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Mechanistic aspects of dihydroxybenzoate dioxygenases
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Lipscomb J.D., and Orville A.M. Mechanistic aspects of dihydroxybenzoate dioxygenases. Met Ions Biol Syst 28 (1992) 243-298
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Lipscomb, J.D.1
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Versatility of biological non-heme Fe(II) centers in oxygen activation reactions
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Kovaleva E.G., and Lipscomb J.D. Versatility of biological non-heme Fe(II) centers in oxygen activation reactions. Nat Chem Biol 4 (2008) 186-193
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X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanism
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Shu L., Chiou Y.M., Orville A.M., Miller M.A., Lipscomb J.D., and Que Jr. L. X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanism. Biochemistry 34 (1995) 6649-6659
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Shu, L.1
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Que Jr., L.6
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6
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0028835678
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Mechanism of extradiol catechol dioxygenases: evidence for a lactone intermediate in the 2,3-dihydroxyphenylpropionate 1,2-dioxygenase reaction
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Sanvoisin J., Langley G.J., and Bugg T.D.H. Mechanism of extradiol catechol dioxygenases: evidence for a lactone intermediate in the 2,3-dihydroxyphenylpropionate 1,2-dioxygenase reaction. J Am Chem Soc 117 (1995) 7836-7837
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Sanvoisin, J.1
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Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102
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Senda T., Sugiyama K., Narita H., Yamamoto T., Kimbara K., Fukuda M., Sato M., Yano K., and Mitsui Y. Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102. J Mol Biol 255 (1996) 735-752
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Sato, M.7
Yano, K.8
Mitsui, Y.9
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8
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0028862027
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Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad
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Han S., Eltis L.D., Timmis K.N., Muchmore S.W., and Bolin J.T. Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science 270 (1995) 976-980
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Han, S.1
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17644413773
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The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes
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Koehntop K.D., Emerson J.P., and Que Jr. L. The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes. J Biol Inorg Chem 10 (2005) 87-93
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Koehntop, K.D.1
Emerson, J.P.2
Que Jr., L.3
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10
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Crystal structures of the reaction intermediate and its homologue of an extradiol-cleaving catecholic dioxygenase
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2 surrogate, this shows that the reaction substrates bind in adjacent sites of the iron, a key element of the proposed mechanism. Insight into the role of the key histidine acid/base catalyst in the active site was also provided.
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2 surrogate, this shows that the reaction substrates bind in adjacent sites of the iron, a key element of the proposed mechanism. Insight into the role of the key histidine acid/base catalyst in the active site was also provided.
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(2002)
J Mol Biol
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Sato, N.1
Uragami, Y.2
Nishizaki, T.3
Takahashi, Y.4
Sazaki, G.5
Sugimoto, K.6
Nonaka, T.7
Masai, E.8
Fukuda, M.9
Senda, T.10
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11
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1642264726
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Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases
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Vetting M.W., Wackett L.P., Que Jr. L., Lipscomb J.D., and Ohlendorf D.H. Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases. J Bacteriol 186 (2004) 1945-1958
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J Bacteriol
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Vetting, M.W.1
Wackett, L.P.2
Que Jr., L.3
Lipscomb, J.D.4
Ohlendorf, D.H.5
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12
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0037139492
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Definitive evidence for monoanionic binding of 2,3-dihydroxybiphenyl to 2,3-dihydroxybiphenyl 1,2-dioxygenase from UV resonance Raman spectroscopy, UV/vis absorption spectroscopy, and crystallography
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The authors use a new approach to directly demonstrate that the aromatic substrate binds to the Fe(II) of an extradiol dioxygenase as a monoanion. This differentiates the substrate binding mode from that found for intradiol dioxygenases (dianion) and suggests a source for the proton needed to promote O-O bond cleavage and the crucial Criegee rearrangement.
