메뉴 건너뛰기




Volumn 51, Issue 8, 2012, Pages 1607-1616

O2-evolving chlorite dismutase as a tool for studying O 2-utilizing enzymes

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ESCHERICHIA COLI; IRON COMPOUNDS; REACTION INTERMEDIATES;

EID: 84863229878     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201906x     Document Type: Article
Times cited : (35)

References (81)
  • 1
    • 0000021902 scopus 로고    scopus 로고
    • Heme/copper terminal oxidases
    • Ferguson Miller, S. and Babcock, G. T. (1996) Heme/copper terminal oxidases Chem. Rev. 96, 2889-2907
    • (1996) Chem. Rev. , vol.96 , pp. 2889-2907
    • Ferguson Miller, S.1    Babcock, G.T.2
  • 4
    • 2442628211 scopus 로고    scopus 로고
    • Fe(II)/α-ketoglutarate-dependent hydroxylases and related enzymes
    • Hausinger, R. P. (2004) Fe(II)/α-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
  • 5
    • 0015890741 scopus 로고
    • Iron and free radical in ribonucleotide reductase. Exchange of iron and Mössbauer spectroscopy of the protein B2 subunit of the Escherichia coli enzyme
    • Atkin, C. L., Thelander, L., Reichard, P., and Lang, G. (1973) Iron and free radical in ribonucleotide reductase. Exchange of iron and Mössbauer spectroscopy of the protein B2 subunit of the Escherichia coli enzyme J. Biol. Chem. 248, 7464-7472
    • (1973) J. Biol. Chem. , vol.248 , pp. 7464-7472
    • Atkin, C.L.1    Thelander, L.2    Reichard, P.3    Lang, G.4
  • 6
  • 8
    • 0345492036 scopus 로고    scopus 로고
    • Mechanism of aromatic amino acid hydroxylation
    • Fitzpatrick, P. F. (2003) Mechanism of aromatic amino acid hydroxylation Biochemistry 42, 14083-14091
    • (2003) Biochemistry , vol.42 , pp. 14083-14091
    • Fitzpatrick, P.F.1
  • 14
    • 15244339209 scopus 로고    scopus 로고
    • Ferritins: Dynamic management of biological iron and oxygen chemistry
    • Liu, X. F. and Theil, E. C. (2005) Ferritins: Dynamic management of biological iron and oxygen chemistry Acc. Chem. Res. 38, 167-175
    • (2005) Acc. Chem. Res. , vol.38 , pp. 167-175
    • Liu, X.F.1    Theil, E.C.2
  • 15
    • 0037560872 scopus 로고    scopus 로고
    • Mechanistic studies on the hydroxylation of methane by methane monooxygenase
    • Baik, M.-H., Martin, N., Friesner, R. A., and Lippard, S. J. (2003) Mechanistic studies on the hydroxylation of methane by methane monooxygenase Chem. Rev. 103, 2385-2419
    • (2003) Chem. Rev. , vol.103 , pp. 2385-2419
    • Baik, M.-H.1    Martin, N.2    Friesner, R.A.3    Lippard, S.J.4
  • 16
    • 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., and Que, L., Jr. (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
  • 20
    • 1942504122 scopus 로고    scopus 로고
    • Oxygen activation by the noncoupled binuclear copper site in peptidylglycine α-hydroxylating monooxygenase. Reaction mechanism and role of the noncoupled nature of the active site
    • Chen, P. and Solomon, E. I. (2004) Oxygen activation by the noncoupled binuclear copper site in peptidylglycine α-hydroxylating monooxygenase. Reaction mechanism and role of the noncoupled nature of the active site J. Am. Chem. Soc. 126, 4991-5000
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4991-5000
    • Chen, P.1    Solomon, E.I.2
  • 21
    • 33645637817 scopus 로고    scopus 로고
    • The copper-enzyme family of dopamine β-monooxygenase and peptidylglycine α-hydroxylating monooxygenase: Resolving the chemical pathway for substrate hydroxylation
