Adenine Press, Schenectady, NY
    • Réat, V., G. Zaccai, M. Ferrand, and C. Pfister. 1997. Functional dynamics in purple membrane. In Biological Macromolecular Dynamics. S. Cusack, H. Buttner, M. Ferrand, P. Langan, and P. Timmins, editors. Adenine Press, Schenectady, NY. 117-122.
    • (1997) Biological Macromolecular Dynamics , pp. 117-122
    • Réat, V.1    Zaccai, G.2    Ferrand, M.3    Pfister, C.4
  • 27
    • 0025877453 scopus 로고
    • Protein hydration and function
    • Rupley, J. A., and G. Careri. 1991. Protein hydration and function. Adv. Protein Chem. 41:37-172.
    • (1991) Adv. Protein Chem. , vol.41 , pp. 37-172
    • Rupley, J.A.1    Careri, G.2
  • 28
    • 0025938315 scopus 로고
    • Protein dynamics: Comparison of simulation with inelastic neutron scattering experiments
    • Smith, J. C. 1991. Protein dynamics: comparison of simulation with inelastic neutron scattering experiments. Q. Rev. Biophys. 25:227-293.
    • (1991) Q. Rev. Biophys. , vol.25 , pp. 227-293
    • Smith, J.C.1
  • 29
    • 0026606219 scopus 로고
    • Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease A at nine different temperatures from 98 to 320 K
    • Tilton, R. F., J. C. Dewan, and G. A. Petsko. 1992. Effects of temperature on protein structure and dynamics: x-ray crystallographic studies of the protein ribonuclease A at nine different temperatures from 98 to 320 K. Biochemistry. 31:2469-2481.
    • (1992) Biochemistry , vol.31 , pp. 2469-2481
    • Tilton, R.F.1    Dewan, J.C.2    Petsko, G.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.