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Volumn 363, Issue 1829, 2005, Pages 807-828

Oxidation by 2-oxoglutarate oxygenases: Non-haem iron systems in catalysis and signalling

Author keywords

Catalysis; Cupin; Hydroxylation; Hypoxia; Iron; JmjC

Indexed keywords


EID: 20744448379     PISSN: 1364503X     EISSN: None     Source Type: Journal    
DOI: 10.1098/rsta.2004.1540     Document Type: Review
Times cited : (54)

References (82)
  • 1
    • 0037456369 scopus 로고    scopus 로고
    • Human and bacterial oxidative demethylases repair alkylation damage in both RNA and DNA
    • Aas, P. A. et al. 2003 Human and bacterial oxidative demethylases repair alkylation damage in both RNA and DNA. Nature 421, 859-863.
    • (2003) Nature , vol.421 , pp. 859-863
    • Aas, P.A.1
  • 2
    • 0035221419 scopus 로고    scopus 로고
    • The DNA-repair protein AlkB, EGL-9 and leprecan define new families of 2-oxoglutarate and iron-dependent dioxygenases
    • RESEARCH0007.1-0.8
    • Aravind, L. & Koonin, E. V. 2001 The DNA-repair protein AlkB, EGL-9 and leprecan define new families of 2-oxoglutarate and iron-dependent dioxygenases. Genome Biol 2. RESEARCH0007.1-0.8.
    • (2001) Genome Biol , vol.2
    • Aravind, L.1    Koonin, E.V.2
  • 3
    • 0000502480 scopus 로고
    • Isopenicillin-N synthase-mechanistic studies
    • Baldwin, J. E. & Bradley, M. 1990 Isopenicillin-N synthase-mechanistic studies. Chem. Rev. 90, 1079-1088.
    • (1990) Chem. Rev. , vol.90 , pp. 1079-1088
    • Baldwin, J.E.1    Bradley, M.2
  • 5
  • 6
    • 0030903149 scopus 로고    scopus 로고
    • Inactivation of 1-aminocyclopropane-1-carboxylate oxidase involves oxidative modifications
    • Barlow, J. N., Zhang, Z. H., John, P., Baldwin, J. E. & Schofield, C. J. 1997 Inactivation of 1-aminocyclopropane-1-carboxylate oxidase involves oxidative modifications. Biochemistry 36, 3563-3569.
    • (1997) Biochemistry , vol.36 , pp. 3563-3569
    • Barlow, J.N.1    Zhang, Z.H.2    John, P.3    Baldwin, J.E.4    Schofield, C.J.5
  • 7
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick, R. K. & McKnight, S. L. 2001 A conserved family of prolyl-4-hydroxylases that modify HIF. Science 294, 1337-1340.
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 9
    • 1542378704 scopus 로고    scopus 로고
    • Dioxygen activation at mononuclear nonheme iron active sites: Enzymes, models, and intermediates
    • Costas, M., Mehn, M. P., Jensen, M. P. & Que Jr, L. 2004 Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates. Chem. Rev. 104, 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
  • 10
    • 0021774436 scopus 로고
    • Stoichiometry and kinetics of the prolyl 4-hydroxylase partial reaction
    • De Jong, L. & Kemp, A. 1984 Stoichiometry and kinetics of the prolyl 4-hydroxylase partial reaction. Biochim. Biophys. Acta 787, 105-111.
    • (1984) Biochim. Biophys. Acta , vol.787 , pp. 105-111
    • De Jong, L.1    Kemp, A.2
  • 11
    • 0019905709 scopus 로고
    • Prolyl 4-hydroxylase activity in relation to the oxidation state of enzyme-bound iron. The role of ascorbate in peptidyl proline hydroxylation
    • De Jong, L., Albracht, S. P. & Kemp, A. 1982 Prolyl 4-hydroxylase activity in relation to the oxidation state of enzyme-bound iron. The role of ascorbate in peptidyl proline hydroxylation. Biochim. Biophys. Acta 704, 326-332.