    • Klinman, J. P. (2006) The copper-enzyme family of dopamine β-monooxygenase and peptidylglycine α-hydroxylating monooxygenase: Resolving the chemical pathway for substrate hydroxylation J. Biol. Chem. 281, 3013-3016
    • (2006) J. Biol. Chem. , vol.281 , pp. 3013-3016
    • Klinman, J.P.1
  • 22
    • 0028108347 scopus 로고
    • Activation of molecular oxygen by flavins and flavoproteins
    • Massey, V. (1994) Activation of molecular oxygen by flavins and flavoproteins J. Biol. Chem. 269, 22459-22462
    • (1994) J. Biol. Chem. , vol.269 , pp. 22459-22462
    • Massey, V.1
  • 23
    • 34247534094 scopus 로고    scopus 로고
    • 2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates
    • 2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates Science 316, 453-457
    • (2007) Science , vol.316 , pp. 453-457
    • Kovaleva, E.G.1    Lipscomb, J.D.2
  • 24
    • 54849437492 scopus 로고    scopus 로고
    • Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase
    • Kovaleva, E. G. and Lipscomb, J. D. (2008) Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase Biochemistry 47, 11168-11170
    • (2008) Biochemistry , vol.47 , pp. 11168-11170
    • Kovaleva, E.G.1    Lipscomb, J.D.2
  • 25
    • 0347264753 scopus 로고    scopus 로고
    • Crystal Structure of Naphthalene Dioxygenase: Side-on Binding of Dioxygen to Iron
    • Karlsson, A., Parales, J. V., Parales, R. E., Gibson, D. T., Eklund, H., and Ramaswamy, S. (2003) Crystal Structure of Naphthalene Dioxygenase: Side-on Binding of Dioxygen to Iron Science 299, 1039-1042
    • (2003) Science , vol.299 , pp. 1039-1042
    • Karlsson, A.1    Parales, J.V.2    Parales, R.E.3    Gibson, D.T.4    Eklund, H.5    Ramaswamy, S.6
  • 26
    • 84962449543 scopus 로고    scopus 로고
    • A critical evaluation of DFT, including time-dependent DFT, applied to bioinorganic chemistry
    • Neese, F. (2006) A critical evaluation of DFT, including time-dependent DFT, applied to bioinorganic chemistry J. Biol. Inorg. Chem. 11, 702-711
    • (2006) J. Biol. Inorg. Chem. , vol.11 , pp. 702-711
    • Neese, F.1
  • 27
    • 27844488367 scopus 로고    scopus 로고
    • Active site structure of class I ribonucleotide reductase intermediate X: A density functional theory analysis of structure, energetics, and spectroscopy
    • Han, W. G., Liu, T. Q., Lovell, T., and Noodleman, L. (2005) Active site structure of class I ribonucleotide reductase intermediate X: A density functional theory analysis of structure, energetics, and spectroscopy J. Am. Chem. Soc. 127, 15778-15790
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 15778-15790
    • Han, W.G.1    Liu, T.Q.2    Lovell, T.3    Noodleman, L.4
  • 29
    • 34249098665 scopus 로고    scopus 로고
    • Spectroscopic and computational evaluation of the structure of the high-spin Fe(IV)-oxo intermediates in taurine:α-ketoglutarate dioxygenase from Escherichia coli and its His99Ala ligand variant
    • Sinnecker, S., Svensen, N., Barr, E. W., Ye, S., Bollinger, J. M., Jr., Neese, F., and Krebs, C. (2007) Spectroscopic and computational evaluation of the structure of the high-spin Fe(IV)-oxo intermediates in taurine:α- ketoglutarate dioxygenase from Escherichia coli and its His99Ala ligand variant J. Am. Chem. Soc. 129, 6168-6179
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 6168-6179
    • Sinnecker, S.1    Svensen, N.2    Barr, E.W.3    Ye, S.4    Bollinger Jr., J.M.5    Neese, F.6    Krebs, C.7
  • 31
    • 0034645606 scopus 로고    scopus 로고
    • Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 1. Evidence for a transient tryptophan radical
