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1
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0032039677
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Oxygen activating nonheme iron enzymes
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Lange S.J., Que L. Jr. Oxygen activating nonheme iron enzymes. Curr. Opin. Chem. Biol. 2:1998;159-172.
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(1998)
Curr. Opin. Chem. Biol.
, vol.2
, pp. 159-172
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Lange, S.J.1
Que, L.Jr.2
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2
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0032760945
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Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes
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Schofield C.J., Zhang Z. Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes. Curr. Opin. Struct. Biol. 9:1999;722-731.
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Curr. Opin. Struct. Biol.
, vol.9
, pp. 722-731
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Schofield, C.J.1
Zhang, Z.2
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7
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0343986411
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One motif, many different reactions
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Que L. Jr. One motif, many different reactions. Nat. Struct. Biol. 7:2000;182-184.
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(2000)
Nat. Struct. Biol.
, vol.7
, pp. 182-184
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Que, L.Jr.1
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8
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0000208617
-
Geometric and electronic structure/function correlations in non-heme iron enzymes
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Solomon E.I., Brunold T.C., Davis M.I., Kemsley J.N., Lee S.-K., Lehnert N., Neese F., Skulan A.J., Yang Y.-S., Zhou J. Geometric and electronic structure/function correlations in non-heme iron enzymes. Chem. Rev. 100:2000;235-350.
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Chem. Rev.
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, pp. 235-350
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Solomon, E.I.1
Brunold, T.C.2
Davis, M.I.3
Kemsley, J.N.4
Lee, S.-K.5
Lehnert, N.6
Neese, F.7
Skulan, A.J.8
Yang, Y.-S.9
Zhou, J.10
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9
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0038747011
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The first characterization of a high-valent iron intermediate in the reaction of an alpha-ketoglutarate-dependent dioxygenase
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This paper reports the first experimental observation of an iron(IV) intermediate in the catalytic cycle of a mononuclear nonheme enzyme
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Price J.C., Barr E.W., Tirupati B., Bollinger J.M. Jr., Krebs C. The first characterization of a high-valent iron intermediate in the reaction of an alpha-ketoglutarate-dependent dioxygenase. Biochemistry. 42:2003;7497-7508 This paper reports the first experimental observation of an iron(IV) intermediate in the catalytic cycle of a mononuclear nonheme enzyme.
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(2003)
Biochemistry
, vol.42
, pp. 7497-7508
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Price, J.C.1
Barr, E.W.2
Tirupati, B.3
Bollinger Jr., J.M.4
Krebs, C.5
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10
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-
0037045257
-
C-H bond activation by a ferric methoxide complex: Modeling the rate-determining step in the mechanism of lipoxygenase
-
An alkoxo iron(III) complex resembling the active form of mammalian lipoxygenases is shown to abstract an H atom from hydrocarbons possessing weak C-H bonds, thus modeling the C-H bond activation step in the proposed mechanism of the enzymes
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Goldsmith C.R., Jonas R.T., Stack T.D.P. C-H bond activation by a ferric methoxide complex: modeling the rate-determining step in the mechanism of lipoxygenase. J. Am. Chem. Soc. 124:2002;83-96 An alkoxo iron(III) complex resembling the active form of mammalian lipoxygenases is shown to abstract an H atom from hydrocarbons possessing weak C-H bonds, thus modeling the C-H bond activation step in the proposed mechanism of the enzymes.
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(2002)
J. Am. Chem. Soc.
, vol.124
, pp. 83-96
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Goldsmith, C.R.1
Jonas, R.T.2
Stack, T.D.P.3
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11
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0033854668
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The iron(II) and 2-oxoacid-dependent dioxygenases and their role in metabolism
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Prescott A.G., Lloyd M.D. The iron(II) and 2-oxoacid-dependent dioxygenases and their role in metabolism. Nat. Prod. Rep. 17:2000;367-383.
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Nat. Prod. Rep.
