메뉴 건너뛰기




Volumn 338, Issue 1, 2005, Pages 230-239

Post-translational self-hydroxylation: A probe for oxygen activation mechanisms in non-heme iron enzymes

Author keywords

Ketoglutarate dependent enzymes; Non heme iron; Oxygen activation; Post translational modification; Ribonucleotide reductase; Self hydroxylation

Indexed keywords

AROMATIC AMINO ACID; ENZYME; IRON; NONHEME IRON PROTEIN; OXYGEN; RIBONUCLEOTIDE REDUCTASE;

EID: 27544460249     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.191     Document Type: Review
Times cited : (14)

References (65)
  • 2
    • 1542378704 scopus 로고    scopus 로고
    • Dioxygen activation at mononuclear nonheme iron active sites: Enzymes, models, and intermediates
    • M. Costas, M.P. Mehn, M.P. Jensen, and L. Que Jr. Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates Chem. Rev. 104 2004 939 986
    • (2004) Chem. Rev. , vol.104 , pp. 939-986
    • Costas, M.1    Mehn, M.P.2    Jensen, M.P.3    Que Jr., L.4
  • 3
    • 2442628211 scopus 로고    scopus 로고
    • Fe(II)/α-ketoglutarate-dependent hydroxylases and related enzymes
    • R.P. Hausinger Fe(II)/α-ketoglutarate-dependent hydroxylases and related enzymes Crit. Rev. Biochem. Mol. Biol. 39 2004 21 68
    • (2004) Crit. Rev. Biochem. Mol. Biol. , vol.39 , pp. 21-68
    • Hausinger, R.P.1
  • 4
    • 0000239991 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes containing binuclear non-heme iron clusters
    • B.J. Wallar, and J.D. Lipscomb Dioxygen activation by enzymes containing binuclear non-heme iron clusters Chem. Rev. 96 1996 2625 2657
    • (1996) Chem. Rev. , vol.96 , pp. 2625-2657
    • Wallar, B.J.1    Lipscomb, J.D.2
  • 5
    • 0035800409 scopus 로고    scopus 로고
    • Dioxygen activation and methane hydroxylation by soluble methane monooxygenase: A tale of two irons and three proteins
    • M. Merkx, D.A. Kopp, M.H. Sazinsky, J.L. Blazyk, J. Müller, and S.J. Lippard Dioxygen activation and methane hydroxylation by soluble methane monooxygenase: a tale of two irons and three proteins Angew. Chem. Int. Ed. 40 2001 2782 2807
    • (2001) Angew. Chem. Int. Ed. , vol.40 , pp. 2782-2807
    • Merkx, M.1    Kopp, D.A.2    Sazinsky, M.H.3    Blazyk, J.L.4    Müller, J.5    Lippard, S.J.6
  • 7
    • 4644317084 scopus 로고    scopus 로고
    • Hydroperoxoferric heme intermediate as a second electrophilic oxidant in cytochrome P450-catalyzed reactions
    • S. Jin, T.A. Bryson, and J.H. Dawson Hydroperoxoferric heme intermediate as a second electrophilic oxidant in cytochrome P450-catalyzed reactions J. Biol. Inorg. Chem. 9 2004 644 653
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 644-653
    • Jin, S.1    Bryson, T.A.2    Dawson, J.H.3
  • 8
    • 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
    • J.C. Price, E.W. Barr, B. Tirupati, J.M. Bollinger Jr., and C. Krebs 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 Biochemistry 42 2003 7497 7508
    • (2003) Biochemistry , vol.42 , pp. 7497-7508
    • Price, J.C.1    Barr, E.W.2    Tirupati, B.3    Bollinger Jr., J.M.4    Krebs, C.5
  • 9
    • 0942298044 scopus 로고    scopus 로고
    • Direct detection of oxygen intermediates in the non-heme Fe enzyme taurine/α-ketoglutarate dioxygenase