    • (1982) Biochim. Biophys. Acta , vol.704 , pp. 326-332
    • De Jong, L.1    Albracht, S.P.2    Kemp, A.3
  • 12
    • 0032752621 scopus 로고    scopus 로고
    • Changes in onion root development induced by the inhibition of peptidylprolyl hydroxylase and influence of the ascorbate system on cell division and elongation
    • De Tullio, M. C., Paciolla, C., Dalla Veechia, F., Rascio, N., D'Emerico, S., De Gara, L., Liso, R. & Arrigoni, O. 1999 Changes in onion root development induced by the inhibition of peptidylprolyl hydroxylase and influence of the ascorbate system on cell division and elongation. Planta 209, 424-434.
    • (1999) Planta , vol.209 , pp. 424-434
    • De Tullio, M.C.1    Paciolla, C.2    Dalla Veechia, F.3    Rascio, N.4    D'Emerico, S.5    De Gara, L.6    Liso, R.7    Arrigoni, O.8
  • 16
    • 17944375360 scopus 로고    scopus 로고
    • C-elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation
    • Epstein, A. C. R. et al. 2001 C-elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107, 43-54.
    • (2001) Cell , vol.107 , pp. 43-54
    • Epstein, A.C.R.1
  • 17
    • 0037068433 scopus 로고    scopus 로고
    • AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli
    • Falnes, P. O., Johansen, R. F. & Seeberg, E. 2002 AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli. Nature 419, 178-182.
    • (2002) Nature , vol.419 , pp. 178-182
    • Falnes, P.O.1    Johansen, R.F.2    Seeberg, E.3
  • 18
    • 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
  • 19
    • 18544386401 scopus 로고    scopus 로고
    • Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor-inhibiting HIF (FIH) and is related to the cupin structural family
    • Hewitson, K. S. et al. 2002 Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor-inhibiting HIF (FIH) and is related to the cupin structural family. J. Biol. Chem. 277, 26 351-26 355.
    • (2002) J. Biol. Chem. , vol.277
    • Hewitson, K.S.1
  • 20
    • 1642286962 scopus 로고    scopus 로고
    • Modulating the hypoxia-inducible factor signalling pathway: Applications from cardiovascular disease to cancer
    • Hewitson, K. S., McNeill, L. A. & Schofield, C. J. 2004 Modulating the hypoxia-inducible factor signalling pathway: applications from cardiovascular disease to cancer. Curr. Pharm. Des. 10, 821-833.
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 821-833
    • Hewitson, K.S.1    McNeill, L.A.2    Schofield, C.J.3
  • 21
    • 0043234538 scopus 로고    scopus 로고
    • Characterisation of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor HIF
    • Hirsila, M., Koivunen, P., Gunzler, V., Kivirikko, K. I. & Myllyharju, J. 2003 Characterisation of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor HIF. J. Biol. Chem. 278, 30 772-30 780.
    • (2003) J. Biol. Chem. , vol.278
    • Hirsila, M.1    Koivunen, P.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 22
    • 0034814309 scopus 로고    scopus 로고
    • Resonance Raman studies of the iron(II)-alpha-keto acid chromophore in model and enzyme complexes
    • Ho, R. Y., Mehn, M. P., Hegg, E. L., Liu, A., Ryle, M. J., Hausinger, R. P. & Que Jr, L. 2001 Resonance Raman studies of the iron(II)-alpha-keto acid chromophore in model and enzyme complexes. J. Am. Chem. Soc. 123, 5022-5029.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5022-5029
    • Ho, R.Y.1    Mehn, M.P.2    Hegg, E.L.3    Liu, A.4    Ryle, M.J.5    Hausinger, R.P.6    Que Jr., L.7
  • 23
    • 0035917313 scopus 로고    scopus 로고
    • 2 sensing
    • 2 sensing. Science 292, 464-468.
    • (2001) Science , vol.292 , pp. 464-468
    • Ivan, M.1
  • 24
    • 0035917808 scopus 로고    scopus 로고
    • 2-regulated prolyl hydroxylation
    • 2-regulated prolyl hydroxylation. Science 292, 468-472.
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1
  • 25
    • 0028899310 scopus 로고
    • Purification and characterization of clavaminate synthase from streptomyces-antibioticus-a multifunctional enzyme of clavam biosynthesis
    • Jane, J. W., Egan, L. A. & Townsend, C. A. 1995 Purification and characterization of clavaminate synthase from streptomyces-antibioticus-a multifunctional enzyme of clavam biosynthesis. J. Biol Chem. 270, 5399-5404.