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Vaillancourt F.H., Barbosa C.J., Spiro T.G., Bolin J.T., Blades M.W., Turner R.F.B., and Eltis L.D. Definitive evidence for monoanionic binding of 2,3-dihydroxybiphenyl to 2,3-dihydroxybiphenyl 1,2-dioxygenase from UV resonance Raman spectroscopy, UV/vis absorption spectroscopy, and crystallography. J Am Chem Soc 124 (2002) 2485-2496. The authors use a new approach to directly demonstrate that the aromatic substrate binds to the Fe(II) of an extradiol dioxygenase as a monoanion. This differentiates the substrate binding mode from that found for intradiol dioxygenases (dianion) and suggests a source for the proton needed to promote O-O bond cleavage and the crucial Criegee rearrangement.
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J Am Chem Soc
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Vaillancourt, F.H.1
Barbosa, C.J.2
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Bolin, J.T.4
Blades, M.W.5
Turner, R.F.B.6
Eltis, L.D.7
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13
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Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase
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Groce S.L., Miller-Rodeberg M.A., and Lipscomb J.D. Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase. Biochemistry 43 (2004) 15141-15153
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Biochemistry
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Groce, S.L.1
Miller-Rodeberg, M.A.2
Lipscomb, J.D.3
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14
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27544492782
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Single-turnover kinetics of 2,3-dihydroxybiphenyl 1,2-dioxygenase reacting with 3-formylcatechol
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Ishida T., Senda T., Tanaka H., Yamamoto A., and Horiike K. Single-turnover kinetics of 2,3-dihydroxybiphenyl 1,2-dioxygenase reacting with 3-formylcatechol. Biochem Biophys Res Commun 338 (2005) 223-229
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Senda, T.2
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Yamamoto, A.4
Horiike, K.5
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15
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3242811958
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Mechanism for catechol ring-cleavage by non-heme iron extradiol dioxygenases
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••]) and predicted that the Criegee rearrangement chemistry occurs in a stepwise rather than the traditional concerted fashion.
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••]) and predicted that the Criegee rearrangement chemistry occurs in a stepwise rather than the traditional concerted fashion.
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Siegbahn, P.E.M.1
Haeffner, F.2
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A comparison of the reaction mechanisms of iron and manganese-containing 2,3-HPCD: an important spin transition for manganese
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Georgiev V., Borowski T., Blomberg M.R.A., and Siegbahn P.E.M. A comparison of the reaction mechanisms of iron and manganese-containing 2,3-HPCD: an important spin transition for manganese. J Biol Inorg Chem 13 (2008) 929-940
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Georgiev V., Borowski T., and Siegbahn P.E.M. Theoretical study of the catalytic reaction mechanism of MndD. J Biol Inorg Chem 11 (2006) 571-585
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Borowski, T.2
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6344291632
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Acid-base catalysis in the extradiol catechol dioxygenase reaction mechanism: site-directed mutagenesis of His-115 and His-179 in Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB)
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Mendel S., Arndt A., and Bugg T.D.H. Acid-base catalysis in the extradiol catechol dioxygenase reaction mechanism: site-directed mutagenesis of His-115 and His-179 in Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB). Biochemistry 43 (2004) 13390-13396
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Mendel, S.1
Arndt, A.2
Bugg, T.D.H.3
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20
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18544362332
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Aromatic ring cleavage by homoprotocatechuate 2,3-dioxygenase: role of His200 in the kinetics of interconversion of reaction cycle intermediates
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Here the chromophoric substrate analog and active site mutagenesis were used to reveal eight intermediates of the extradiol reaction cycle including a spectroscopically characterized oxy intermediate. The role of His200 as the active site acid is strongly supported.
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Groce S.L., and Lipscomb J.D. Aromatic ring cleavage by homoprotocatechuate 2,3-dioxygenase: role of His200 in the kinetics of interconversion of reaction cycle intermediates. Biochemistry 44 (2005) 7175-7188. Here the chromophoric substrate analog and active site mutagenesis were used to reveal eight intermediates of the extradiol reaction cycle including a spectroscopically characterized oxy intermediate. The role of His200 as the active site acid is strongly supported.