    • D.A. Proshlyakov, T.F. Henshaw, G.R. Monterosso, M.J. Ryle, and R.P. Hausinger Direct detection of oxygen intermediates in the non-heme Fe enzyme taurine/α-ketoglutarate dioxygenase J. Am. Chem. Soc. 126 2004 1022 1023
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1022-1023
    • Proshlyakov, D.A.1    Henshaw, T.F.2    Monterosso, G.R.3    Ryle, M.J.4    Hausinger, R.P.5
  • 10
    • 3042770458 scopus 로고    scopus 로고
    • EXAFS spectroscopic evidence for an FeO unit in the Fe(IV) intermediate observed during oxygen activation by taurine:α-ketoglutarate dioxygenase
    • P.J. Riggs-Gelasco, J.C. Price, R.B. Guyer, J.H. Brehm, E.W. Barr, J.M. Bollinger Jr., and C. Krebs EXAFS spectroscopic evidence for an FeO unit in the Fe(IV) intermediate observed during oxygen activation by taurine:α- ketoglutarate dioxygenase J. Am. Chem. Soc. 126 2004 8108 8109
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8108-8109
    • Riggs-Gelasco, P.J.1    Price, J.C.2    Guyer, R.B.3    Brehm, J.H.4    Barr, E.W.5    Bollinger Jr., J.M.6    Krebs, C.7
  • 11
    • 0142183453 scopus 로고    scopus 로고
    • Evidence for hydrogen abstraction from C1 of taurine by the high-spin Fe(IV) intermediate detected during oxygen activation by taurine:α- ketoglutarate dioxygenase (TauD)
    • J.C. Price, E.W. Barr, T.E. Glass, C. Krebs, and J.M. Bollinger Jr. Evidence for hydrogen abstraction from C1 of taurine by the high-spin Fe(IV) intermediate detected during oxygen activation by taurine:α-ketoglutarate dioxygenase (TauD) J. Am. Chem. Soc. 125 2003 13008 13009
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13008-13009
    • Price, J.C.1    Barr, E.W.2    Glass, T.E.3    Krebs, C.4    Bollinger Jr., J.M.5
  • 12
    • 4644302003 scopus 로고    scopus 로고
    • The oxo/peroxo debate: A nonheme iron perspective
    • L. Que Jr. The oxo/peroxo debate: a nonheme iron perspective J. Biol. Inorg. Chem. 9 2004 684 690
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 684-690
    • Que Jr., L.1
  • 13
    • 0031796531 scopus 로고    scopus 로고
    • Harnessing free radicals: Formation and function of the tyrosyl radical in ribonucleotide reductase
    • J. Stubbe, and P. Riggs-Gelasco Harnessing free radicals: formation and function of the tyrosyl radical in ribonucleotide reductase Trends Biol. Sci. 23 1998 438 443
    • (1998) Trends Biol. Sci. , vol.23 , pp. 438-443
    • Stubbe, J.1    Riggs-Gelasco, P.2
  • 14
    • 17644413773 scopus 로고    scopus 로고
    • The 2-His-1-carboxylate facial triad: A versatile platform for dioxygen activation by mononuclear nonheme iron(II) enzymes
    • K.D. Koehntop, J.P. Emerson, and L. Que Jr. The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear nonheme iron(II) enzymes J. Biol. Inorg. Chem. 10 2005 87 93
    • (2005) J. Biol. Inorg. Chem. , vol.10 , pp. 87-93
    • Koehntop, K.D.1    Emerson, J.P.2    Que Jr., L.3
  • 15
    • 0029740493 scopus 로고    scopus 로고
    • Reconsideration of X, the diiron intermediate formed during cofactor assembly in E. coli ribonucleotide reductase
    • B.E. Sturgeon, D. Burdi, S. Chen, B.-H. Huynh, D.E. Edmondson, J. Stubbe, and B.M. Hoffman Reconsideration of X, the diiron intermediate formed during cofactor assembly in E. coli ribonucleotide reductase J. Am. Chem. Soc. 118 1996 7551 7557