    • (1995) J. Biol Chem. , vol.270 , pp. 5399-5404
    • Jane, J.W.1    Egan, L.A.2    Townsend, C.A.3
  • 26
    • 0025763437 scopus 로고
    • Enzyme catalysis-not different, just better
    • Knowles, J. R. 1991 Enzyme catalysis-not different, just better. Nature 350, 121-124.
    • (1991) Nature , vol.350 , pp. 121-124
    • Knowles, J.R.1
  • 27
    • 0037446983 scopus 로고    scopus 로고
    • Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells
    • Knowles, H. J., Raval, R. R., Harris, A. L. & Ratcliffe, P. J. 2003 Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells. Cancer Res. 63, 1764-1768.
    • (2003) Cancer Res. , vol.63 , pp. 1764-1768
    • Knowles, H.J.1    Raval, R.R.2    Harris, A.L.3    Ratcliffe, P.J.4
  • 28
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • Lando, D., Peet, D. J., Gorman, J. J., Whelan, D. A., Whitelaw, M. L. & Bruick, R. K. 2002a FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev. 16, 1466-1471.
    • (2002) Genes Dev. , vol.16 , pp. 1466-1471
    • Lando, D.1    Peet, D.J.2    Gorman, J.J.3    Whelan, D.A.4    Whitelaw, M.L.5    Bruick, R.K.6
  • 29
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain: A hypoxic switch
    • Lando, D., Peet, D. J., Whelan, D. A., Gorman, J. J. & Whitelaw, M. L. 2002b Asparagine hydroxylation of the HIF transactivation domain: a hypoxic switch. Science 295, 858-861.
    • (2002) Science , vol.295 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3    Gorman, J.J.4    Whitelaw, M.L.5
  • 31
    • 0034802889 scopus 로고    scopus 로고
    • Alternative reactivity of an alpha-ketoglutarate-dependent iron(II) oxygenase: Enzyme self-hydroxylation
    • Liu, A., Ho, R. Y., Que Jr, L., Ryle, M. J., Phinney, B. S. & Hausinger, R. P. 2001 Alternative reactivity of an alpha-ketoglutarate-dependent iron(II) oxygenase: enzyme self-hydroxylation. J. Am. Chem. Soc. 123, 5126-5127.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5126-5127
    • Liu, A.1    Ho, R.Y.2    Que Jr., L.3    Ryle, M.J.4    Phinney, B.S.5    Hausinger, R.P.6
  • 32
    • 0033574483 scopus 로고    scopus 로고
    • Studies on the active site of deacetoxycephalosporin C synthase
    • Lloyd, M. D. et al. 1999a Studies on the active site of deacetoxycephalosporin C synthase. J. Mol. Biol. 287, 943-960.
    • (1999) J. Mol. Biol. , vol.287 , pp. 943-960
    • Lloyd, M.D.1
  • 33
    • 0033551837 scopus 로고    scopus 로고
    • Product-substrate engineering by bacteria: Studies on clavaminate synthase, a trifunctional dioxygenase
    • Lloyd, M. D. et al. 1999b Product-substrate engineering by bacteria: studies on clavaminate synthase, a trifunctional dioxygenase. Tetrahedron 55, 10 201-10 220.
    • (1999) Tetrahedron , vol.55
    • Lloyd, M.D.1
  • 35
    • 0035903468 scopus 로고    scopus 로고
    • Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation
    • Masson, N., Willam, C., Maxwell, P. H., Pugh, C. W. & Ratcliffe, P. J. 2001 Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation. EMBO J. 20, 5197-5206.
    • (2001) EMBO J. , vol.20 , pp. 5197-5206
    • Masson, N.1    Willam, C.2    Maxwell, P.H.3    Pugh, C.W.4    Ratcliffe, P.J.5
  • 36
    • 0036846033 scopus 로고    scopus 로고
    • Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803
    • McNeill, L. A., Hewitson, K. S., Claridge, T. D., Seibel, J. F., Horsfall, L. E. & Schofield, C. J. 2002a Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803. Biochem. J. 367, 571-575.
