메뉴 건너뛰기




Volumn 51, Issue 33, 2012, Pages 6654-6666

Inverse solvent isotope effects demonstrate slow aquo release from hypoxia inducible factor-prolyl hydroxylase (PHD2)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC CONDITIONS; ACTIVE SITE; ANAEROBIC METABOLISM; CIRCULAR DICHROISM SPECTRA; COORDINATION SITES; COORDINATION SPHERE; EXTENDED X-RAY ABSORPTION FINE STRUCTURE ANALYSIS; HYDROXYLASES; KETOGLUTARATE; PROLYL HYDROXYLASE DOMAINS; RATE-LIMITING STEPS; SECONDARY STRUCTURES; SOLVENT ISOTOPE EFFECTS; SPECTROSCOPIC PROBES; UNDERLYING MECHANISM; UV-VISIBLE;

EID: 84865437643     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300229y     Document Type: Article
Times cited : (26)

References (63)
  • 1
    • 0242330181 scopus 로고    scopus 로고
    • Oxygen sensing in the hypoxic response pathway: Regulation of the hypoxia-inducible transcription factor
    • DOI 10.1101/gad.1145503
    • Bruick, R. K. (2003) Oxygen sensing in the hypoxic response pathway: regulation of the hypoxia-inducible transcription factor Genes Dev. 17, 2614-2623 (Pubitemid 37363065)
    • (2003) Genes and Development , vol.17 , Issue.21 , pp. 2614-2623
    • Bruick, R.K.1
  • 2
    • 33847050240 scopus 로고    scopus 로고
    • Non-heme dioxygenases: Cellular sensors and regulators jelly rolled into one?
    • Ozer, A. and Bruick, R. K. (2007) Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one? Nat. Chem. Biol. 3, 144-153
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 144-153
    • Ozer, A.1    Bruick, R.K.2
  • 3
    • 8344237449 scopus 로고    scopus 로고
    • Hydroxylation of HIF-1: Oxygen sensing at the molecular level
    • Semenza, G. L. (2004) Hydroxylation of HIF-1: Oxygen sensing at the molecular level Physiology 19, 176-182 (Pubitemid 39481932)
    • (2004) Physiology , Issue.4 , pp. 176-182
    • Semenza, G.L.1
  • 5
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • DOI 10.1126/science.1066373
    • Bruick, R. K. and McKnight, S. L. (2001) A conserved family of prolyl-4-hydroxylases that modify HIF Science 294, 1337-1340 (Pubitemid 33063099)
    • (2001) Science , vol.294 , Issue.5545 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 8
    • 2442628211 scopus 로고    scopus 로고
    • FeII/alpha-ketoglutarate-dependent hydroxylases and related enzymes
    • Hausinger, R. P. (2004) FeII/alpha-ketoglutarate-dependent hydroxylases and related enzymes Crit. Rev. Biochem. Mol. Biol. 39, 21-68
    • (2004) Crit. Rev. Biochem. Mol. Biol. , vol.39 , pp. 21-68
    • Hausinger, R.P.1
  • 15
    • 0037161271 scopus 로고    scopus 로고
    • X-ray crystal structure of Escherichia coli taurine/α-ketoglutarate dioxygenase complexed to ferrous iron and substrates
    • DOI 10.1021/bi016014e
    • Elkins, J. M., Ryle, M. J., Clifton, I. J., Dunning Hotopp, J. C., Lloyd, J. S., Burzlaff, N. I., Baldwin, J. E., Hausinger, R. P., and Roach, P. L. (2002) X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates Biochemistry 41, 5185-5192 (Pubitemid 34411673)
    • (2002) Biochemistry , vol.41 , Issue.16 , pp. 5185-5192
    • Elkins, J.M.1    Ryle, M.J.2    Clifton, I.J.3    Dunning Hotopp, J.C.4    Lloyd, J.S.5    Burzlaff, N.I.6    Baldwin, J.E.7    Hausinger, R.P.8    Roach, P.L.9
  • 16
