메뉴 건너뛰기




Volumn 7, Issue 6, 2003, Pages 674-682

Functional models for mononuclear nonheme iron enzymes

Author keywords

[No Author keywords available]

Indexed keywords

IRON; METAL; NONHEME IRON PROTEIN; OXYGEN;

EID: 0344896568     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2003.10.008     Document Type: Review
Times cited : (34)

References (52)
  • 1
    • 0032039677 scopus 로고    scopus 로고
    • Oxygen activating nonheme iron enzymes
    • Lange S.J., Que L. Jr. Oxygen activating nonheme iron enzymes. Curr. Opin. Chem. Biol. 2:1998;159-172.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 159-172
    • Lange, S.J.1    Que, L.Jr.2
  • 2
    • 0032760945 scopus 로고    scopus 로고
    • Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes
    • 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.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 722-731
    • Schofield, C.J.1    Zhang, Z.2
  • 7
    • 0343986411 scopus 로고    scopus 로고
    • One motif, many different reactions
    • Que L. Jr. One motif, many different reactions. Nat. Struct. Biol. 7:2000;182-184.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 182-184
    • Que, L.Jr.1
  • 9
    • 0038747011 scopus 로고    scopus 로고
    • The first characterization of a high-valent iron intermediate in the reaction of an alpha-ketoglutarate-dependent dioxygenase
    • This paper reports the first experimental observation of an iron(IV) intermediate in the catalytic cycle of a mononuclear nonheme enzyme
    • 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.
    • (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
  • 10
    • 0037045257 scopus 로고    scopus 로고
    • 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
    • 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.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 83-96
    • Goldsmith, C.R.1    Jonas, R.T.2    Stack, T.D.P.3
  • 11
    • 0033854668 scopus 로고    scopus 로고
    • The iron(II) and 2-oxoacid-dependent dioxygenases and their role in metabolism
    • 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.
    • (2000) Nat. Prod. Rep. , vol.17 , pp. 367-383
    • Prescott, A.G.1    Lloyd, M.D.2
  • 12
    • 0032852842 scopus 로고    scopus 로고
    • Tetrahydropterin-dependent amino acid hydroxylases
    • Fitzpatrick P.F. Tetrahydropterin-dependent amino acid hydroxylases. Annu. Rev. Biochem. 68:1999;355-381.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 355-381
    • Fitzpatrick, P.F.1
  • 13
    • 0037774509 scopus 로고    scopus 로고
    • 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
    • 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.
    • (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
  • 14
    • 0037467108 scopus 로고    scopus 로고
    • IV=O oxidant
    • 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.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2113-2128
    • Jensen, M.P.1    Lange, S.J.2    Mehn, M.P.3    Que, E.L.4    Que, L.Jr.5
  • 15
    • 0034029015 scopus 로고    scopus 로고
    • Aromatic hydrocarbon dioxygenases in environmental biotechnology
    • Gibson D.T., Parales R.E. Aromatic hydrocarbon dioxygenases in environmental biotechnology. Curr. Opin. Biotechnol. 11:2000;236-243.
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 236-243
    • Gibson, D.T.1    Parales, R.E.2
  • 16
    • 0037181365 scopus 로고    scopus 로고
    • 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.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3026-3035
    • Chen, K.1    Costas, M.2    Kim, J.3    Tipton, A.K.4    Que, L.Jr.5
  • 18
    • 0042021461 scopus 로고    scopus 로고
    • 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.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9912-9913
    • Fujita, M.1    Costas, M.2    Que, L.Jr.3
  • 20
    • 0141742706 scopus 로고    scopus 로고
    • Simple iron catalyst for terminal alkene epoxidation
    • Dubois G., Murphy A., Stack T.D.P. Simple iron catalyst for terminal alkene epoxidation. Org. Lett. 5:2003;2469-2472.
    • (2003) Org. Lett. , vol.5 , pp. 2469-2472
    • Dubois, G.1    Murphy, A.2    Stack, T.D.P.3
  • 22
    • 0034804120 scopus 로고    scopus 로고
    • Modeling Rieske dioxygenases: The first example of iron-catalyzed asymmetric cis-dihydroxylation of olefins
    • 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.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6722-6723
    • Costas, M.1    Tipton, A.K.2    Chen, K.3    Jo, D.-H.4    Que, L.Jr.5
  • 23
    • 0037414293 scopus 로고    scopus 로고
    • 2+-catalyzed heterolytic RO-OH bond cleavage and substrate oxidation: A functional synthetic nonheme iron monooxygenase system
    • 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
    • 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.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3678-3679
    • Foster, T.L.1    Caradonna, J.P.2
  • 24
    • 11544259897 scopus 로고    scopus 로고
    • Cleavage of nucleic acids by bleomycin
    • Burger R.M. Cleavage of nucleic acids by bleomycin. Chem. Rev. 98:1998;1153-1169.
    • (1998) Chem. Rev. , vol.98 , pp. 1153-1169
    • Burger, R.M.1
  • 25
    • 0037042234 scopus 로고    scopus 로고
    • 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.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4966-4967
    • Mathé, C.1    Mattioli, T.A.2    Horner, O.3    Lombard, M.4    Latour, J.-M.5    Fontecave, M.6    Nivière, V.7
  • 26