    • (2002) Biochem. J. , vol.367 , pp. 571-575
    • McNeill, L.A.1    Hewitson, K.S.2    Claridge, T.D.3    Seibel, J.F.4    Horsfall, L.E.5    Schofield, C.J.6
  • 38
    • 0037774509 scopus 로고    scopus 로고
    • Oxygen activation by nonheme iron(II) complexes: Alpha-keto carboxylate versus carboxylate
    • Mehn, M. P., Fujisawa, K., Hegg, E. L. & Que Jr, L. 2003 Oxygen activation by nonheme iron(II) complexes: alpha-keto carboxylate versus carboxylate. J. Am. Chem. Soc. 125, 7828-7842.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7828-7842
    • Mehn, M.P.1    Fujisawa, K.2    Hegg, E.L.3    Que Jr., L.4
  • 41
    • 0037358282 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylases, the key enzymes of collagen biosynthesis
    • Myllyharju, J. 2003 Prolyl 4-hydroxylases, the key enzymes of collagen biosynthesis. Matrix Biol. 22, 15-24.
    • (2003) Matrix Biol. , vol.22 , pp. 15-24
    • Myllyharju, J.1
  • 42
    • 0035068434 scopus 로고    scopus 로고
    • Collagens and collagen-related diseases
    • Myllyharju, J. & Kivirikko, K. I. 2001 Collagens and collagen-related diseases. Ann. Med. 33, 7-21.
    • (2001) Ann. Med. , vol.33 , pp. 7-21
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 44
    • 0021329173 scopus 로고
    • Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase
    • Myllyla, R., Majamaa, K., Gunzler, V., Hanauskeabel, H. M. & Kivirikko, K. I. 1984 Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase. J. Biol. Chem. 259, 5403-5405.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5403-5405
    • Myllyla, R.1    Majamaa, K.2    Gunzler, V.3    Hanauskeabel, H.M.4    Kivirikko, K.I.5
  • 45
    • 4644366115 scopus 로고    scopus 로고
    • Conformational flexibility of the C terminus with implications for substrate binding and catalysis revealed in a new crystal form of deacetoxycephalosporin C synthase
    • Öster, L. M., Van Scheltinga, A. C., Valegård, K., Hose, A. M., Dubus, A., Hajdu, J. & Andersson, I. 2004 Conformational flexibility of the C terminus with implications for substrate binding and catalysis revealed in a new crystal form of deacetoxycephalosporin C synthase. J. Mol. Biol. 343, 157-171.
    • (2004) J. Mol. Biol. , vol.343 , pp. 157-171
    • Öster, L.M.1    Van Scheltinga, A.C.2    Valegård, K.3    Hose, A.M.4    Dubus, A.5    Hajdu, J.6    Andersson, I.7
  • 46
    • 0033854668 scopus 로고    scopus 로고
    • The iron(II) and 2-oxoacid-dependent dioxygenases and their role in metabolism
    • Prescott, A. G. & Lloyd, M. D. 2000 The iron(II) and 2-oxoacid-dependent dioxygenases and their role in metabolism. Nat. Prod. Rep. 17, 367-383.
    • (2000) Nat. Prod. Rep. , vol.17 , pp. 367-383
    • Prescott, A.G.1    Lloyd, M.D.2
  • 47
    • 0038747011 scopus 로고    scopus 로고
    • 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
    • Price, J. C., Barr, E. W., Tirupati, B., Bollinger Jr, J. M. & 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.
    • (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
  • 48
    • 0942298044 scopus 로고    scopus 로고
    • Direct detection of oxygen intermediates in the non-heme Fe enzyme taurine/alpha-ketoglutarate dioxygenase
    • Proshlyakov, D. A., Henshaw, T. F., Monterosso, G. R., Ryle, M. J. & Hausinger, R. P. 2004 Direct detection of oxygen intermediates in the non-heme Fe enzyme taurine/alpha-ketoglutarate dioxygenase. J. Am. Chem. Soc. 126, 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
  • 49
    • 0025230340 scopus 로고
    • Enzymatic-reaction selectivity by negative catalysis or how do enzymes deal with highly reactive intermediates
    • Retey, J. 1990 Enzymatic-reaction selectivity by negative catalysis or how do enzymes deal with highly reactive intermediates. Angew. Chem. Int. Ed. Engl. 29, 355-361.