    • Baldwin, J., Krebs, C., Ley, B. A., Edmondson, D. E., Huynh, B. H., and Bollinger, J. M., Jr. (2000) Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 1. Evidence for a transient tryptophan radical J. Am. Chem. Soc. 122, 12195-12206
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12195-12206
    • Baldwin, J.1    Krebs, C.2    Ley, B.A.3    Edmondson, D.E.4    Huynh, B.H.5    Bollinger Jr., J.M.6
  • 32
    • 20144380031 scopus 로고    scopus 로고
    • Kinetic dissection of the catalytic mechanism of taurine:α- ketoglutarate dioxygenase (TauD) from Escherichia coli
    • Price, J. C., Barr, E. W., Hoffart, L. M., Krebs, C., and Bollinger, J. M., Jr. (2005) Kinetic dissection of the catalytic mechanism of taurine:α-ketoglutarate dioxygenase (TauD) from Escherichia coli Biochemistry 44, 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
  • 33
    • 33645879244 scopus 로고    scopus 로고
    • Stalking intermediates in oxygen activation by iron enzymes: Motivation and method
    • Bollinger, J. M., Jr. and Krebs, C. (2006) Stalking intermediates in oxygen activation by iron enzymes: Motivation and method J. Inorg. Biochem. 100, 586-605
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 586-605
    • Bollinger Jr., J.M.1    Krebs, C.2
  • 34
    • 34547616469 scopus 로고    scopus 로고
    • A manganese(IV)/iron(IV) intermediate in assembly of the manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase
    • Jiang, W., Hoffart, L. M., Krebs, C., and Bollinger, J. M., Jr. (2007) A manganese(IV)/iron(IV) intermediate in assembly of the manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase Biochemistry 46, 8709-8716
    • (2007) Biochemistry , vol.46 , pp. 8709-8716
    • Jiang, W.1    Hoffart, L.M.2    Krebs, C.3    Bollinger Jr., J.M.4
  • 35
    • 0026347398 scopus 로고
    • Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase
    • Bollinger, J. M., Jr., Edmondson, D. E., Huynh, B. H., Filley, J., Norton, J. R., and Stubbe, J. (1991) Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase Science 253, 292-298
    • (1991) Science , vol.253 , pp. 292-298
    • Bollinger Jr., J.M.1    Edmondson, D.E.2    Huynh, B.H.3    Filley, J.4    Norton, J.R.5    Stubbe, J.6
  • 36
    • 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
    • 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 α-ketoglutarate-dependent dioxygenase: A high-spin Fe(IV) complex in taurine/α-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
  • 37
    • 33846379972 scopus 로고    scopus 로고
    • Two interconverting Fe(IV) intermediates in aliphatic chlorination by the halogenase CytC3
    • Galonić, D. P., Barr, E. W., Walsh, C. T., Bollinger, J. M., Jr., and Krebs, C. (2007) Two interconverting Fe(IV) intermediates in aliphatic chlorination by the halogenase CytC3 Nat. Chem. Biol. 3, 113-116
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 113-116
    • Galonić, D.P.1    Barr, E.W.2    Walsh, C.T.3    Bollinger Jr., J.M.4    Krebs, C.5
  • 38
    • 70349736097 scopus 로고    scopus 로고
    • A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus
    • Korboukh, V. K., Li, N., Barr, E. W., Bollinger, J. M., Jr., and Krebs, C. (2009) A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus J. Am. Chem. Soc. 131, 13608-13609
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 13608-13609
    • Korboukh, V.K.1    Li, N.2    Barr, E.W.3    Bollinger Jr., J.M.4    Krebs, C.5
  • 39
    • 65249103153 scopus 로고    scopus 로고
    • Substrate-triggered formation and remarkable stability of the C-H bond-cleaving chloroferryl intermediate in the aliphatic halogenase, SyrB2