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7551-7557
    • Sturgeon, B.E.1    Burdi, D.2    Chen, S.3    Huynh, B.-H.4    Edmondson, D.E.5    Stubbe, J.6    Hoffman, B.M.7
  • 17
    • 0032506972 scopus 로고    scopus 로고
    • EXAFS characterization of the intermediate X generated during the assembly of the Escherichia coli ribonucleotide reductase R2 diferric tyrosyl radical cofactor
    • P.J. Riggs-Gelasco, L. Shu, S. Chen, D. Burdi, B.H. Huynh, L. Que Jr., and J. Stubbe EXAFS characterization of the intermediate X generated during the assembly of the Escherichia coli ribonucleotide reductase R2 diferric tyrosyl radical cofactor J. Am. Chem. Soc. 120 1998 849 860
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 849-860
    • Riggs-Gelasco, P.J.1    Shu, L.2    Chen, S.3    Burdi, D.4    Huynh, B.H.5    Que Jr., L.6    Stubbe, J.7
  • 18
    • 0017615856 scopus 로고
    • Nature of the free radical in ribonucleotide reductase from Escherichia coli
    • B.-M. Sjöberg, P. Reichard, A. Gräslund, and A. Ehrenberg Nature of the free radical in ribonucleotide reductase from Escherichia coli J. Biol. Chem. 252 1977 536 541
    • (1977) J. Biol. Chem. , vol.252 , pp. 536-541
    • Sjöberg, B.-M.1    Reichard, P.2    Gräslund, A.3    Ehrenberg, A.4
  • 19
    • 0022763898 scopus 로고
    • Identification of the stable free radical tyrosine residue in ribonucleotide reductase
    • A. Larsson, and B.-M. Sjöberg Identification of the stable free radical tyrosine residue in ribonucleotide reductase EMBO J. 5 1986 2037 2040
    • (1986) EMBO J. , vol.5 , pp. 2037-2040
    • Larsson, A.1    Sjöberg, B.-M.2
  • 20
    • 0019182317 scopus 로고
    • On the mechanism of ribonucleoside diphosphate reductase from Escherichia coli. Evidence for 3′-CH bond cleavage
    • J. Stubbe, and D. Ackles On the mechanism of ribonucleoside diphosphate reductase from Escherichia coli. Evidence for 3′-CH bond cleavage J. Biol. Chem. 255 1980 8027 8030
    • (1980) J. Biol. Chem. , vol.255 , pp. 8027-8030
    • Stubbe, J.1    Ackles, D.2
  • 21
    • 0021099682 scopus 로고
    • A substrate radical intermediate in the reaction between ribonucleotide reductase from Escherichia coli and 2′-azido-2′-deoxynucleoside diphosphates
    • B.-M. Sjöberg, A. Gräslund, and F. Eckstein A substrate radical intermediate in the reaction between ribonucleotide reductase from Escherichia coli and 2′-azido-2′-deoxynucleoside diphosphates J. Biol. Chem. 258 1983 8060 8067
    • (1983) J. Biol. Chem. , vol.258 , pp. 8060-8067
    • Sjöberg, B.-M.1    Gräslund, A.2    Eckstein, F.3
  • 22
    • 0027283896 scopus 로고
    • Structure and function of the Escherichia coli ribonucleotide reductase protein R2
    • P. Nordlund, and H. Eklund Structure and function of the Escherichia coli ribonucleotide reductase protein R2 J. Mol. Biol. 232 1993 123 164
    • (1993) J. Mol. Biol. , vol.232 , pp. 123-164
    • Nordlund, P.1    Eklund, H.2
  • 23
    • 0028486194 scopus 로고
    • Structure of ribonucleotide reductase protein R1
    • U. Uhlin, and H. Eklund Structure of ribonucleotide reductase protein R1 Nature 370 1994 533 539