    • 12144286270 scopus 로고    scopus 로고
    • Crystal Structure of the Alkylsulfatase AtsK: Insights into the Catalytic Mechanism of the Fe(II) α-Ketoglutarate-Dependent Dioxygenase Superfamily
    • DOI 10.1021/bi035752v
    • Muller, I., Kahnert, A., Pape, T., Sheldrick, G. M., Meyer-Klaucke, W., Dierks, T., Kertesz, M., and Uson, I. (2004) Crystal structure of the alkylsulfatase AtsK: insights into the catalytic mechanism of the Fe(II) alpha-ketoglutarate-dependent dioxygenase superfamily Biochemistry 43, 3075-3088 (Pubitemid 38352258)
    • (2004) Biochemistry , vol.43 , Issue.11 , pp. 3075-3088
    • Muller, I.1    Kahnert, A.2    Pape, T.3    Sheldrick, G.M.4    Meyer-Klaucke, W.5    Dierks, T.6    Kertesz, M.7    Uson, I.8
  • 18
    • 0034828607 scopus 로고    scopus 로고
    • Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional α-KG-dependent non-heme iron enzyme: Correlation with mechanisms and reactivities
    • DOI 10.1021/ja004025+
    • Zhou, J., Kelly, W. L., Bachmann, B. O., Gunsior, M., Townsend, C. A., and Solomon, E. I. (2001) Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional alpha-KG-dependent non-heme iron enzyme: Correlation with mechanisms and reactivities J. Am. Chem. Soc. 123, 7388-7398 (Pubitemid 32879456)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.30 , pp. 7388-7398
    • Zhou, J.1    Kelly, W.L.2    Bachmann, B.O.3    Gunsior, M.4    Townsend, C.A.5    Solomon, E.I.6
  • 19
    • 0032481388 scopus 로고    scopus 로고
    • Circular dichroism and magnetic circular dichroism spectroscopic studies of the non-heme ferrous active site in clavaminate synthase and its interaction with α-ketoglutarate cosubstrate
    • DOI 10.1021/ja972408a
    • Pavel, E. G., Zhou, J., Busby, R. W., Gunsior, M., Townsend, C. A., and Solomon, E. I. (1998) Circular dichroism and magnetic circular dichroism spectroscopic studies of the non-heme ferrous active site in clavaminate synthase and its interaction with alpha-ketoglutarate cosubstrate J. Am. Chem. Soc. 120, 743-753 (Pubitemid 28081952)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.4 , pp. 743-753
    • Pavel, E.G.1    Zhou, J.2    Busby, R.W.3    Gunsior, M.4    Townsend, C.A.5    Solomon, E.I.6
  • 20
    • 11244279649 scopus 로고    scopus 로고
    • Many amino acid substitutions in a hypoxia-inducible transcription factor (HIF)-1α-like peptide cause only minor changes in its hydroxylation by the HIF prolyl 4-hydroxylases: Substitution of 3,4-dehydroproline or azetidine-2-carboxylic acid for the proline leads to a high rate of uncoupled 2-oxoglutarate decarboxylation
    • DOI 10.1074/jbc.M410287200
    • Myllyharju, J., Li, D. X., Hirsila, M., Koivunen, P., Brenner, M. C., Xu, L., Yang, C., and Kivirikko, K. I. (2004) Many amino acid substitutions in a hypoxia-inducible transcription factor (HIF)-1 alpha-like peptide cause only minor changes in its hydroxylation by the HIF prolyl 4-hydroxylases-Substitution of 3,4-dehydroproline or azetidine-2-carboxylic acid for the proline leads to a high rate of uncoupled 2-oxoglutarate decarboxylation J. Biol. Chem. 279, 55051-55059 (Pubitemid 40066497)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 55051-55059
    • Li, D.1    Hirsila, M.2    Koivunen, P.3    Brenner, M.C.4    Xu, L.5    Yang, C.6    Kivirikko, K.I.7    Myllyharju, J.8
