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Volumn 2, Issue 5, 2010, Pages 400-405

Million-fold activation of the [Fe2 (μ-O)2 ] diamond core for C-H bond cleavage

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; HYDROGEN; IRON DERIVATIVE;

EID: 77951693360     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.586     Document Type: Article
Times cited : (198)

References (47)
  • 1
    • 44349148129 scopus 로고    scopus 로고
    • Selective oxidation of aliphatic C-H bonds in the synthesis of complex molecules
    • Christmann, M. Selective oxidation of aliphatic C-H bonds in the synthesis of complex molecules. Angew. Chem. Int. Ed. 47, 2740-2742 (2008).
    • (2008) Angew. Chem. Int. Ed. , vol.47 , pp. 2740-2742
    • Christmann, M.1
  • 3
    • 0000239991 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes containing binuclear non-heme iron clusters
    • Wallar, B. J. & Lipscomb, J. D. Dioxygen activation by enzymes containing binuclear non-heme iron clusters. Chem. Rev. 96, 2625-2658 (1996).
    • (1996) Chem. Rev. , vol.96 , pp. 2625-2658
    • Wallar, B.J.1    Lipscomb, J.D.2
  • 4
    • 0000208617 scopus 로고    scopus 로고
    • Geometric and electronic structure/function correlations in non-heme iron enzymes
    • Solomon, E. I. et al. Geometric and electronic structure/function correlations in non-heme iron enzymes. Chem. Rev. 100, 235-349 (2000).
    • (2000) Chem. Rev. , vol.100 , pp. 235-349
    • Solomon, E.I.1
  • 5
    • 1542378704 scopus 로고    scopus 로고
    • Oxygen activation at mononuclear nonheme iron: Enzymes, intermediates, and models
    • Costas, M., Mehn, M. P., Jensen, M. P. & Que, L., Jr. Oxygen activation at mononuclear nonheme iron: Enzymes, intermediates, and models. Chem. Rev. 104, 939-986 (2004).
    • (2004) Chem. Rev. , vol.104 , pp. 939-986
    • Costas, M.1    Mehn, M.P.2    Jensen, M.P.3    Que Jr., L.4
  • 7
    • 0036197490 scopus 로고    scopus 로고
    • Electronic structure and reactivity of high-valent oxo iron porphyrins
    • Fujii, H. Electronic structure and reactivity of high-valent oxo iron porphyrins. Coord. Chem. Rev. 226, 51-60 (2002).
    • (2002) Coord. Chem. Rev. , vol.226 , pp. 51-60
    • Fujii, H.1
  • 9
    • 0030614503 scopus 로고    scopus 로고
    • 2 diamond core structure for the key intermediate Q of methane monooxygenase
    • 2 diamond core structure for the key intermediate Q of methane monooxygenase. Science 275, 515-518 (1997).
    • (1997) Science , vol.275 , pp. 515-518
    • Shu, L.1
  • 10
    • 33846334797 scopus 로고    scopus 로고
    • Theoretical model studies of the iron dimer complex of MMO and RNR
    • Siegbahn, P. E. M. Theoretical model studies of the iron dimer complex of MMO and RNR. Inorg. Chem. 38, 2880-2889 (1999).
    • (1999) Inorg. Chem. , vol.38 , pp. 2880-2889
    • Siegbahn, P.E.M.1
  • 11
    • 0037560872 scopus 로고    scopus 로고
    • Mechanistic studies on the hydroxylation of methane by methane monooxygenase
    • Baik, M.-H., Newcomb, M., Friesner, R. A. & Lippard, S. J. Mechanistic studies on the hydroxylation of methane by methane monooxygenase. Chem. Rev. 103, 2385-2420 (2003).
    • (2003) Chem. Rev. , vol.103 , pp. 2385-2420
    • Baik, M.-H.1    Newcomb, M.2    Friesner, R.A.3    Lippard, S.J.4
  • 12
    • 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. et al. 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).