    • (1994) Nature , vol.370 , pp. 533-539
    • Uhlin, U.1    Eklund, H.2
  • 24
    • 0028774182 scopus 로고
    • The ribonucleotide reductase jigsaw puzzle: A large piece falls into place
    • B.-M. Sjöberg The ribonucleotide reductase jigsaw puzzle: a large piece falls into place Structure 2 1994 793 796
    • (1994) Structure , vol.2 , pp. 793-796
    • Sjöberg, B.-M.1
  • 25
    • 0032575296 scopus 로고    scopus 로고
    • Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: Structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins
    • D.T. Logan, F. deMaré, B.O. Persson, A. Slaby, B.-M. Sjöberg, and P. Nordlund Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins Biochemistry 37 1998 10798 10807
    • (1998) Biochemistry , vol.37 , pp. 10798-10807
    • Logan, D.T.1    Demaré, F.2    Persson, B.O.3    Slaby, A.4    Sjöberg, B.-M.5    Nordlund, P.6
  • 26
    • 0028899417 scopus 로고
    • Residues important for radical stability in ribonucleotide reductase from Escherichia coli
    • M. Ormö, K. Regnström, Z. Wang, L. Que Jr., M. Sahlin, and B.-M. Sjöberg Residues important for radical stability in ribonucleotide reductase from Escherichia coli J. Biol. Chem. 270 1995 6570 6576
    • (1995) J. Biol. Chem. , vol.270 , pp. 6570-6576
    • Ormö, M.1    Regnström, K.2    Wang, Z.3    Que Jr., L.4    Sahlin, M.5    Sjöberg, B.-M.6
  • 28
    • 0027424785 scopus 로고
    • Autocatalytic generation of dopa in the engineered protein R2 F208Y from Escherichia coli ribonucleotide reductase and crystal structure of the dopa-208 protein
    • A. Åberg, M. Ormö, P. Nordlund, and B.-M. Sjöberg Autocatalytic generation of dopa in the engineered protein R2 F208Y from Escherichia coli ribonucleotide reductase and crystal structure of the dopa-208 protein Biochemistry 32 1993 9845 9850
    • (1993) Biochemistry , vol.32 , pp. 9845-9850
    • Åberg, A.1    Ormö, M.2    Nordlund, P.3    Sjöberg, B.-M.4
  • 29
    • 0028168338 scopus 로고
    • Dioxygen is the source of the μ-oxo bridge in iron ribonucleotide reductase
    • J. Ling, M. Sahlin, B.-M. Sjöberg, T.M. Loehr, and J. Sanders-Loehr Dioxygen is the source of the μ-oxo bridge in iron ribonucleotide reductase J. Biol. Chem. 269 1994 5595 5601
    • (1994) J. Biol. Chem. , vol.269 , pp. 5595-5601
    • Ling, J.1    Sahlin, M.2    Sjöberg, B.-M.3    Loehr, T.M.4    Sanders-Loehr, J.5
  • 30
    • 0032577245 scopus 로고    scopus 로고
    • New paramagnetic species formed at the expense of the transient tyrosyl radical in mutant protein R2 F208Y of Escherichia coli ribonucleotide reductase
    • A. Liu, M. Sahlin, S. Pötsch, B.-M. Sjöberg, and A. Gräslund New paramagnetic species formed at the expense of the transient tyrosyl radical in mutant protein R2 F208Y of Escherichia coli ribonucleotide reductase Biochem. Biophys. Rec. Commun. 246 1998 740 745
    • (1998) Biochem. Biophys. Rec. Commun. , vol.246 , pp. 740-745
    • Liu, A.1    Sahlin, M.2    Pötsch, S.3    Sjöberg, B.-M.4    Gräslund, A.5
  • 31
    • 0032570317 scopus 로고    scopus 로고
    • Electron injection through a specific pathway determines the outcome of oxygen activation at the diiron cluster in the F208Y mutant of Escherichia coli ribonucleotide reductase protein R2