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Biochemistry
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Groce, S.L.1
Lipscomb, J.D.2
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21
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27744516150
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The role of histidine 200 in MndD, the Mn(II)-dependent 3,4-dihydroxyphenylacetate 2,3-dioxygenase from Arthrobacter globiformis CM-2, a site-directed mutagenesis study
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Emerson J.P., Wagner M.L., Reynolds M.F., Que Jr. L., Sadowsky M.J., and Wackett L.P. The role of histidine 200 in MndD, the Mn(II)-dependent 3,4-dihydroxyphenylacetate 2,3-dioxygenase from Arthrobacter globiformis CM-2, a site-directed mutagenesis study. J Biol Inorg Chem 10 (2005) 751-760
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Emerson, J.P.1
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Que Jr., L.4
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Wackett, L.P.6
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23
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34247534094
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2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates
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Here three intermediates of the extradiol dioxygenase catalytic cycle were trapped in a single crystal and structurally characterized for the first time.
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2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates. Science 316 (2007) 453-457. Here three intermediates of the extradiol dioxygenase catalytic cycle were trapped in a single crystal and structurally characterized for the first time.
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Science
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Kovaleva, E.G.1
Lipscomb, J.D.2
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25
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0347264753
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Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron
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Karlsson A., Parales J.V., Parales R.E., Gibson D.T., Eklund H., and Ramaswamy S. Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron. Science 299 (2003) 1039-1042
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Karlsson, A.1
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26
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Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates
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Costas M., Mehn M.P., Jensen M.P., and Que Jr. L. Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates. Chem Rev 104 (2004) 939-986
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Chem Rev
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Costas, M.1
Mehn, M.P.2
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Que Jr., L.4
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27
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0034813032
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Extradiol oxidative cleavage of catechols by ferrous and ferric complexes of 1,4,7-triazacyclononane: insight into the mechanism of the extradiol catechol dioxygenases
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The authors use biomimetic chemistry to show the requirement for a proton and the favorable application of Fe(II) in extradiol cleavage mechanisms.
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Lin G., Reid G., and Bugg T.D.H. Extradiol oxidative cleavage of catechols by ferrous and ferric complexes of 1,4,7-triazacyclononane: insight into the mechanism of the extradiol catechol dioxygenases. J Am Chem Soc 123 (2001) 5030-5039. The authors use biomimetic chemistry to show the requirement for a proton and the favorable application of Fe(II) in extradiol cleavage mechanisms.
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J Am Chem Soc
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Lin, G.1
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Bugg T.D.H. Dioxygenase enzymes: catalytic mechanisms and chemical models. Tetrahedron 59 (2003) 7075-7101
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Bugg T.D.H., and Ramaswamy S. Non-heme iron-dependent dioxygenases: unravelling catalytic mechanisms for complex enzymatic oxidations. Curr Opin Chem Biol 12 (2008) 134-140
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Evidence from mechanistic probes for distinct hydroperoxide rearrangement mechanisms in the intradiol and extradiol catechol dioxygenases
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Xin M., and Bugg T.D.H. Evidence from mechanistic probes for distinct hydroperoxide rearrangement mechanisms in the intradiol and extradiol catechol dioxygenases. J Am Chem Soc 130 (2008) 10422-10430
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Conversion of extradiol aromatic ring-cleaving homoprotocatechuate 2,3-dioxygenase into an intradiol cleaving enzyme
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Groce S.L., and Lipscomb J.D. Conversion of extradiol aromatic ring-cleaving homoprotocatechuate 2,3-dioxygenase into an intradiol cleaving enzyme. J Am Chem Soc 125 (2003) 11780-11781
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Groce, S.L.1
Lipscomb, J.D.2
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Directed evolution of a non-heme-iron-dependent extradiol catechol dioxygenase: identification of mutants with intradiol oxidative cleavage activity
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Schlosrich J., Eley K.L., Crowley P.J., and Bugg T.D.H. Directed evolution of a non-heme-iron-dependent extradiol catechol dioxygenase: identification of mutants with intradiol oxidative cleavage activity. Chembiochem 7 (2006) 1899-1908
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Schlosrich, J.1
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Swapping metals in Fe- and Mn-dependent dioxygenases: evidence for oxygen activation without a change in metal redox state
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Here it was shown that the reaction rate through the O-O bond cleavage step is the same for Fe(II) or Mn(II) in the active site. This provides the first evidence in support of the mechanistic hypothesis that the metal does not change oxidation state at key steps in the oxygen activation and insertion process. This is a unique property of the extradiol dioxygenases.