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 849-860
    • Riggs-Gelasco, P.J.1
  • 13
    • 57049098226 scopus 로고    scopus 로고
    • Structural analysis of the Mn (IV)/Fe (III) cofactor of Chlamydia trachomatis ribonucleotide reductase by extended X-ray absorption fine structure spectroscopy and density functional theory calculations
    • Younker, J. M. et al. Structural analysis of the Mn (IV)/Fe (III) cofactor of Chlamydia trachomatis ribonucleotide reductase by extended X-ray absorption fine structure spectroscopy and density functional theory calculations. J. Am. Chem. Soc. 130, 15022-15027 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 15022-15027
    • Younker, J.M.1
  • 14
    • 0029274199 scopus 로고
    • A high-valent nonheme iron intermediate
    • 3
    • 3. J. Am. Chem. Soc. 117, 2778-2792 (1995).
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2778-2792
    • Dong, Y.1
  • 15
    • 0033538303 scopus 로고    scopus 로고
    • 2 diamond core
    • Implications for the core structures of methane monooxygenase intermediate Q and ribonucleotide reductase intermediate
    • 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).
    • (1999) X. J. Am. Chem. Soc. , vol.121 , pp. 5230-5237
    • Hsu, H.-F.1    Dong, Y.2    Shu, L.3    Young Jr., V.G.4    Que Jr., L.5
  • 16
    • 38049169173 scopus 로고    scopus 로고
    • 2] diamond core proposed for methane monooxygenase intermediate Q
    • 2] diamond core proposed for methane monooxygenase intermediate Q. Proc. Natl Acad. Sci. USA 104, 20713-20718 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20713-20718
    • Xue, G.1
  • 17
    • 58549096706 scopus 로고    scopus 로고
    • Insights into the P-to-Q conversion in the catalytic cycle of methane monooxygenase from a synthetic model system
    • Xue, G., Fiedler, A. T., Martinho, M., Můnck, E. & Que, L., Jr. Insights into the P-to-Q conversion in the catalytic cycle of methane monooxygenase from a synthetic model system. Proc. Natl Acad. Sci. USA 105, 20615-20620 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 20615-20620
    • Xue, G.1    Fiedler, A.T.2    Martinho, M.3    Můnck, E.4    Que Jr., L.5
  • 19
    • 33745728199 scopus 로고    scopus 로고
    • Two-state reactivity in alkane hydroxylation by non-heme iron-oxo complexes
    • Hirao, H., Kumar, D., Que, L., Jr & Shaik, S. Two-state reactivity in alkane hydroxylation by non-heme iron-oxo complexes. J. Am. Chem. Soc. 128, 8590-8606 (2006).
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 8590-8606
    • Hirao, H.1    Kumar, D.2    Que Jr., L.3    Shaik, S.4
  • 20
    • 84962419519 scopus 로고    scopus 로고
    • IV=O complexes: Fe-O bonding and its contributions to reactivity
    • IV=O complexes: Fe-O bonding and its contributions to reactivity. J. Am. Chem. Soc. 129, 15983-15996 (2007).
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15983-15996
    • Decker, A.1
  • 21
    • 33645868668 scopus 로고    scopus 로고
    • High-valent nonheme iron-oxo species in biomimetic oxidations
    • Shan, X. & Que, L., Jr. High-valent nonheme iron-oxo species in biomimetic oxidations. J. Inorg. Biochem. 100, 421-433 (2006).
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 421-433
    • Shan, X.1    Que Jr., L.2
  • 22
    • 34547732579 scopus 로고    scopus 로고
    • The road to non-heme oxoferryls and beyond
    • Que, L., Jr. The road to non-heme oxoferryls and beyond. Acc. Chem. Res. 40, 493-500 (2007).
    • (2007) Acc. Chem. Res. , vol.40 , pp. 493-500
    • Que Jr., L.1
  • 23
    • 27544486220 scopus 로고    scopus 로고
    • IV=O: Spectroscopic identification and oxo group exchange
    • IV=O: Spectroscopic identification and oxo group exchange. Angew. Chem. Int. Ed. 44, 6871-6874 (2005).