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, pp. 367-383
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Prescott, A.G.1
Lloyd, M.D.2
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12
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0032852842
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Tetrahydropterin-dependent amino acid hydroxylases
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Fitzpatrick P.F. Tetrahydropterin-dependent amino acid hydroxylases. Annu. Rev. Biochem. 68:1999;355-381.
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Annu. Rev. Biochem.
, vol.68
, pp. 355-381
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Fitzpatrick, P.F.1
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13
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0037774509
-
Oxygen activation by nonheme iron(II) complexes: Alpha-keto carboxylate versus carboxylate
-
This paper investigates the key role the α-keto carboxylate cofactor plays in oxygen activation by mononuclear nonheme iron enzymes with a series of synthetic iron(II) complexes containing α-keto carboxylate or carboxylate ligands. Both types of complexes react with molecular oxygen to hydroxylate a ligand phenyl ring, but the α-keto carboxylate complexes react two orders of magnitude faster than the corresponding carboxylate complexes
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Mehn M.P., Fujisawa K., Hegg E.L., Que L. Jr. Oxygen activation by nonheme iron(II) complexes: alpha-keto carboxylate versus carboxylate. J. Am. Chem. Soc. 125:2003;7828-7842 This paper investigates the key role the α-keto carboxylate cofactor plays in oxygen activation by mononuclear nonheme iron enzymes with a series of synthetic iron(II) complexes containing α-keto carboxylate or carboxylate ligands. Both types of complexes react with molecular oxygen to hydroxylate a ligand phenyl ring, but the α-keto carboxylate complexes react two orders of magnitude faster than the corresponding carboxylate complexes.
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(2003)
J. Am. Chem. Soc.
, vol.125
, pp. 7828-7842
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Mehn, M.P.1
Fujisawa, K.2
Hegg, E.L.3
Que Jr., L.4
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14
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0037467108
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IV=O oxidant
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III-OOR intermediate is proposed to undergo homolytic O-O bond cleavage to afford an oxoiron(IV) species as an unobserved reactive intermediate, which hydroxylates the ortho position of a pendant aryl substituent on the supporting ligand
-
III-OOR intermediate is proposed to undergo homolytic O-O bond cleavage to afford an oxoiron(IV) species as an unobserved reactive intermediate, which hydroxylates the ortho position of a pendant aryl substituent on the supporting ligand.
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(2003)
J. Am. Chem. Soc.
, vol.125
, pp. 2113-2128
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Jensen, M.P.1
Lange, S.J.2
Mehn, M.P.3
Que, E.L.4
Que, L.Jr.5
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15
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0034029015
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Aromatic hydrocarbon dioxygenases in environmental biotechnology
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Gibson D.T., Parales R.E. Aromatic hydrocarbon dioxygenases in environmental biotechnology. Curr. Opin. Biotechnol. 11:2000;236-243.
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(2000)
Curr. Opin. Biotechnol.
, vol.11
, pp. 236-243
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Gibson, D.T.1
Parales, R.E.2
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16
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0037181365
-
III-OOH coin
-
V=O oxidant. Catalysts that give rise to high-spin intermediates favor diol formation via an undetermined mechanism
-
V=O oxidant. Catalysts that give rise to high-spin intermediates favor diol formation via an undetermined mechanism.
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(2002)
J. Am. Chem. Soc.
, vol.124
, pp. 3026-3035
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-
Chen, K.1
Costas, M.2
Kim, J.3
Tipton, A.K.4
Que, L.Jr.5
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18
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0042021461
-
2: Electrophilic versus nucleophilic mechanisms
-
III-OOH intermediate formed during catalysis is reported. Catalysts that give rise to low-spin species oxidize via an electrophilic mechanism, while catalysts that give rise to high-spin species oxidize via a nucleophilic mechanism
-
III-OOH intermediate formed during catalysis is reported. Catalysts that give rise to low-spin species oxidize via an electrophilic mechanism, while catalysts that give rise to high-spin species oxidize via a nucleophilic mechanism.