  • 22
    • 0018132306 scopus 로고
    • Partial reaction of prolyl hydroxylase. (Gly-Pro-Ala)(n) stimulates α-ketoglutarate decarboxylation without prolyl hydroxylation
    • Rao, N. V. and Adams, E. (1978) Partial reaction of prolyl hydroxylase. (Gly-PRO-Ala)n stimulates alpha-ketoglutarate decarboxylation without prolyl hydroxylation J. Biol. Chem. 253, 6327-6330 (Pubitemid 9025305)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.18 , pp. 6327-6330
    • Rao, N.V.1    Adams, E.2
  • 23
    • 0032478205 scopus 로고    scopus 로고
    • Ascorbic acid-dependent turnover and reactivation of 2,4- dichlorophenoxyacetic acid/α-ketoglutarate dioxygenase using thiophenoxyacetic acid
    • DOI 10.1021/bi972388p
    • Saari, R. E. and Hausinger, R. P. (1998) Ascorbic acid-dependent turnover and reactivation of 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase using thiophenoxyacetic acid Biochemistry 37, 3035-3042 (Pubitemid 28145757)
    • (1998) Biochemistry , vol.37 , Issue.9 , pp. 3035-3042
    • Saari, R.E.1    Hausinger, R.P.2
  • 25
    • 0034802889 scopus 로고    scopus 로고
    • Alternative reactivity of an α-ketoglutarate-dependent iron(II) oxygenase: Enzyme self-hydroxylation
    • DOI 10.1021/ja005879x
    • Liu, A., Ho, R. Y., Que, L., Jr., Ryle, M. J., Phinney, B. S., and Hausinger, R. P. (2001) Alternative reactivity of an alpha-ketoglutarate- dependent iron(II) oxygenase: enzyme self-hydroxylation J. Am. Chem. Soc. 123, 5126-5127 (Pubitemid 32905680)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.21 , pp. 5126-5127
    • Liu, A.1    Ho, R.Y.N.2    Que Jr., L.3
  • 26
    • 55349091988 scopus 로고    scopus 로고
    • Coordination changes and auto-hydroxylation of FIH-1: Uncoupled O2-activation in a human hypoxia sensor
    • Chen, Y. H., Comeaux, L. M., Herbst, R. W., Saban, E., Kennedy, D. C., Maroney, M. J., and Knapp, M. J. (2008) Coordination changes and auto-hydroxylation of FIH-1: uncoupled O2-activation in a human hypoxia sensor J. Inorg. Biochem. 102, 2120-2129
    • (2008) J. Inorg. Biochem. , vol.102 , pp. 2120-2129
    • Chen, Y.H.1    Comeaux, L.M.2    Herbst, R.W.3    Saban, E.4    Kennedy, D.C.5    Maroney, M.J.6    Knapp, M.J.7
  • 27
    • 14844358869 scopus 로고    scopus 로고
    • IV-oxo intermediate
    • DOI 10.1021/bi048746n
    • Grzyska, P. K., Ryle, M. J., Monterosso, G. R., Liu, J., Ballou, D. P., and Hausinger, R. P. (2005) Steady-state and transient kinetic analyses of taurine/alpha-ketoglutarate dioxygenase: Effects of oxygen concentration, alternative sulfonates, and active-site variants on the Fe(IV)-oxo intermediate Biochemistry 44, 3845-3855 (Pubitemid 40358036)
    • (2005) Biochemistry , vol.44 , Issue.10 , pp. 3845-3855
    • Grzyska, P.K.1    Ryle, M.J.2    Monterosso, G.R.3    Liu, J.4    Ballou, D.P.5    Hausinger, R.P.6
  • 28
    • 0002379632 scopus 로고
    • Theoretical basis and mechanistic utility of solvent isotope effects
    • (Cook, P. F. Ed.), pp, CRC Press, Boca Raton
    • Quinn, D. M. and Sutton, L. D. (1991) Theoretical Basis and Mechanistic Utility of Solvent Isotope Effects, in Enzyme Mechanism from Isotope Effects (Cook, P. F., Ed.), pp 73-126, CRC Press, Boca Raton.