    • (1990) Angew. Chem. Int. Ed. Engl. , vol.29 , pp. 355-361
    • Retey, J.1
  • 50
    • 3042770458 scopus 로고    scopus 로고
    • EXAFS spectroscopic evidence for an Fe=O unit in the Fe(IV) intermediate observed during oxygen activation by taurine:alpha-ketoglutarate dioxygenase
    • Riggs-Gelasco, P. J., Price, J. C., Guyer, R. B., Brehm, J. H., Barr, E. W., Bollinger Jr, J. M. & Krebs, C. 2004 EXAFS spectroscopic evidence for an Fe=O unit in the Fe(IV) intermediate observed during oxygen activation by taurine:alpha-ketoglutarate dioxygenase. J. Am. Chem. Soc. 126, 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
  • 52
    • 0030947388 scopus 로고    scopus 로고
    • Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation
    • Roach, P. L., Clifton, I. J., Hensgens, C. M. H., Shibata, N., Schofield, C. J., Hajdu, J. & Baldwin, J. E. 1997 Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation. Nature 387, 827-830.
    • (1997) Nature , vol.387 , pp. 827-830
    • Roach, P.L.1    Clifton, I.J.2    Hensgens, C.M.H.3    Shibata, N.4    Schofield, C.J.5    Hajdu, J.6    Baldwin, J.E.7
  • 54
    • 1542328170 scopus 로고    scopus 로고
    • Mechanistic studies of 1-aminocyclopropane-1-carboxylic acid oxidase: Single turnover reaction
    • Rocklin, A. M., Kato, K., Liu, H. W., Que Jr, L. & Lipscomb, J. D. 2004 Mechanistic studies of 1-aminocyclopropane-1-carboxylic acid oxidase: single turnover reaction. J. Biol. Inorg. Chem. 9, 171-182.
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 171-182
    • Rocklin, A.M.1    Kato, K.2    Liu, H.W.3    Que Jr., L.4    Lipscomb, J.D.5
  • 55
    • 0033576280 scopus 로고    scopus 로고
    • Stopped-flow kinetic analysis of Escherichia coli taurine/alpha-ketoglutarate dioxygenase: Interactions with alpha-ketoglutarate, taurine, and oxygen
    • Ryle, M. J., Padmakumar, R. & Hausinger, R. P. 1999 Stopped-flow kinetic analysis of Escherichia coli taurine/alpha-ketoglutarate dioxygenase: interactions with alpha-ketoglutarate, taurine, and oxygen. Biochemistry 38, 15 278-15 286.
    • (1999) Biochemistry , vol.38
    • Ryle, M.J.1    Padmakumar, R.2    Hausinger, R.P.3
  • 56
    • 0037465344 scopus 로고    scopus 로고
    • 2- and alpha-ketoglutarate-dependent tyrosyl radical formation in TauD, an alpha-keto acid-dependent non-heme iron dioxygenase
    • Ryle, M. J., Liu, A., Muthukumaran, R. B., Ho, R. Y., Koehntop, K. D., McCracken, J., Que Jr, L. & Hausinger, R. P. 2003 02- and alpha-ketoglutarate-dependent tyrosyl radical formation in TauD, an alpha-keto acid-dependent non-heme iron dioxygenase. Biochemistry 42, 1854-1862.
    • (2003) Biochemistry , vol.42 , pp. 1854-1862
    • Ryle, M.J.1    Liu, A.2    Muthukumaran, R.B.3    Ho, R.Y.4    Koehntop, K.D.5    McCracken, J.6    Que Jr., L.7    Hausinger, R.P.8
  • 57
    • 0032478205 scopus 로고    scopus 로고
    • Ascorbic acid-dependent turnover and reactivation of 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase using thiophenoxyacetic acid
    • Saari, R. E. & 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.
    • (1998) Biochemistry , vol.37 , pp. 3035-3042
    • Saari, R.E.1    Hausinger, R.P.2
  • 58
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T. C., Hinks, J. A., Tonks, N. K. & Barford, D. 2003 Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423, 769-773.
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.C.4    Hinks, J.A.5    Tonks, N.K.6    Barford, D.7
  • 60
    • 0032760945 scopus 로고    scopus 로고
    • Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes
    • Schofield, C. J. & Zhang, Z. H. 1999 Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes. Curr. Opin. Struct. Biol. 9, 722-731.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 722-731
    • Schofield, C.J.1    Zhang, Z.H.2
  • 62
    • 0034663989 scopus 로고    scopus 로고
    • HIF-1 and human disease: One highly involved factor
    • Semenza, G. L. 2000 HIF-1 and human disease: one highly involved factor. Genes Dev. 14, 1983-1991.