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(2003)
J. Am. Chem. Soc.
, vol.125
, pp. 9912-9913
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Fujita, M.1
Costas, M.2
Que, L.Jr.3
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20
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0141742706
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Simple iron catalyst for terminal alkene epoxidation
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Dubois G., Murphy A., Stack T.D.P. Simple iron catalyst for terminal alkene epoxidation. Org. Lett. 5:2003;2469-2472.
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(2003)
Org. Lett.
, vol.5
, pp. 2469-2472
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Dubois, G.1
Murphy, A.2
Stack, T.D.P.3
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22
-
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0034804120
-
Modeling Rieske dioxygenases: The first example of iron-catalyzed asymmetric cis-dihydroxylation of olefins
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This is the first instance of an iron complex that is capable of oxidizing olefins enantioselectively to cis-diols
-
Costas M., Tipton A.K., Chen K., Jo D.-H., Que L. Jr. Modeling Rieske dioxygenases: the first example of iron-catalyzed asymmetric cis-dihydroxylation of olefins. J. Am. Chem. Soc. 123:2001;6722-6723 This is the first instance of an iron complex that is capable of oxidizing olefins enantioselectively to cis-diols.
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(2001)
J. Am. Chem. Soc.
, vol.123
, pp. 6722-6723
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Costas, M.1
Tipton, A.K.2
Chen, K.3
Jo, D.-H.4
Que, L.Jr.5
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23
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0037414293
-
2+-catalyzed heterolytic RO-OH bond cleavage and substrate oxidation: A functional synthetic nonheme iron monooxygenase system
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A diiron(II) complex is shown to catalyze heterolytic O-O bond cleavage of 2-methyl-1-phenyl-2-propyl-hydroperoxide yielding 2-methyl-1-phenyl-propan-2- ol and an oxidant capable of efficient oxidation of cyclohexane and thioanisole. In contrast, the corresponding diiron(III) complex yields products from homolytic cleavage
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2+-catalyzed heterolytic RO-OH bond cleavage and substrate oxidation: a functional synthetic nonheme iron monooxygenase system. J. Am. Chem. Soc. 125:2003;3678-3679 A diiron(II) complex is shown to catalyze heterolytic O-O bond cleavage of 2-methyl-1-phenyl-2- propyl-hydroperoxide yielding 2-methyl-1-phenyl-propan-2-ol and an oxidant capable of efficient oxidation of cyclohexane and thioanisole. In contrast, the corresponding diiron(III) complex yields products from homolytic cleavage.
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(2003)
J. Am. Chem. Soc.
, vol.125
, pp. 3678-3679
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Foster, T.L.1
Caradonna, J.P.2
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24
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11544259897
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Cleavage of nucleic acids by bleomycin
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Burger R.M. Cleavage of nucleic acids by bleomycin. Chem. Rev. 98:1998;1153-1169.
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(1998)
Chem. Rev.
, vol.98
, pp. 1153-1169
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Burger, R.M.1
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25
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0037042234
-
Identification of iron(III) peroxo species in the active site of the superoxide reductase SOR from Desulfoarculus baarsii
-
2 that can be characterized by resonance Raman spectroscopy. An O-O vibration was identified in this experiment, representing the first direct evidence for an iron-peroxo species in this family of enzymes
-
2 that can be characterized by resonance Raman spectroscopy. An O-O vibration was identified in this experiment, representing the first direct evidence for an iron-peroxo species in this family of enzymes.