    • Matthews, M. L., Krest, C. M., Barr, E. W., Vaillancourt, F. H., Walsh, C. T., Green, M. T., Krebs, C., and Bollinger, J. M., Jr. (2009) Substrate-triggered formation and remarkable stability of the C-H bond-cleaving chloroferryl intermediate in the aliphatic halogenase, SyrB2 Biochemistry 48, 4331-4343
    • (2009) Biochemistry , vol.48 , pp. 4331-4343
    • Matthews, M.L.1    Krest, C.M.2    Barr, E.W.3    Vaillancourt, F.H.4    Walsh, C.T.5    Green, M.T.6    Krebs, C.7    Bollinger Jr., J.M.8
  • 40
    • 78149373621 scopus 로고    scopus 로고
    • Cytochrome P450 compound I: Capture, characterization, and C-H bond activation kinetics
    • Rittle, J. and Green, M. T. (2010) Cytochrome P450 compound I: Capture, characterization, and C-H bond activation kinetics Science 330, 933-937
    • (2010) Science , vol.330 , pp. 933-937
    • Rittle, J.1    Green, M.T.2
  • 42
    • 2442664147 scopus 로고    scopus 로고
    • Use of a chemical trigger for electron transfer to characterize a precursor to cluster X in assembly of the iron-radical cofactor of Escherichia coli ribonucleotide reductase
    • Saleh, L., Krebs, C., Ley, B. A., Naik, S., Huynh, B. H., and Bollinger, J. M., Jr. (2004) Use of a chemical trigger for electron transfer to characterize a precursor to cluster X in assembly of the iron-radical cofactor of Escherichia coli ribonucleotide reductase Biochemistry 43, 5953-5964
    • (2004) Biochemistry , vol.43 , pp. 5953-5964
    • Saleh, L.1    Krebs, C.2    Ley, B.A.3    Naik, S.4    Huynh, B.H.5    Bollinger Jr., J.M.6
  • 45
    • 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
    • Riggs-Gelasco, P. J., Shu, L., Chen, S., Burdi, D., Huynh, B. H., Que, L., Jr., and Stubbe, J. (1998) 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, 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
  • 47
    • 1542377662 scopus 로고    scopus 로고
    • Dioxygen activation in methane monooxygenase: A theoretical study
    • Gherman, B. F., Baik, M.-H., Lippard, S. J., and Friesner, R. A. (2004) Dioxygen activation in methane monooxygenase: A theoretical study J. Am. Chem. Soc. 126, 2978-2990
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2978-2990
    • Gherman, B.F.1    Baik, M.-H.2    Lippard, S.J.3    Friesner, R.A.4
  • 48
    • 0033538303 scopus 로고    scopus 로고
    • 2 diamond core. Implications for the core structures of methane monooxygenase intermediate Q and ribonucleotide reductase intermediate X
    • 2 diamond core. Implications for the core structures of methane monooxygenase intermediate Q and ribonucleotide reductase intermediate X J. Am. Chem. Soc. 121, 5230-5237
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 5230-5237
    • Hsu, H.F.1    Dong, Y.H.2    Shu, L.J.3    Young, V.G.4    Que, L.5
  • 51
    • 43249130246 scopus 로고    scopus 로고
    • Chemical and steady-state kinetic analyses of a heterologously expressed heme dependent chlorite dismutase
    • Streit, B. R. and DuBois, J. L. (2008) Chemical and steady-state kinetic analyses of a heterologously expressed heme dependent chlorite dismutase Biochemistry 47, 5271-5280
    • (2008) Biochemistry , vol.47 , pp. 5271-5280
    • Streit, B.R.1    Dubois, J.L.2
  • 52
    • 3142726522 scopus 로고    scopus 로고
    • Microbial perchlorate reduction: Rocket-fuelled metabolism
    • Coates, J. D. and Achenbach, L. A. (2004) Microbial perchlorate reduction: Rocket-fuelled metabolism Nat. Rev. Microbiol. 2, 569-580
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 569-580
    • Coates, J.D.1    Achenbach, L.A.2