    • (2000) Genes Dev. , vol.14 , pp. 1983-1991
    • Semenza, G.L.1
  • 63
    • 4043086511 scopus 로고    scopus 로고
    • Biosynthesis of carbapenem antibiotics: New carbapenarn substrates for carbapenem synthase (CarC)
    • Sleeman, M. C., Smith, P., Kellam, B., Chhabra, S. R., Bycroft, B. W. & Schofield, C. J. 2004 Biosynthesis of carbapenem antibiotics: new carbapenarn substrates for carbapenem synthase (CarC). Chembiochem 5, 879-882.
    • (2004) Chembiochem , vol.5 , pp. 879-882
    • Sleeman, M.C.1    Smith, P.2    Kellam, B.3    Chhabra, S.R.4    Bycroft, B.W.5    Schofield, C.J.6
  • 64
    • 0034103729 scopus 로고    scopus 로고
    • Ascorbic acid: Metabolism and functions of a multi-facetted molecule
    • Smirnoff, N. 2000 Ascorbic acid: metabolism and functions of a multi-facetted molecule. Curr. Opin. Plant Biol. 3, 229-235.
    • (2000) Curr. Opin. Plant Biol. , vol.3 , pp. 229-235
    • Smirnoff, N.1
  • 65
    • 0038375539 scopus 로고    scopus 로고
    • Carbapenem biosynthesis: Confirmation of stereochemical assignments and the role of CarC in the ring Stereoinversion process from L-proline
    • Stapon, A., Li, R. F. & Townsend, C. A. 2003a Carbapenem biosynthesis: confirmation of stereochemical assignments and the role of CarC in the ring Stereoinversion process from L-proline. J. Am. Chem. Soc. 125, 8486-8493.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8486-8493
    • Stapon, A.1    Li, R.F.2    Townsend, C.A.3
  • 66
    • 0347625829 scopus 로고    scopus 로고
    • Synthesis of (3S,5R)-carbapenam-3-carboxylic acid and its role in carbapenem biosynthesis and the Stereoinversion problem
    • Stapon, A., Li, R. F. & Townsend, C. A. 2003b Synthesis of (3S,5R)-carbapenam-3-carboxylic acid and its role in carbapenem biosynthesis and the Stereoinversion problem. J. Am. Chem. Soc. 125, 15 746-15 747.
    • (2003) J. Am. Chem. Soc. , vol.125
    • Stapon, A.1    Li, R.F.2    Townsend, C.A.3
  • 67
    • 0036801379 scopus 로고    scopus 로고
    • New reactions in clavulanic acid biosynthesis
    • Townsend, C. A. 2002 New reactions in clavulanic acid biosynthesis. Curr. Opin. Chem. Biol. 6, 583-589.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 583-589
    • Townsend, C.A.1
  • 68
    • 0021716724 scopus 로고
    • Stereochemical investigation of the α-ketoglutarate-dependent 3Prime;-hydroxylation in cephalosporin biosynthesis
    • Townsend, C. A. & Barrabee, E. B. 1984 Stereochemical investigation of the α-ketoglutarate-dependent 3Prime;-hydroxylation in cephalosporin biosynthesis. J. Chem. Soc. Chem. Commun., pp. 1586-1588.
    • (1984) J. Chem. Soc. Chem. Commun. , pp. 1586-1588
    • Townsend, C.A.1    Barrabee, E.B.2
  • 69
    • 0022382829 scopus 로고
    • Stereochemical fate of chiral-methyl valine in the ring expansion of penicillin-N to deacetoxycephalosporin-C
    • Townsend, C. A., Theis, A. B., Neese, A. S., Barrabee, E. B. & Poland, D. 1985 Stereochemical fate of chiral-methyl valine in the ring expansion of penicillin-N to deacetoxycephalosporin-C. J. Am. Chem. Soc. 107, 4760-4767.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 4760-4767
    • Townsend, C.A.1    Theis, A.B.2    Neese, A.S.3    Barrabee, E.B.4    Poland, D.5
  • 70
    • 0037068446 scopus 로고    scopus 로고
    • Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage
    • Trewick, S. C., Henshaw, T. F., Hausinger, R. P., Lindahl, T. & Sedgwick, B. 2002 Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage. Nature 419, 174-178.