    • (2005) Angew. Chem. Int. Ed. , vol.44 , pp. 6871-6874
    • Pestovsky, O.1
  • 24
    • 0028794470 scopus 로고
    • III sites of relevance to cluster X of Escherichia coli ribonucleotide reductase
    • III sites of relevance to cluster X of Escherichia coli ribonucleotide reductase. J. Am. Chem. Soc. 117, 11377-11378 (1995).
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11377-11378
    • Dong, Y.1    Que Jr., L.2    Kauffmann, K.3    Můnck, E.4
  • 25
    • 0342314443 scopus 로고    scopus 로고
    • 2 diamond core: A terminal iron (IV)-oxo species generated from the oxidation of a bis (μ-oxo) diiron (III) complex
    • 2 diamond core: A terminal iron (IV)-oxo species generated from the oxidation of a bis (μ-oxo) diiron (III) complex. J. Am. Chem. Soc. 122, 3789-3790 (2000).
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 3789-3790
    • Zheng, H.1    Yoo, S.J.2    Můnck, E.3    Que Jr., L.4
  • 26
    • 70349972275 scopus 로고    scopus 로고
    • A synthetic high-spin oxoiron (IV) complex. Generation, spectroscopic characterization and reactivity
    • England, J. et al. A synthetic high-spin oxoiron (IV) complex. Generation, spectroscopic characterization and reactivity. Angew. Chem. Int. Ed. 48, 3622-3626 (2009).
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 3622-3626
    • England, J.1
  • 27
    • 0142151778 scopus 로고    scopus 로고
    • III/II complexes with terminal hydroxo and oxo ligands: Probing reactivity via O-H bond dissociation energies
    • III/II complexes with terminal hydroxo and oxo ligands: Probing reactivity via O-H bond dissociation energies. J. Am. Chem. Soc. 125, 13234-13242 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13234-13242
    • Gupta, R.1    Borovik, A.S.2
  • 28
    • 0027951575 scopus 로고
    • Mechanism of assembly of the tyrosyl radical-diiron (III) cofactor of E. coli ribonucleotide reductase. 1. Mo̊ssbauer characterization of the diferric radical precursor
    • Ravi, N., Bollinger, J. M., Jr., Huynh, B. H., Edmondson, D. E. & Stubbe, J. Mechanism of assembly of the tyrosyl radical-diiron (III) cofactor of E. coli ribonucleotide reductase. 1. Mo̊ssbauer characterization of the diferric radical precursor. J. Am. Chem. Soc. 116, 8007-8014 (1994).
    • (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
  • 29
    • 0029740493 scopus 로고    scopus 로고
    • Reconsideration of X, the diiron intermediate formed during cofactor assembly in E. coli ribonucleotide reductase
    • Sturgeon, B. E. et al. Reconsideration of X, the diiron intermediate formed during cofactor assembly in E. coli ribonucleotide reductase. J. Am. Chem. Soc. 118, 7551-7557 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7551-7557
    • Sturgeon, B.E.1
  • 30
    • 0003988115 scopus 로고    scopus 로고
    • Spectroscopy and Magnetism, ed Que, L. Jr., University Science Books
    • Můnck, E. in Physical Methods in Bioinorganic Chemistry. Spectroscopy and Magnetism (ed Que, L. Jr.) 287-319 (University Science Books, 2000).
    • (2000) Physical Methods in Bioinorganic Chemistry. , pp. 287-319
    • Můnck, E.1
  • 32
    • 33645879244 scopus 로고    scopus 로고
    • Stalking intermediates in oxygen activation by iron enzymes: Motivation and method
    • Bollinger, J. M., Jr. & Krebs, C. Stalking intermediates in oxygen activation by iron enzymes: Motivation and method. J. Inorg. Biochem. 100, 586-605 (2006).