    • (1991) Enzyme Mechanism from Isotope Effects , pp. 73-126
    • Quinn, D.M.1    Sutton, L.D.2
  • 29
    • 0035954384 scopus 로고    scopus 로고
    • Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1
    • DOI 10.1021/bi002893d
    • Tomchick, D. R., Phan, P., Cymborowski, M., Minor, W., and Holman, T. R. (2001) Structural and functional characterization of second-coordination sphere mutants of soybean lipoxpgenase-1 Biochemistry 40, 7509-7517 (Pubitemid 32578015)
    • (2001) Biochemistry , vol.40 , Issue.25 , pp. 7509-7517
    • Tomchick, D.R.1    Phan, P.2    Cymborowski, M.3    Minor, W.4    Holman, T.R.5
  • 30
    • 0026455197 scopus 로고
    • Mechanistic studies on the human matrix metalloproteinase stromelysin
    • Harrison, R. K., Chang, B., Niedzwiecki, L., and Stein, R. L. (1992) Mechanistic studies on the human matrix metalloproteinase stromelysin Biochemistry 31, 10757-10762
    • (1992) Biochemistry , vol.31 , pp. 10757-10762
    • Harrison, R.K.1    Chang, B.2    Niedzwiecki, L.3    Stein, R.L.4
  • 31
    • 0032555189 scopus 로고    scopus 로고
    • Hydrolysis of N-succinyl-L,L-diaminopimelic acid by the Haemophilus influenzae dapE-encoded desuccinylase: Metal activation, solvent isotope effects, and kinetic mechanism
    • DOI 10.1021/bi9806807
    • Born, T. L., Zheng, R. J., and Blanchard, J. S. (1998) Hydrolysis of N -succinyl- l, l -diaminopimelic acid by the Haemophilus influenzae dapE-encoded desuccinylase: Metal activation, solvent isotope effects, and kinetic mechanism Biochemistry 37, 10478-10487 (Pubitemid 28357571)
    • (1998) Biochemistry , vol.37 , Issue.29 , pp. 10478-10487
    • Born, T.L.1    Zheng, R.2    Blanchard, J.S.3
  • 33
    • 77749286320 scopus 로고    scopus 로고
    • The rate-limiting catalytic steps of hydroxymandelate synthase from Amycolatopsis orientalis
    • He, P. Q., Conrad, J. A., and Moran, G. R. (2010) The rate-limiting catalytic steps of hydroxymandelate synthase from Amycolatopsis orientalis Biochemistry 49, 1998-2007
    • (2010) Biochemistry , vol.49 , pp. 1998-2007
    • He, P.Q.1    Conrad, J.A.2    Moran, G.R.3
  • 34
    • 77956631879 scopus 로고    scopus 로고
    • Evidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygen
    • Flashman, E., Hoffart, L. M., Hamed, R. B., Bollinger, J. M., Krebs, C., and Schofield, C. J. (2010) Evidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygen FEBS J. 277, 4089-4099
    • (2010) FEBS J. , vol.277 , pp. 4089-4099
    • Flashman, E.1    Hoffart, L.M.2    Hamed, R.B.3    Bollinger, J.M.4    Krebs, C.5    Schofield, C.J.6
  • 35
    • 56749180745 scopus 로고    scopus 로고
    • Kinetic characterization and identification of a novel inhibitor of hypoxia-inducible factor prolyl hydroxylase 2 using a time-resolved fluorescence resonance energy transfer-based assay technology
    • Dao, J. H., Kurzeja, R. J. M., Morachis, J. M., Veith, H., Lewis, J., Yu, V., Tegley, C. M., and Tagari, P. (2009) Kinetic characterization and identification of a novel inhibitor of hypoxia-inducible factor prolyl hydroxylase 2 using a time-resolved fluorescence resonance energy transfer-based assay technology Anal. Biochem. 384, 213-223
    • (2009) Anal. Biochem. , vol.384 , pp. 213-223
    • Dao, J.H.1    Kurzeja, R.J.M.2    Morachis, J.M.3    Veith, H.4    Lewis, J.5    Yu, V.6    Tegley, C.M.7    Tagari, P.8
  • 37
    • 84861923067 scopus 로고    scopus 로고
    • Screening chelating inhibitors of HIF-prolyl hydroxylase domain 2 (PHD2) and factor inhibiting HIF (FIH)