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(2002)
J. Am. Chem. Soc.
, vol.124
, pp. 4966-4967
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-
Mathé, C.1
Mattioli, T.A.2
Horner, O.3
Lombard, M.4
Latour, J.-M.5
Fontecave, M.6
Nivière, V.7
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26
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0347264753
-
Crystal structure of naphthalene dioxygenase: Side-on binding of dioxygen to iron
-
This paper reports the first crystal structures of a nonheme iron enzyme with dioxygen bound to the iron center in a side-on fashion
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Karlsson A., Parales J.V., Parales R.E., Gibson D.T., Eklund H., Ramaswamy S. Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron. Science. 299:2003;1039-1042 This paper reports the first crystal structures of a nonheme iron enzyme with dioxygen bound to the iron center in a side-on fashion.
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(2003)
Science
, vol.299
, pp. 1039-1042
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Karlsson, A.1
Parales, J.V.2
Parales, R.E.3
Gibson, D.T.4
Eklund, H.5
Ramaswamy, S.6
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27
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0000920237
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Characterization and properties of nonheme iron peroxo complexes
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Girerd J.-J., Banse F., Simaan A.J. Characterization and properties of nonheme iron peroxo complexes. Struct. Bonding. 97:2000;145-177.
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(2000)
Struct. Bonding
, vol.97
, pp. 145-177
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Girerd, J.-J.1
Banse, F.2
Simaan, A.J.3
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29
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0037425168
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2
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2. Inorg. Chem. 42:2003;2470-2477.
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(2003)
Inorg. Chem.
, vol.42
, pp. 2470-2477
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Balland, V.1
Banse, F.2
Anxolabéhère-Mallart, E.3
Ghiladi, M.4
Mattioli, T.A.5
Philouze, C.6
Blondin, G.7
Girerd, J.-J.8
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30
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0041870990
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Iron complexes containing the ligand N,N′-bis(6-methyl-2- pyridylmethyl)-N,N′-bis(2-pyridylmethyl)ethane-1,2-diamine: Structural, spectroscopic, and electrochemical studies, reactivity with hydrogen peroxide and the formation of a low-spin Fe-OOH complex
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Balland V., Banse F., Anxolabéhère-Mallart E., Nierlich M., Girerd J.-J. Iron complexes containing the ligand N,N′-bis(6-methyl-2- pyridylmethyl)-N,N′-bis(2-pyridylmethyl)ethane-1,2-diamine: structural, spectroscopic, and electrochemical studies, reactivity with hydrogen peroxide and the formation of a low-spin Fe-OOH complex. Eur. J. Inorg. Chem. 13:2003;2529-2535.
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(2003)
Eur. J. Inorg. Chem.
, vol.13
, pp. 2529-2535
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Balland, V.1
Banse, F.2
Anxolabéhère-Mallart, E.3
Nierlich, M.4
Girerd, J.-J.5
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32
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0037063569
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Electronic structure and reactivity of low-spin Fe(III)-hydroperoxo complexes: Comparison to activated bleomycin
-
III-OOH complexes with neutral N5 ligands shows a strong π-interaction between the iron and peroxide in such systems, which weakens the O-O bond.This interaction is not present in activated bleomycin due to the presence of the amidate ligand, resulting in different spectroscopic properties and reactivity
-
III-OOH complexes with neutral N5 ligands shows a strong π-interaction between the iron and peroxide in such systems, which weakens the O-O bond.This interaction is not present in activated bleomycin due to the presence of the amidate ligand, resulting in different spectroscopic properties and reactivity.
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(2002)
J. Am. Chem. Soc.
, vol.124
, pp. 10810-10822
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Lehnert, N.1
Neese, F.2
Ho, R.Y.N.3
Que, L.Jr.4
Solomon, E.I.5
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33
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0346245904
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End-on and side-on peroxo derivatives of nonheme iron complexes with pentadentate ligands: Models for putative intermediates in biological iron/dioxygen chemistry
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2) intermediates in the N4Py ligand system. EXAFS studies provide the first metrical parameters for the iron coordination spheres in such peroxo complexes
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2) intermediates in the N4Py ligand system. EXAFS studies provide the first metrical parameters for the iron coordination spheres in such peroxo complexes.