  • 53
    • 77952558152 scopus 로고    scopus 로고
    • How Active-Site Protonation State Influences the Reactivity and Ligation of the Heme in Chlorite Dismutase
    • Streit, B. R., Blanc, B., Lukat-Rodgers, G. S., Rodgers, K. R., and DuBois, J. L. (2010) How Active-Site Protonation State Influences the Reactivity and Ligation of the Heme in Chlorite Dismutase J. Am. Chem. Soc. 132, 5711-5724
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 5711-5724
    • Streit, B.R.1    Blanc, B.2    Lukat-Rodgers, G.S.3    Rodgers, K.R.4    Dubois, J.L.5
  • 54
    • 79953889758 scopus 로고    scopus 로고
    • Chlorite Dismutases, DyPs, and EfeB: 3 Microbial Heme Enzyme Families Comprise the CDE Structural Superfamily
    • Goblirsch, B., Kurker, R. C., Streit, B. R., Wilmot, C. M., and DuBois, J. L. (2011) Chlorite Dismutases, DyPs, and EfeB: 3 Microbial Heme Enzyme Families Comprise the CDE Structural Superfamily J. Mol. Biol. 408, 379-398
    • (2011) J. Mol. Biol. , vol.408 , pp. 379-398
    • Goblirsch, B.1    Kurker, R.C.2    Streit, B.R.3    Wilmot, C.M.4    Dubois, J.L.5
  • 55
    • 33646347856 scopus 로고    scopus 로고
    • Oxygen activation by a mixed-valent, diiron(II/III) cluster in the glycol cleavage reaction catalyzed by myo -inositol oxygenase
    • Xing, G., Barr, E. W., Diao, Y., Hoffart, L. M., Prabhu, K. S., Arner, R. J., Reddy, C. C., Krebs, C., and Bollinger, J. M., Jr. (2006) Oxygen activation by a mixed-valent, diiron(II/III) cluster in the glycol cleavage reaction catalyzed by myo -inositol oxygenase Biochemistry 45, 5402-5412
    • (2006) Biochemistry , vol.45 , pp. 5402-5412
    • Xing, G.1    Barr, E.W.2    Diao, Y.3    Hoffart, L.M.4    Prabhu, K.S.5    Arner, R.J.6    Reddy, C.C.7    Krebs, C.8    Bollinger Jr., J.M.9
  • 57
    • 49749199032 scopus 로고
    • Cleavage of Haem-Protein Link by Acid Methylketone
    • Teal, F. W. (1959) Cleavage of Haem-Protein Link by Acid Methylketone Biochim. Biophys. Acta 35, 543
    • (1959) Biochim. Biophys. Acta , vol.35 , pp. 543
    • Teal, F.W.1
  • 58
    • 0019888169 scopus 로고
    • Apoprotein Formation and Heme Reconstitution of Cytochrome P450cam
    • Wagner, G., Perez, M., Toscano, W. A., and Gunsalus, I. (1981) Apoprotein Formation and Heme Reconstitution of Cytochrome P450cam J. Biol. Chem. 256, 6262-6265
    • (1981) J. Biol. Chem. , vol.256 , pp. 6262-6265
    • Wagner, G.1    Perez, M.2    Toscano, W.A.3    Gunsalus, I.4
  • 59
    • 49649145902 scopus 로고
    • EPR signal intensity and powder shapes: A reexamination
    • Aasa, R. and Vänngård, T. (1975) EPR signal intensity and powder shapes: A reexamination J. Magn. Reson. 19, 308-315
    • (1975) J. Magn. Reson. , vol.19 , pp. 308-315
    • Aasa, R.1    Vänngård, T.2
  • 60
    • 42049105952 scopus 로고    scopus 로고
    • Rapid and quantitative activation of Chlamydia trachomatis ribonucleotide reductase by hydrogen peroxide
    • Jiang, W., Xie, J., Nørgaard, H., Bollinger, J. M., Jr., and Krebs, C. (2008) Rapid and quantitative activation of Chlamydia trachomatis ribonucleotide reductase by hydrogen peroxide Biochemistry 47, 4477-4483
    • (2008) Biochemistry , vol.47 , pp. 4477-4483
    • Jiang, W.1    Xie, J.2    Nørgaard, H.3    Bollinger Jr., J.M.4    Krebs, C.5
  • 61
    • 57049085691 scopus 로고    scopus 로고
    • The manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase: Structure, assembly, radical initiation, and evolution
    • Bollinger, J. M., Jr., Jiang, W., Green, M. T., and Krebs, C. (2008) The manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase: Structure, assembly, radical initiation, and evolution Curr. Opin. Struct. Biol. 18, 650-657