    • Flagg, S. C., Martin, C. B., Taabazuing, C. Y., Holmes, B. E., and Knapp, M. J. (2012) Screening chelating inhibitors of HIF-prolyl hydroxylase domain 2 (PHD2) and factor inhibiting HIF (FIH) J. Inorg. Biochem. 113, 25-30
    • (2012) J. Inorg. Biochem. , vol.113 , pp. 25-30
    • Flagg, S.C.1    Martin, C.B.2    Taabazuing, C.Y.3    Holmes, B.E.4    Knapp, M.J.5
  • 38
    • 33846315497 scopus 로고    scopus 로고
    • Studies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assay
    • DOI 10.1042/BJ20061151
    • Ehrismann, D., Flashman, E., Genn, D. N., Mathioudakis, N., Hewitson, K. S., Ratcliffe, P. J., and Schofield, C. J. (2007) Studies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assay Biochem. J. 401, 227-234 (Pubitemid 46114616)
    • (2007) Biochemical Journal , vol.401 , Issue.1 , pp. 227-234
    • Ehrismann, D.1    Flashman, E.2    Genn, D.N.3    Mathioudakis, N.4    Hewitson, K.S.5    Ratcliffe, P.J.6    Schofield, C.J.7
  • 39
    • 84865443139 scopus 로고    scopus 로고
    • (1980-1981) 61 st ed. CRC Press Inc. Boca Raton
    • (1980-1981) CRC Reference Book, 61 st ed., CRC Press Inc., Boca Raton.
    • CRC Reference Book
  • 40
    • 79958050379 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy structural investigation of early intermediates in the mechanism of DNA repair by human ABH2
    • Giri, N. C., Sun, H., Chen, H., Costa, M., and Maroney, M. J. X-ray absorption spectroscopy structural investigation of early intermediates in the mechanism of DNA repair by human ABH2, Biochemistry 50, 5067-5076.
    • Biochemistry , vol.50 , pp. 5067-5076
    • Giri, N.C.1    Sun, H.2    Chen, H.3    Costa, M.4    Maroney, M.J.5
  • 41
    • 0035857403 scopus 로고    scopus 로고
    • Immobilized metal complexes in porous organic hosts: Development of a material for the selective and reversible binding of nitric oxide
    • DOI 10.1021/ja003282b
    • Padden, K. M., Krebs, J. F., MacBeth, C. E., Scarrow, R. C., and Borovik, A. S. (2001) Immobilized metal complexes in porous organic hosts: Development of a material for the selective and reversible binding of nitric oxide J. Am. Chem. Soc. 123, 1072-1079 (Pubitemid 32148174)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.6 , pp. 1072-1079
    • Padden, K.M.1    Krebs, J.F.2    MacBeth, C.E.3    Scarrow, R.C.4    Borovik, A.S.5
  • 42
    • 33747604978 scopus 로고    scopus 로고
    • SIXpack: A graphical user interface for XAS analysis using IFEFFIT
    • DOI 10.1238/Physica.Topical.115a01011, Proceedings of the 12th X-ray Absorption Fine Structure International Conference, XAFS12
    • Webb, S. M. (2005) SIXpack: a graphical user interface for XAS analysis using IFEFFIT Phys. Scr. T115, 1011-1014 (Pubitemid 351525058)
    • (2005) Physica Scripta T , vol.T115 , pp. 1011-1014
    • Webb, S.M.1
  • 44
    • 0017339091 scopus 로고
    • Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies
    • Cleland, W. W. (1977) Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies Adv. Enzymol. 273-387
    • (1977) Adv. Enzymol. , pp. 273-387
    • Cleland, W.W.1
  • 46
    • 0033576280 scopus 로고    scopus 로고
    • Stopped-flow kinetic analysis of Escherichia coli taurine/α- ketoglutarate dioxygenase: Interactions with α-ketoglutarate, taurine, and oxygen
    • Ryle, M. J., Padmakumar, R., and Hausinger, R. P. (1999) Stopped-flow kinetic analysis of Escherichia coli taurine/alpha-ketoglutarate dioxygenase: interactions with alpha-ketoglutarate, taurine, and oxygen Biochemistry 38, 15278-15286 (Pubitemid 129520361)
    • (1999) Biochemistry , vol.38 , Issue.46 , pp. 15278-15286
    • Ryle, M.J.1    Padmakumar, R.2    Hausinger, R.P.3
  • 47