    • S.E. Parkin, S. Chen, B.A. Ley, L. Mangravite, D.E. Edmondson, B.H. Huynh, and J.M. Bollinger Jr. Electron injection through a specific pathway determines the outcome of oxygen activation at the diiron cluster in the F208Y mutant of Escherichia coli ribonucleotide reductase protein R2 Biochemistry 37 1998 1124 1130
    • (1998) Biochemistry , vol.37 , pp. 1124-1130
    • Parkin, S.E.1    Chen, S.2    Ley, B.A.3    Mangravite, L.4    Edmondson, D.E.5    Huynh, B.H.6    Bollinger Jr., J.M.7
  • 32
    • 0029987181 scopus 로고    scopus 로고
    • Mechanism of assembly of the diferric cluster-tyrosyl radical cofactor of Escherichia coli ribonucleotide reductase from the diferrous form of the R2 subunit
    • W.H. Tong, S. Chen, S.G. Lloyd, D.E. Edmonson, B.H. Huynh, and J. Stubbe Mechanism of assembly of the diferric cluster-tyrosyl radical cofactor of Escherichia coli ribonucleotide reductase from the diferrous form of the R2 subunit J. Am. Chem. Soc. 118 1996 2107 2108
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2107-2108
    • Tong, W.H.1    Chen, S.2    Lloyd, S.G.3    Edmonson, D.E.4    Huynh, B.H.5    Stubbe, J.6
  • 34
    • 0028963767 scopus 로고
    • Evidence by site-directed mutagenesis supports long-range electron transfer in mouse ribonucleotide reductase
    • U. Rova, K. Goodtzova, R. Ingemarson, G. Behravan, A. Gräslund, and L. Thelander Evidence by site-directed mutagenesis supports long-range electron transfer in mouse ribonucleotide reductase Biochemistry 34 1995 4267 4275
    • (1995) Biochemistry , vol.34 , pp. 4267-4275
    • Rova, U.1    Goodtzova, K.2    Ingemarson, R.3    Behravan, G.4    Gräslund, A.5    Thelander, L.6
  • 35
    • 0029812067 scopus 로고    scopus 로고
    • Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase
    • M. Ekberg, M. Sahlin, M. Eriksson, and B.-M. Sjöberg Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase J. Biol. Chem. 271 1996 20655 20659
    • (1996) J. Biol. Chem. , vol.271 , pp. 20655-20659
    • Ekberg, M.1    Sahlin, M.2    Eriksson, M.3    Sjöberg, B.-M.4
  • 37
    • 0242667931 scopus 로고    scopus 로고
    • Structural characterization of the peroxodiiron(III) intermediate generated during oxygen activation by the W48A/D84E variant of ribonucleotide reductase protein R2 from Escherichia coli
    • J. Baldwin, C. Krebs, L. Saleh, M. Stelling, B.H. Huynh, J.M. Bollinger Jr., and P. Riggs-Gelasco Structural characterization of the peroxodiiron(III) intermediate generated during oxygen activation by the W48A/D84E variant of ribonucleotide reductase protein R2 from Escherichia coli Biochemistry 42 2003 13269 13279
    • (2003) Biochemistry , vol.42 , pp. 13269-13279
    • Baldwin, J.1    Krebs, C.2    Saleh, L.3    Stelling, M.4    Huynh, B.H.5    Bollinger Jr., J.M.6    Riggs-Gelasco, P.7
  • 39
    • 0032552729 scopus 로고    scopus 로고
    • 2 activation by non-heme diiron proteins: Identification of a symmetric μ-1,2-peroxide in a mutant of ribonucleotide reductase
    • 2 activation by non-heme diiron proteins: identification of a symmetric μ-1,2-peroxide in a mutant of ribonucleotide reductase Biochemistry 37 1998 14659 14663
    • (1998) Biochemistry , vol.37 , pp. 14659-14663