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 650-657
    • Bollinger Jr., J.M.1    Jiang, W.2    Green, M.T.3    Krebs, C.4
  • 62
    • 34250811950 scopus 로고    scopus 로고
    • The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state
    • Jiang, W., Bollinger, J. M., Jr., and Krebs, C. (2007) The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state J. Am. Chem. Soc. 129, 7504-7505
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 7504-7505
    • Jiang, W.1    Bollinger Jr., J.M.2    Krebs, C.3
  • 63
    • 49749105567 scopus 로고    scopus 로고
    • Branched activation- and catalysis-specific pathways for electron relay to the manganese/iron cofactor in ribonucleotide reductase from Chlamydia trachomatis
    • Jiang, W., Saleh, L., Barr, E. W., Xie, J., Gardner, M. M., Krebs, C., and Bollinger, J. M., Jr. (2008) Branched activation- and catalysis-specific pathways for electron relay to the manganese/iron cofactor in ribonucleotide reductase from Chlamydia trachomatis Biochemistry 47, 8477-8484
    • (2008) Biochemistry , vol.47 , pp. 8477-8484
    • Jiang, W.1    Saleh, L.2    Barr, E.W.3    Xie, J.4    Gardner, M.M.5    Krebs, C.6    Bollinger Jr., J.M.7
  • 64
    • 0001175609 scopus 로고
    • Mössbauer spectroscopy of iron porphyrins
    • Debrunner, P. G. (1989) Mössbauer spectroscopy of iron porphyrins Phys. Bioinorg. Chem. Ser. 4, 137-234
    • (1989) Phys. Bioinorg. Chem. Ser. , vol.4 , pp. 137-234
    • Debrunner, P.G.1
  • 66
    • 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)
    • Price, J. C., Barr, E. W., Glass, T. E., Krebs, C., and Bollinger, J. M., Jr. (2003) 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, 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
  • 67
    • 0942298044 scopus 로고    scopus 로고
    • Direct detection of oxygen intermediates in the non-heme Fe enzyme taurine/α-ketoglutarate dioxygenase
    • Proshlyakov, D. A., Henshaw, T. F., Monterosso, G. R., Ryle, M. J., and Hausinger, R. P. (2004) Direct detection of oxygen intermediates in the non-heme Fe enzyme taurine/α-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
  • 68
    • 3042770458 scopus 로고    scopus 로고
    • EXAFS spectroscopic evidence for an Fe = O unit in the Fe(IV) intermediate observed during oxygen activation by taurine:α-ketoglutarate dioxygenase
    • Riggs-Gelasco, P. J., Price, J. C., Guyer, R. B., Brehm, J. H., Barr, E. W., Bollinger, J. M., Jr., and Krebs, C. (2004) EXAFS spectroscopic evidence for an Fe = O unit in the Fe(IV) intermediate observed during oxygen activation by taurine:α-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
  • 69
    • 67749143925 scopus 로고    scopus 로고
    • Indentification of Protonated Oxygenic Ligands of Ribonucleotide Reductase Intermediate X
    • Shanmugam, M., Doan, P. E., Lees, N. S., Stubbe, J., and Hoffman, B. M. (2009) Indentification of Protonated Oxygenic Ligands of Ribonucleotide Reductase Intermediate X J. Am. Chem. Soc. 131, 3370-3376
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 3370-3376
    • Shanmugam, M.1    Doan, P.E.2    Lees, N.S.3    Stubbe, J.4    Hoffman, B.M.5
  • 70
    • 0037396273 scopus 로고    scopus 로고
    • Di-iron-tyrosyl radical ribonucleotide reductases
    • Stubbe, J. (2003) Di-iron-tyrosyl radical ribonucleotide reductases Curr. Opin. Chem. Biol. 7, 183-188
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 183-188
    • Stubbe, J.1
  • 71
    • 0027951575 scopus 로고