    • 0032583527 scopus 로고    scopus 로고
    • Substrate binding to the α-ketoglutarate-dependent non-heme iron enzyme clavaminate synthase 2: Coupling mechanism of oxidative decarboxylation and hydroxylation [14]
    • DOI 10.1021/ja983534x
    • Zhou, J., Gunsior, M., Bachmann, B. O., Townsend, C. A., and Solomon, E. I. (1998) Substrate binding to the α-ketoglutarate-dependent non-heme iron enzyme clavaminate synthase 2: Coupling mechanism of oxidative decarboxylation and hydroxylation J. Am. Chem. Soc. 120, 13539-13540 (Pubitemid 29025230)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.51 , pp. 13539-13540
    • Zhou, J.1    Gunsior, M.2    Bachmann, B.O.3    Townsend, C.A.4    Solomon, E.I.5
  • 48
    • 84962463451 scopus 로고    scopus 로고
    • a Values of Hydrated Transition Metal Cations by a Combined Density Functional and Continuum Dielectric Theory
    • Li, J., Fisher, C. L., Chen, J. L., Bashford, D., and Noodleman, L. (1996) Calculation of redox potentials and pK(a) values of hydrated transition metal cations by a combined density functional and continuum dielectric theory Inorg. Chem. 35, 4694-4702 (Pubitemid 126452861)
    • (1996) Inorganic Chemistry , vol.35 , Issue.16 , pp. 4694-4702
    • Li, J.1    Fisher, C.L.2    Chen, J.L.3    Bashford, D.4    Noodleman, L.5
  • 49
    • 0028167993 scopus 로고
    • X-ray-absorption studies on catechol 2,3-dioxygenase from pseudomonas-putida Mt2
    • Bertini, I., Briganti, F., Mangani, S., Nolting, H. F., and Scozzafava, A. (1994) X-ray-absorption studies on catechol 2,3-dioxygenase from pseudomonas-putida Mt2 Biochemistry 33, 10777-10784
    • (1994) Biochemistry , vol.33 , pp. 10777-10784
    • Bertini, I.1    Briganti, F.2    Mangani, S.3    Nolting, H.F.4    Scozzafava, A.5
  • 51
    • 0142025560 scopus 로고
    • Structure and dynamics of hydrated ions
    • Ohtaki, H. and Radnai, T. (1993) Structure and dynamics of hydrated ions Chem. Rev. 93, 1157-1204
    • (1993) Chem. Rev. , vol.93 , pp. 1157-1204
    • Ohtaki, H.1    Radnai, T.2
  • 52
    • 58649114732 scopus 로고    scopus 로고
    • Dissection of the stepwise mechanism to beta-lactam formation and elucidation of a rate-determining conformational change in beta-lactam synthetase
    • Townsend, C. A., Raber, M. L., and Freeman, M. F. (2009) Dissection of the stepwise mechanism to beta-lactam formation and elucidation of a rate-determining conformational change in beta-lactam synthetase J. Biol. Chem. 284, 207-217
    • (2009) J. Biol. Chem. , vol.284 , pp. 207-217
    • Townsend, C.A.1    Raber, M.L.2    Freeman, M.F.3
  • 53
    • 0001151833 scopus 로고
    • Inverse solvent isotope effects in the nad-malic enzyme reaction are the result of the viscosity difference between D2o and H2o - Implications for solvent isotope effect studies
    • Karsten, W. E., Lai, C. J., and Cook, P. F. (1995) Inverse solvent isotope effects in the nad-malic enzyme reaction are the result of the viscosity difference between D2o and H2o-Implications for solvent isotope effect studies J. Am. Chem. Soc. 117, 5914-5918
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5914-5918
    • Karsten, W.E.1    Lai, C.J.2    Cook, P.F.3
  • 54
    • 0038747011 scopus 로고    scopus 로고
    • The first direct characterization of a high-valent iron intermediate in the reaction of an α-ketoglutarate-dependent dioxygenase: A high-spin Fe(IV) complex in taurine/α-ketoglutarate dioxygenase (TauD) from Escherichia coli
    • DOI 10.1021/bi030011f