    • Moënne-Loccoz, P.1    Baldwin, J.2    Ley, B.A.3    Loehr, T.M.4    Bollinger Jr., J.M.5
  • 42
    • 0021329173 scopus 로고
    • Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase
    • R. Myllylä, K. Majamaa, V. Günzler, H.N. Hanauske-Abel, and K.I. Kivirikko Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase J. Biol. Chem. 259 1984 5403 5405
    • (1984) J. Biol. Chem. , vol.259 , pp. 5403-5405
    • Myllylä, R.1    Majamaa, K.2    Günzler, V.3    Hanauske-Abel, H.N.4    Kivirikko, K.I.5
  • 43
    • 0030770813 scopus 로고    scopus 로고
    • Characterization of α-ketoglutarate-dependent taurine dioxygenase from Escherichia coli
    • E. Eichhorn, J.R. van der Ploeg, M.A. Kertesz, and T. Leisinger Characterization of α-ketoglutarate-dependent taurine dioxygenase from Escherichia coli J. Biol. Chem. 272 1997 23031 23036
    • (1997) J. Biol. Chem. , vol.272 , pp. 23031-23036
    • Eichhorn, E.1    Van Der Ploeg, J.R.2    Kertesz, M.A.3    Leisinger, T.4
  • 44
    • 0034814309 scopus 로고    scopus 로고
    • Resonance Raman studies of the iron(II)-α-keto acid chromophore in model and enzyme complexes
    • R.Y.N. Ho, M.P. Mehn, E.L. Hegg, A. Liu, M.J. Ryle, R.P. Hausinger, and L. Que Jr. Resonance Raman studies of the iron(II)-α-keto acid chromophore in model and enzyme complexes J. Am. Chem. Soc. 123 2001 5022 5029
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5022-5029
    • Ho, R.Y.N.1    Mehn, M.P.2    Hegg, E.L.3    Liu, A.4    Ryle, M.J.5    Hausinger, R.P.6    Que Jr., L.7
  • 46
    • 20144380031 scopus 로고    scopus 로고
    • Kinetic dissection of the catalytic mechanism of taurine:α- ketoglutarate dioxygenase (TauD) from Escherichia coli
    • J.C. Price, E.W. Barr, L.M. Hoffart, C. Krebs, and J.M. Bollinger Jr. Kinetic dissection of the catalytic mechanism of taurine:α-ketoglutarate dioxygenase (TauD) from Escherichia coli Biochemistry 44 2005 8138 8147
    • (2005) Biochemistry , vol.44 , pp. 8138-8147
    • Price, J.C.1    Barr, E.W.2    Hoffart, L.M.3    Krebs, C.4    Bollinger Jr., J.M.5
  • 48
    • 0037389772 scopus 로고    scopus 로고
    • Interconversion of two oxidized forms of taurine/α-ketoglutarate dioxygenase, a non-heme iron hydroxylase: Evidence for bicarbonate binding
    • M.J. Ryle, K.D. Koehntop, A. Liu, L. Que Jr., and R.P. Hausinger Interconversion of two oxidized forms of taurine/α-ketoglutarate dioxygenase, a non-heme iron hydroxylase: evidence for bicarbonate binding Proc. Natl. Acad. Sci. USA 100 2003 3790 3795
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3790-3795
    • Ryle, M.J.1    Koehntop, K.D.2    Liu, A.3    Que Jr., L.4    Hausinger, R.P.5
  • 49
    • 0034802889 scopus 로고    scopus 로고
    • Alternative reactivity of an α-ketoglutarate-dependent iron(II) oxygenase: Enzyme self-hydroxylation
    • A. Liu, R.Y.N. Ho, L. Que Jr., M.J. Ryle, B.S. Phinney, and R.P. Hausinger Alternative reactivity of an α-ketoglutarate-dependent iron(II) oxygenase: enzyme self-hydroxylation J. Am. Chem. Soc. 123 2001 5126 5127
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5126-5127
    • Liu, A.1    Ho, R.Y.N.2    Que Jr., L.3    Ryle, M.J.4    Phinney, B.S.5    Hausinger, R.P.6
  • 50
  • 51
    • 0020422576 scopus 로고