    • Mechanism of assembly of the tyrosyl radical-diiron(III) cofactor of E. coli ribonucleotide reductase. 1. Mössbauer characterization of the diferric radical precursor
    • Ravi, N., Bollinger, J. M., Jr., Huynh, B. H., Edmondson, D. E., and Stubbe, J. (1994) Mechanism of assembly of the tyrosyl radical-diiron(III) cofactor of E. coli ribonucleotide reductase. 1. Mössbauer characterization of the diferric radical precursor J. Am. Chem. Soc. 116, 8007-8014
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 8007-8014
    • Ravi, N.1    Bollinger Jr., J.M.2    Huynh, B.H.3    Edmondson, D.E.4    Stubbe, J.5
  • 72
    • 0029740493 scopus 로고    scopus 로고
    • Reconsideration of X, the diiron intermediate formed during cofactor assembly in E. coli ribonucleotide reductase
    • Sturgeon, B. E., Burdi, D., Chen, S., Huynh, B. H., Edmondson, D. E., Stubbe, J., and Hoffman, B. M. (1996) Reconsideration of X, the diiron intermediate formed during cofactor assembly in E. coli ribonucleotide reductase J. Am. Chem. Soc. 118, 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
  • 73
    • 0038208381 scopus 로고    scopus 로고
    • Radical initiation in the class I ribonucleotide reductase: Long-range proton-coupled electron transfer?
    • Stubbe, J., Nocera, D. G., Yee, C. S., and Chang, M. C. Y. (2003) Radical initiation in the class I ribonucleotide reductase: Long-range proton-coupled electron transfer? Chem. Rev. 103, 2167-2202
    • (2003) Chem. Rev. , vol.103 , pp. 2167-2202
    • Stubbe, J.1    Nocera, D.G.2    Yee, C.S.3    Chang, M.C.Y.4
  • 74
    • 34047141801 scopus 로고    scopus 로고
    • Enzymatic C-H activation by metal-superoxo intermediates
    • Bollinger, J. M., Jr. and Krebs, C. (2007) Enzymatic C-H activation by metal-superoxo intermediates Curr. Opin. Chem. Biol. 11, 151-158
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 151-158
    • Bollinger Jr., J.M.1    Krebs, C.2
  • 78
    • 0007003379 scopus 로고
    • Biochemical studies on inositol. IV. Conversion of inositol to glucuronic acid by rat kidney extracts
    • Charalampous, F. C. and Lyras, C. (1957) Biochemical studies on inositol. IV. Conversion of inositol to glucuronic acid by rat kidney extracts J. Biol. Chem. 228, 1-13
    • (1957) J. Biol. Chem. , vol.228 , pp. 1-13
    • Charalampous, F.C.1    Lyras, C.2
  • 80
    • 2342618805 scopus 로고    scopus 로고
    • Microsecond freeze-hyperquenching: Development of a new ultrafast micro-mixing and sampling technology and application to enzyme catalysis
    • Cherepanov, A. V. and de Vries, S. (2004) Microsecond freeze-hyperquenching: development of a new ultrafast micro-mixing and sampling technology and application to enzyme catalysis Biochim. Biophys. Acta 1656, 1-31
    • (2004) Biochim. Biophys. Acta , vol.1656 , pp. 1-31
    • Cherepanov, A.V.1    De Vries, S.2
  • 81
    • 84856718630 scopus 로고    scopus 로고
    • Evidence That the β Subunit of Chlamydia trachomatis Ribonucleotide Reductase Is Active with the Manganese Ion of Its Manganese(IV)/Iron(III) Cofactor in Site 1
    • Dassama, L. M. K., Boal, A. K., Krebs, C., Rosenzweig, A. C., and Bollinger, J. M., Jr. (2012) Evidence That the β Subunit of Chlamydia trachomatis Ribonucleotide Reductase Is Active with the Manganese Ion of Its Manganese(IV)/Iron(III) Cofactor in Site 1 J. Am. Chem. Soc. 134, 2520-2523
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 2520-2523
    • Dassama, L.M.K.1    Boal, A.K.2    Krebs, C.3    Rosenzweig, A.C.4    Bollinger Jr., J.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.