    • 0347264753 scopus 로고    scopus 로고
    • 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
    • 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.
    • (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
  • 27
    • 0000920237 scopus 로고    scopus 로고
    • Characterization and properties of nonheme iron peroxo complexes
    • Girerd J.-J., Banse F., Simaan A.J. Characterization and properties of nonheme iron peroxo complexes. Struct. Bonding. 97:2000;145-177.
    • (2000) Struct. Bonding , vol.97 , pp. 145-177
    • Girerd, J.-J.1    Banse, F.2    Simaan, A.J.3
  • 30
    • 0041870990 scopus 로고    scopus 로고
    • 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
    • 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.
    • (2003) Eur. J. Inorg. Chem. , vol.13 , pp. 2529-2535
    • Balland, V.1    Banse, F.2    Anxolabéhère-Mallart, E.3    Nierlich, M.4    Girerd, J.-J.5
  • 32
    • 0037063569 scopus 로고    scopus 로고
    • 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.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10810-10822
    • Lehnert, N.1    Neese, F.2    Ho, R.Y.N.3    Que, L.Jr.4    Solomon, E.I.5
  • 33
    • 0346245904 scopus 로고    scopus 로고
    • End-on and side-on peroxo derivatives of nonheme iron complexes with pentadentate ligands: Models for putative intermediates in biological iron/dioxygen chemistry
    • 2) intermediates in the N4Py ligand system. EXAFS studies provide the first metrical parameters for the iron coordination spheres in such peroxo complexes
    • 2) intermediates in the N4Py ligand system. EXAFS studies provide the first metrical parameters for the iron coordination spheres in such peroxo complexes.
    • (2003) Inorg. Chem. , vol.42 , pp. 2639-2653
    • 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
  • 34
    • 0037010036 scopus 로고    scopus 로고
    • III-OOH intermediate
    • - ligand is characterized as a model for a key intermediate in the catalytic cycle of superoxide reductase
    • - ligand is characterized as a model for a key intermediate in the catalytic cycle of superoxide reductase.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11709-11717
    • Shearer, J.1    Scarrow, R.C.2    Kovacs, J.A.3
  • 36
    • 0035904991 scopus 로고    scopus 로고
    • The electronic structure of nonheme iron(III)-hydroperoxo and iron(III)-peroxo complexes studied by Mössbauer and electron paramagnetic resonance spectroscopies
    • 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.
    • (2001) Inorg. Chem. , vol.40 , pp. 6538-6540
    • Simaan, A.J.1    Banse, F.2    Girerd, J.-J.3    Wieghardt, K.4    Bill, E.5
  • 38
    • 0036007785 scopus 로고    scopus 로고
    • Mononuclear nonheme iron(III) peroxide complexes: Syntheses, characterization, mass spectrometric and kinetic studies
    • 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.
    • (2002) J Chem Soc, Dalton Trans , pp. 310-317
    • Hazell, A.1    McKenzie, C.J.2    Nielsen, L.P.3    Schindler, S.4    Weitzer, M.5
  • 39
    • 0032539185 scopus 로고    scopus 로고
    • 3-: Electronic structure of the side-on ferric-peroxide bond and its relevance to reactivity
    • 3-: electronic structure of the side-on ferric-peroxide bond and its relevance to reactivity. J. Am. Chem. Soc. 120:1998;12829-12848.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 12829-12848
    • Neese, F.1    Solomon, E.I.2
  • 40
    • 0037467719 scopus 로고    scopus 로고
    • Electronic structure and reactivity of high-spin iron-alkyl and -pterinperoxo complexes
    • 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.
    • (2003) Inorg. Chem. , vol.42 , pp. 469-481
    • Lehnert, N.1    Fujisawa, K.2    Solomon, E.I.3
  • 41
    • 0035956535 scopus 로고    scopus 로고
    • Electronic structure of high-spin iron(III)-alkylperoxo complexes and its relation to low-spin analogues: Reaction coordinate of O-O bond homolysis
    • 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.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 12802-12816
    • Lehnert, N.1    Ho, R.Y.N.2    Que, L.Jr.3    Solomon, E.I.4
  • 42
    • 0037169656 scopus 로고    scopus 로고
    • 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.
    • (2002) Inorg. Chem. , vol.41 , pp. 616-618
    • Wada, A.1    Ogo, S.2    Nagatomo, S.3    Kitagawa, T.4    Watanabe, Y.5    Jitsukawa, K.6    Masuda, H.7
  • 44
    • 0034731019 scopus 로고    scopus 로고
    • Electronic structure of activated bleomycin: Oxygen intermediates in heme versus nonheme iron
    • 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.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 11703-11724
    • Neese, F.1    Zaleski, J.M.2    Loeb-Zaleski, K.3    Solomon, E.I.4
  • 45
    • 0000239991 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes containing binuclear nonheme iron clusters
    • Wallar B.J., Lipscomb J.D. Dioxygen activation by enzymes containing binuclear nonheme iron clusters. Chem. Rev. 96:1996;2625-2657.
    • (1996) Chem. Rev. , vol.96 , pp. 2625-2657
    • Wallar, B.J.1    Lipscomb, J.D.2
  • 46
    • 0039302669 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes with mononuclear nonheme iron active sites
    • Que L. Jr., Ho R.Y.N. Dioxygen activation by enzymes with mononuclear nonheme iron active sites. Chem. Rev. 96:1996;2607-2624.
    • (1996) Chem. Rev. , vol.96 , pp. 2607-2624
    • Que, L.Jr.1    Ho, R.Y.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.