    • Blue color, metal content, and substrate binding in 4- hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. Strain P.J. 874
    • S. Lindstedt, and M. Rundgren Blue color, metal content, and substrate binding in 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. Strain P.J. 874 J. Biol. Chem. 257 1982 11922 11931
    • (1982) J. Biol. Chem. , vol.257 , pp. 11922-11931
    • Lindstedt, S.1    Rundgren, M.2
  • 53
    • 0033566995 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: An enzyme involved in the tyrosine degradation pathway
    • L. Serre, A. Sailland, D. Sy, P. Boudec, A. Rolland, E. Pebay-Peyroula, and C. Cohen-Addad Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: an enzyme involved in the tyrosine degradation pathway Structure 7 1999 977 988
    • (1999) Structure , vol.7 , pp. 977-988
    • Serre, L.1    Sailland, A.2    Sy, D.3    Boudec, P.4    Rolland, A.5    Pebay-Peyroula, E.6    Cohen-Addad, C.7
  • 54
    • 0032578427 scopus 로고    scopus 로고
    • Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 Å resolution: Self-hydroxylation of Phe300 and the pterin-binding site
    • K.E. Goodwill, C. Sabatier, and R.C. Stevens Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 Å resolution: self-hydroxylation of Phe300 and the pterin-binding site Biochemistry 37 1998 13437 13445
    • (1998) Biochemistry , vol.37 , pp. 13437-13445
    • Goodwill, K.E.1    Sabatier, C.2    Stevens, R.C.3
  • 55
    • 0033600563 scopus 로고    scopus 로고
    • Phenylalanine residues in the active site of tyrosine hydroxylase: Mutagenesis of Phe300 and Phe309 to alanine and metal ion-catalyzed hydroxylation of Phe 300
    • H.R. Ellis, S.C. Daubner, R.I. McCulloch, and P.F. Fitzpatrick Phenylalanine residues in the active site of tyrosine hydroxylase: mutagenesis of Phe300 and Phe309 to alanine and metal ion-catalyzed hydroxylation of Phe 300 Biochemistry 38 1999 10909 10914
    • (1999) Biochemistry , vol.38 , pp. 10909-10914
    • Ellis, H.R.1    Daubner, S.C.2    McCulloch, R.I.3    Fitzpatrick, P.F.4
  • 56
    • 0034093759 scopus 로고    scopus 로고
    • Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hydroxylase
    • H. Erlandsen, E. Bjørgo, T. Flatmark, and R.C. Stevens Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hydroxylase Biochemistry 39 2000 2208 2217
    • (2000) Biochemistry , vol.39 , pp. 2208-2217
    • Erlandsen, H.1    Bjørgo, E.2    Flatmark, T.3    Stevens, R.C.4
  • 57
    • 0037462093 scopus 로고    scopus 로고
    • Posttranslational hydroxylation of human phenylalanine hydroxylase is a novel example of enzyme self-repair within the second coordination sphere of catalytic iron
    • S.D. Kinzie, M. Thevis, K. Ngo, J. Whitelegge, J.A. Loo, and M.M. Abu-Omar Posttranslational hydroxylation of human phenylalanine hydroxylase is a novel example of enzyme self-repair within the second coordination sphere of catalytic iron J. Am. Chem. Soc. 125 2003 4710 4711
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4710-4711
    • Kinzie, S.D.1    Thevis, M.2    Ngo, K.3    Whitelegge, J.4    Loo, J.A.5    Abu-Omar, M.M.6
  • 58
    • 0031047005 scopus 로고    scopus 로고
    • Identification of an Fe(III)-dihydroxyphenylalanine site in recombinant phosphomannose isomerase from Candida albicans