    • Price, J. C., Barr, E. W., Tirupati, B., Bollinger, J. M., Jr., and Krebs, C. (2003) The first direct characterization of a high-valent iron intermediate in the reaction of an alpha-ketoglutarate-dependent dioxygenase: a high-spin FeIV complex in taurine/alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli Biochemistry 42, 7497-7508 (Pubitemid 36740493)
    • (2003) Biochemistry , vol.42 , Issue.24 , pp. 7497-7508
    • Price, J.C.1    Barr, E.W.2    Tirupati, B.3    Bollinger Jr., J.M.4    Krebs, C.5
  • 55
    • 43649098548 scopus 로고    scopus 로고
    • Redox tuning over almost 1 v in a structurally conserved active site: Lessons from Fe-containing superoxide dismutase
    • Miller, A. F. (2008) Redox tuning over almost 1 V in a structurally conserved active site: Lessons from Fe-containing superoxide dismutase Acc. Chem. Res. 41, 501-510
    • (2008) Acc. Chem. Res. , vol.41 , pp. 501-510
    • Miller, A.F.1
  • 56
    • 43649099121 scopus 로고    scopus 로고
    • Spectroscopic and computational investigation of second-sphere contributions to redox tuning in Escherichia coli iron superoxide dismutase
    • Brunold, T. C., Grove, L. E., Xie, J., Yikilmaz, E., and Miller, A. F. (2008) Spectroscopic and computational investigation of second-sphere contributions to redox tuning in Escherichia coli iron superoxide dismutase Inorg. Chem. 47, 3978-3992
    • (2008) Inorg. Chem. , vol.47 , pp. 3978-3992
    • Brunold, T.C.1    Grove, L.E.2    Xie, J.3    Yikilmaz, E.4    Miller, A.F.5
  • 57
    • 0141706648 scopus 로고    scopus 로고
    • Kinetic studies of oxygen reactivity in soybean lipoxygenase-1
    • DOI 10.1021/bi0300884
    • Knapp, M. J. and Klinman, J. P. (2003) Kinetic studies of oxygen reactivity in soybean lipoxygenase-1 Biochemistry 42, 11466-11475 (Pubitemid 37205741)
    • (2003) Biochemistry , vol.42 , Issue.39 , pp. 11466-11475
    • Knapp, M.J.1    Klinman, J.P.2
  • 58
    • 0032501464 scopus 로고    scopus 로고
    • Spectroscopic and functional characterization of a ligand coordination mutant of soybean lipoxygenase-1: First coordination sphere analogue of human 15-lipoxygenase
    • DOI 10.1021/ja982844c
    • Holman, T. R., Zhou, J., and Solomon, E. I. (1998) Spectroscopic and functional characterization of a ligand coordination mutant of soybean lipoxygenase-1: First coordination sphere analogue of human 15-lipoxygenase J. Am. Chem. Soc. 120, 12564-12572 (Pubitemid 29003613)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.48 , pp. 12564-12572
    • Holman, T.R.1    Zhou, J.2    Solomon, E.I.3
  • 60
    • 0019349208 scopus 로고
    • The expression of isotope effects on enzyme-catalyzed reactions
    • Northrop, D. B. (1981) The expression of isotope effects on enzyme-catalyzed reactions Annu. Rev. Biochem. 50, 103-131
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 103-131
    • Northrop, D.B.1
  • 61
    • 27244461847 scopus 로고
    • Effective rate constants and general isotope effect equations for steady-state enzymatic-reactions with multiple isotope-sensitive steps
    • Tian, G. C. (1992) Effective rate constants and general isotope effect equations for steady-state enzymatic-reactions with multiple isotope-sensitive steps Bioorg. Chem. 20, 95-106
    • (1992) Bioorg. Chem. , vol.20 , pp. 95-106
    • Tian, G.C.1
  • 62
    • 0020726823 scopus 로고
    • Solvent isotope effects on the reaction catalyzed by alcohol- dehydrogenase from equine liver
    • Taylor, K. B. (1983) Solvent isotope effects on the reaction catalyzed by alcohol-dehydrogenase from equine liver Biochemistry 22, 1040-1045
    • (1983) Biochemistry , vol.22 , pp. 1040-1045
    • Taylor, K.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.