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(2003)
Inorg. Chem.
, vol.42
, pp. 2639-2653
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Roelfes, G.1
Vrajmasu, V.2
Chen, K.3
Ho, R.Y.N.4
Rohde, J.-U.5
Zondervan, C.6
La Crois, R.M.7
Schudde, E.P.8
Lutz, M.9
Spek, A.L.10
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34
-
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0037010036
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III-OOH intermediate
-
- ligand is characterized as a model for a key intermediate in the catalytic cycle of superoxide reductase
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- ligand is characterized as a model for a key intermediate in the catalytic cycle of superoxide reductase.
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(2002)
J. Am. Chem. Soc.
, vol.124
, pp. 11709-11717
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Shearer, J.1
Scarrow, R.C.2
Kovacs, J.A.3
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36
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0035904991
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The electronic structure of nonheme iron(III)-hydroperoxo and iron(III)-peroxo complexes studied by Mössbauer and electron paramagnetic resonance spectroscopies
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Simaan A.J., Banse F., Girerd J.-J., Wieghardt K., Bill E. The electronic structure of nonheme iron(III)-hydroperoxo and iron(III)-peroxo complexes studied by Mössbauer and electron paramagnetic resonance spectroscopies. Inorg. Chem. 40:2001;6538-6540.
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Inorg. Chem.
, vol.40
, pp. 6538-6540
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Simaan, A.J.1
Banse, F.2
Girerd, J.-J.3
Wieghardt, K.4
Bill, E.5
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37
-
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0036906613
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+, studied by Mössbauer spectroscopy-implications for the electronic structures of peroxo model complexes
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+, studied by Mössbauer spectroscopy-implications for the electronic structures of peroxo model complexes. Eur. J. Inorg. Chem. 12:2002;3278-3283.
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(2002)
Eur. J. Inorg. Chem.
, vol.12
, pp. 3278-3283
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Horner, O.1
Jeandey, C.2
Oddou, J.-L.3
Bonville, P.4
Mckenzie, C.J.5
Latour, J.-M.6
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38
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0036007785
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Mononuclear nonheme iron(III) peroxide complexes: Syntheses, characterization, mass spectrometric and kinetic studies
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Hazell A, McKenzie CJ, Nielsen LP, Schindler S, Weitzer M: Mononuclear nonheme iron(III) peroxide complexes: syntheses, characterization, mass spectrometric and kinetic studies. J Chem Soc, Dalton Trans 2002:310-317.
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(2002)
J Chem Soc, Dalton Trans
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Hazell, A.1
McKenzie, C.J.2
Nielsen, L.P.3
Schindler, S.4
Weitzer, M.5
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39
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0032539185
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3-: Electronic structure of the side-on ferric-peroxide bond and its relevance to reactivity
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3-: electronic structure of the side-on ferric-peroxide bond and its relevance to reactivity. J. Am. Chem. Soc. 120:1998;12829-12848.
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, vol.120
, pp. 12829-12848
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Neese, F.1
Solomon, E.I.2
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40
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0037467719
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Electronic structure and reactivity of high-spin iron-alkyl and -pterinperoxo complexes
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Lehnert N., Fujisawa K., Solomon E.I. Electronic structure and reactivity of high-spin iron-alkyl and -pterinperoxo complexes. Inorg. Chem. 42:2003;469-481.
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(2003)
Inorg. Chem.
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Lehnert, N.1
Fujisawa, K.2
Solomon, E.I.3
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41
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0035956535
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Electronic structure of high-spin iron(III)-alkylperoxo complexes and its relation to low-spin analogues: Reaction coordinate of O-O bond homolysis
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Lehnert N., Ho R.Y.N., Que L. Jr., Solomon E.I. Electronic structure of high-spin iron(III)-alkylperoxo complexes and its relation to low-spin analogues: reaction coordinate of O-O bond homolysis. J. Am. Chem. Soc. 123:2001;12802-12816.