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Emerson J.P., Kovaleva E.G., Farquhar E.R., Lipscomb J.D., and Que Jr. L. Swapping metals in Fe- and Mn-dependent dioxygenases: evidence for oxygen activation without a change in metal redox state. Proc Natl Acad Sci U S A 105 (2008) 7347-7352. Here it was shown that the reaction rate through the O-O bond cleavage step is the same for Fe(II) or Mn(II) in the active site. This provides the first evidence in support of the mechanistic hypothesis that the metal does not change oxidation state at key steps in the oxygen activation and insertion process. This is a unique property of the extradiol dioxygenases.
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Proc Natl Acad Sci U S A
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Emerson, J.P.1
Kovaleva, E.G.2
Farquhar, E.R.3
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Que Jr., L.5
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34
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Intermediate in the O-O Bond Cleavage Reaction of an Extradiol Dioxygenase
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Kovaleva E.G., and Lipscomb JD. Intermediate in the O-O Bond Cleavage Reaction of an Extradiol Dioxygenase. Biochemistry 47 (2008) 11168-11170
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Kovaleva, E.G.1
Lipscomb JD2
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35
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38349108723
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The mechanism for isopenicillin N synthase from density-functional modeling highlights the similarities with other enzymes in the 2-His-1-carboxylate family
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Lundberg M., Siegbahn P.E.M., and Morokuma K. The mechanism for isopenicillin N synthase from density-functional modeling highlights the similarities with other enzymes in the 2-His-1-carboxylate family. Biochemistry 47 (2008) 1031-1042
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Lundberg, M.1
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Interactions of isopenicillin N synthase with cyclopropyl-containing substrate analogues reveal new mechanistic insight
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Howard-Jones A.R., Elkins J.M., Clifton I.J., Roach P.L., Adlington R.M., Baldwin J.E., and Rutledge P.J. Interactions of isopenicillin N synthase with cyclopropyl-containing substrate analogues reveal new mechanistic insight. Biochemistry 46 (2007) 4755-4762
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Biochemistry
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Howard-Jones, A.R.1
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38
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33947700818
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Radical intermediates in monooxygenase reactions of Rieske dioxygenases
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Chakrabarty S., Austin R.N., Deng D., Groves J.T., and Lipscomb J.D. Radical intermediates in monooxygenase reactions of Rieske dioxygenases. J Am Chem Soc 129 (2007) 3514-3515
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Chakrabarty, S.1
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Lipscomb, J.D.5
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39
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34447326187
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Hydrogen peroxide dependent cis-dihydroxylation of benzoate by fully oxidized benzoate 1,2-dioxygenase
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Neibergall M.B., Stubna A., Mekmouche Y., Münck E., and Lipscomb J.D. Hydrogen peroxide dependent cis-dihydroxylation of benzoate by fully oxidized benzoate 1,2-dioxygenase. Biochemistry 46 (2007) 8004-8016
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Neibergall, M.B.1
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40
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34249098665
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Spectroscopic and computational evaluation of the structure of the high-spin Fe(IV)-oxo intermediates in taurine: alpha -ketoglutarate dioxygenase from Escherichia coli and its His99Ala ligand variant
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Sinnecker S., Svensen N., Barr E.W., Ye S., Bollinger Jr. J.M., Neese F., and Krebs C. Spectroscopic and computational evaluation of the structure of the high-spin Fe(IV)-oxo intermediates in taurine: alpha -ketoglutarate dioxygenase from Escherichia coli and its His99Ala ligand variant. J Am Chem Soc 129 (2007) 6168-6179
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Krebs, C.7
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35048831968
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Direct spectroscopic evidence for a high-spin Fe(IV) intermediate in tyrosine hydroxylase
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Eser B.E., Barr E.W., Frantom P.A., Saleh L., Bollinger Jr. J.M., Krebs C., and Fitzpatrick P.F. Direct spectroscopic evidence for a high-spin Fe(IV) intermediate in tyrosine hydroxylase. J Am Chem Soc 129 (2007) 11334-11335
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