    • (2002) Nature , vol.419 , pp. 174-178
    • Trewick, S.C.1    Henshaw, T.F.2    Hausinger, R.P.3    Lindahl, T.4    Sedgwick, B.5
  • 71
    • 0346463040 scopus 로고    scopus 로고
    • Mechanistic studies on three 2-oxoglutarate-dependent oxygenases of flavonoid biosynthesis anthocyanidin synthase, flavonol synthase, and flavanone 3 beta-hydroxylase
    • Turnbull, J. J., Nakajima, J., Welford, R. W. D., Yamazaki, M., Saito, K. & Schofield, C. J. 2004 Mechanistic studies on three 2-oxoglutarate-dependent oxygenases of flavonoid biosynthesis anthocyanidin synthase, flavonol synthase, and flavanone 3 beta-hydroxylase. J. Biol. Chem. 279, 1206-1216.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1206-1216
    • Turnbull, J.J.1    Nakajima, J.2    Welford, R.W.D.3    Yamazaki, M.4    Saito, K.5    Schofield, C.J.6
  • 73
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase IB
    • van Montfort, R. L. M., Congreve, M., Tisi, D., Carr, R. & Jhoti, H. 2003 Oxidation state of the active-site cysteine in protein tyrosine phosphatase IB. Nature 423, 773-777.
    • (2003) Nature , vol.423 , pp. 773-777
    • Van Montfort, R.L.M.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 75
    • 2042540729 scopus 로고    scopus 로고
    • The trinity of life: The genome, the proteome, and the mineral chemical elements
    • Williams, R. J. P. & Da Silva, J. J. R. F. 2004 The trinity of life: the genome, the proteome, and the mineral chemical elements. J. Chem. Educ. 81, 738-749.
    • (2004) J. Chem. Educ. , vol.81 , pp. 738-749
    • Williams, R.J.P.1    Da Silva, J.J.R.F.2
  • 77
  • 78
    • 0037165643 scopus 로고    scopus 로고
    • Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate-substrate-NO complex: Evidence for metal centred rearrangements
    • Zhang, Z. H., Ren, J. S., Harlos, K., McKinnon, C. H., Clifton, I. J. & Schofield, C. J. 2002 Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate-substrate-NO complex: evidence for metal centred rearrangements. FEBS Lett. 517, 7-12.
    • (2002) FEBS Lett. , vol.517 , pp. 7-12
    • Zhang, Z.H.1    Ren, J.S.2    Harlos, K.3    McKinnon, C.H.4    Clifton, I.J.5    Schofield, C.J.6
  • 79
    • 5544323881 scopus 로고    scopus 로고
    • Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase (the ethylene forming enzyme)
    • In press
    • Zhang, Z., Ren, J.-S. Clifton, I. J. & Schofield, D. J. In press Crystal structure and mechanistic implications of 1-Aminocyclopropane-1-carboxylic acid Oxidase (the ethylene forming enzyme) Chem. Biol.
    • Chem. Biol.
    • Zhang, Z.1    Ren, J.-S.2    Clifton, I.J.3    Schofield, D.J.4
  • 80
    • 0032583527 scopus 로고    scopus 로고
    • Substrate binding to the alpha-ketoglutarate-dependent non-heme iron enzyme clavaminate synthase 2: Coupling mechanism of oxidative decarboxylation and hydroxylation
    • Zhou, J., Gunsior, M., Bachmann, B. O., Townsend, C. A. & Solomon, E. I.1998 Substrate binding to the alpha-ketoglutarate-dependent non-heme iron enzyme clavaminate synthase 2: coupling mechanism of oxidative decarboxylation and hydroxylation. J. Am. Chem. Soc. 120, 13 539-13 540.
    • (1998) J. Am. Chem. Soc. , vol.120
    • Zhou, J.1    Gunsior, M.2    Bachmann, B.O.3    Townsend, C.A.4    Solomon, E.I.5
  • 81
    • 0034828607 scopus 로고    scopus 로고
    • Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional alpha-KG-dependent non-heme iron enzyme: Correlation with mechanisms and reactivities
    • Zhou, J., Kelly, W. L., Bachmann, B. O., Gunsior, M., Townsend, C. A. &: 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.
    • (2001) J. Am. Chem. Soc. , vol.123 , 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


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