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J. Am. Chem. Soc.
, vol.123
, pp. 12802-12816
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Lehnert, N.1
Ho, R.Y.N.2
Que, L.Jr.3
Solomon, E.I.4
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42
-
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0037169656
-
Reactivity of hydroperoxide bound to a mononuclear nonheme iron site
-
III-OOH intermediate is isolated and characterized. Its reactivity towards substrates suggests that the bound peroxide has nucleophilic character
-
III-OOH intermediate is isolated and characterized. Its reactivity towards substrates suggests that the bound peroxide has nucleophilic character.
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(2002)
Inorg. Chem.
, vol.41
, pp. 616-618
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Wada, A.1
Ogo, S.2
Nagatomo, S.3
Kitagawa, T.4
Watanabe, Y.5
Jitsukawa, K.6
Masuda, H.7
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43
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0037006848
-
A new mononuclear iron(III) complex containing a peroxocarbonate ligand
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2. It is the first synthetic mononuclear iron-peroxo complex to be crystallographically characterized
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2. It is the first synthetic mononuclear iron-peroxo complex to be crystallographically characterized.
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(2002)
Angew. Chem. Int. Ed. Engl.
, vol.41
, pp. 1202-1204
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Hashimoto, K.1
Nagatomo, S.2
Fujinami, S.3
Furutachi, H.4
Ogo, S.5
Suzuki, M.6
Uehara, A.7
Maeda, Y.8
Watanabe, Y.9
Kitagawa, T.10
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44
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0034731019
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Electronic structure of activated bleomycin: Oxygen intermediates in heme versus nonheme iron
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Neese F., Zaleski J.M., Loeb-Zaleski K., Solomon E.I. Electronic structure of activated bleomycin: oxygen intermediates in heme versus nonheme iron. J. Am. Chem. Soc. 122:2000;11703-11724.
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J. Am. Chem. Soc.
, vol.122
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Neese, F.1
Zaleski, J.M.2
Loeb-Zaleski, K.3
Solomon, E.I.4
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45
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0000239991
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Dioxygen activation by enzymes containing binuclear nonheme iron clusters
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Wallar B.J., Lipscomb J.D. Dioxygen activation by enzymes containing binuclear nonheme iron clusters. Chem. Rev. 96:1996;2625-2657.
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, pp. 2625-2657
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Wallar, B.J.1
Lipscomb, J.D.2
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46
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0039302669
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Dioxygen activation by enzymes with mononuclear nonheme iron active sites
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Que L. Jr., Ho R.Y.N. Dioxygen activation by enzymes with mononuclear nonheme iron active sites. Chem. Rev. 96:1996;2607-2624.
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(1996)
Chem. Rev.
, vol.96
, pp. 2607-2624
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Que, L.Jr.1
Ho, R.Y.N.2
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47
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0037436143
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IV=O complex
-
-1 reflect increased Fe-O π bonding
-
-1 reflect increased Fe-O π bonding.
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(2003)
Science
, vol.299
, pp. 1037-1039
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Rohde, J.-U.1
In, J.-H.2
Lim, M.H.3
Brennessel, W.W.4
Bukowski, M.R.5
Stubna, A.6
Münck, E.7
Nam, W.8
Que, L.Jr.9
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48
-
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0012900781
-
IV=O complex of a tetradentate tripodal nonheme ligand
-
IV=O intermediate that is supported by a tetradentate tripodal ligand
-
IV=O intermediate that is supported by a tetradentate tripodal ligand.
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(2003)
Proc. Natl. Acad. Sci. U.S.A.
, vol.100
, pp. 3665-3670
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Lim, M.H.1
Rohde, J.-U.2
Stubna, A.3
Bukowski, M.R.4
Costas, M.5
Ho, R.Y.N.6
Münck, E.7
Nam, W.8
Que, L.Jr.9
|