    • J.J. Smith, A.J. Thomson, A.E. Proudfoot, and T.N. Wells Identification of an Fe(III)-dihydroxyphenylalanine site in recombinant phosphomannose isomerase from Candida albicans Eur. J. Biochem. 244 1997 325 333
    • (1997) Eur. J. Biochem. , vol.244 , pp. 325-333
    • Smith, J.J.1    Thomson, A.J.2    Proudfoot, A.E.3    Wells, T.N.4
  • 60
    • 27144467824 scopus 로고    scopus 로고
    • Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme
    • 10.1038/nature03924
    • L.J. Higgins, F. Yan, P. Liu, H.-W. Liu, and C.L. Drennan Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme Nature 2005 10.1038/nature03924
    • (2005) Nature
    • Higgins, L.J.1    Yan, F.2    Liu, P.3    Liu, H.-W.4    Drennan, C.L.5
  • 61
    • 4143091496 scopus 로고    scopus 로고
    • Oxygenase activity in the self-hydroxylation of (S)-2- hydroxypropylphosphonic acid epoxidase involved in fosfomycin biosynthesis
    • P. Liu, M.P. Mehn, F. Yan, Z. Zhao, L. Que Jr., and H.-W. Liu Oxygenase activity in the self-hydroxylation of (S)-2-hydroxypropylphosphonic acid epoxidase involved in fosfomycin biosynthesis J. Am. Chem. Soc. 126 2004 10306 10312
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 10306-10312
    • Liu, P.1    Mehn, M.P.2    Yan, F.3    Zhao, Z.4    Que Jr., L.5    Liu, H.-W.6
  • 62
    • 4644268354 scopus 로고    scopus 로고
    • One oxidant, many pathways: A theoretical perspective of monooxygenation mechanisms by cytochrome P450 enzymes
    • S. Shaik, S.P. de Visser, and D. Kumar One oxidant, many pathways: a theoretical perspective of monooxygenation mechanisms by cytochrome P450 enzymes J. Biol. Inorg. Chem. 9 2004 661 668
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 661-668
    • Shaik, S.1    De Visser, S.P.2    Kumar, D.3
  • 63
    • 0020488069 scopus 로고
    • A stereochemical concept for the catalytic mechanism of prolyl hydroxylase. Applicability to classification and design of inhibitors
    • H.M. Hanauske-Abel, and V. Günzler A stereochemical concept for the catalytic mechanism of prolyl hydroxylase. Applicability to classification and design of inhibitors J. Theor. Biol. 94 1982 421 455
    • (1982) J. Theor. Biol. , vol.94 , pp. 421-455
    • Hanauske-Abel, H.M.1    Günzler, V.2
  • 64
    • 19744365629 scopus 로고    scopus 로고
    • Reactions of the peroxo intermediate of soluble methane monooxygenase hydroxylase with ethers
    • L.G. Beauvais, and S.J. Lippard Reactions of the peroxo intermediate of soluble methane monooxygenase hydroxylase with ethers J. Am. Chem. Soc. 127 2005 7370 7378
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 7370-7378
    • Beauvais, L.G.1    Lippard, S.J.2
  • 65
    • 0030903149 scopus 로고    scopus 로고
    • Inactivation of 1-aminocyclopropane-1-carboxylate oxidase involves oxidative modifications
    • J.N. Barlow, Z. Zhang, P. John, J.E. Baldwin, and C.J. Schofield Inactivation of 1-aminocyclopropane-1-carboxylate oxidase involves oxidative modifications Biochemistry 36 1997 3563 3569
    • (1997) Biochemistry , vol.36 , pp. 3563-3569
    • Barlow, J.N.1    Zhang, Z.2    John, P.3    Baldwin, J.E.4    Schofield, C.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.