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 586-605
    • Bollinger Jr., J.M.1    Krebs, C.2
  • 34
    • 34547725316 scopus 로고    scopus 로고
    • Reactivity of high-valent iron-oxo species in enzymes and synthetic reagents: A tale of many states
    • Shaik, S., Hirao, H. & Kumar, D. Reactivity of high-valent iron-oxo species in enzymes and synthetic reagents: a tale of many states. Acc. Chem. Res. 40, 523-542 (2007).
    • (2007) Acc. Chem. Res. , vol.40 , pp. 523-542
    • Shaik, S.1    Hirao, H.2    Kumar, D.3
  • 36
    • 39749096483 scopus 로고    scopus 로고
    • Direct evidence for an iron (IV)-oxo porphyrin π-cation radical as an active oxidant in catalytic oxygenation reactions
    • Han, A.-R. et al. Direct evidence for an iron (IV)-oxo porphyrin π-cation radical as an active oxidant in catalytic oxygenation reactions. Chem. Commun. 2008, 1076-1078 (2008).
    • (2008) Chem. Commun. , vol.2008 , pp. 1076-1078
    • Han, A.-R.1
  • 37
    • 67650501146 scopus 로고    scopus 로고
    • A highly reactive P450 model compound I
    • Bell, S. R. & Groves, J. T. A highly reactive P450 model compound I. J. Am. Chem. Soc. 131, 9640-9641 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 9640-9641
    • Bell, S.R.1    Groves, J.T.2
  • 38
    • 67849118867 scopus 로고    scopus 로고
    • A diiron (IV) complex that cleaves strong C-H and O-H bonds
    • Wang, D., Farquhar, E. R., Stubna, A., Můnck, E. & Que, L., Jr. A diiron (IV) complex that cleaves strong C-H and O-H bonds. Nature Chem. 1, 145-150 (2009).
    • (2009) Nature Chem. , vol.1 , pp. 145-150
    • Wang, D.1    Farquhar, E.R.2    Stubna, A.3    Můnck, E.4    Que Jr., L.5
  • 39
    • 0000647193 scopus 로고    scopus 로고
    • Hydrogen atom abstraction by metal-oxo complexes: Understanding the analogy with organic radical reactions
    • Mayer, J. M. Hydrogen atom abstraction by metal-oxo complexes: Understanding the analogy with organic radical reactions. Acc. Chem. Res. 31, 441-450 (1998).
    • (1998) Acc. Chem. Res. , vol.31 , pp. 441-450
    • Mayer, J.M.1
  • 41
    • 0029654151 scopus 로고
    • - transfer in the oxidation of toluene by permanganate
    • - transfer in the oxidation of toluene by permanganate. Science 269, 1849-1851 (1995).
    • (1995) Science , vol.269 , pp. 1849-1851
    • Gardner, K.A.1    Mayer, J.M.2
  • 42
    • 0344718437 scopus 로고    scopus 로고
    • A potentiometric study of acid-base equilibria of substituted pyridines in acetonitrile
    • DOI 10.1016/S0003-2670(98)00771-5, PII S0003267098007715
    • Augustin-Nowacka, D. & Chmurzyňski, L. A potentiometric study of acid-base equilibria of substituted pyridines in acetonitrile. Anal. Chim. Acta 381, 215-220 (1999). (Pubitemid 29073298)
    • (1999) Analytica Chimica Acta , vol.381 , Issue.2-3 , pp. 215-220
    • Augustin-Nowacka, D.1    Chmurzynski, L.2
  • 43
    • 57149083074 scopus 로고    scopus 로고
    • Oxidative reactivity difference among the metal oxo and metal hydroxo moieties: Ph dependent hydrogen abstraction by a manganese (IV) complex having two hydroxide ligands
    • Yin, G. et al. Oxidative reactivity difference among the metal oxo and metal hydroxo moieties: ph dependent hydrogen abstraction by a manganese (IV) complex having two hydroxide ligands. J. Am. Chem. Soc. 130, 16245-16253 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 16245-16253
    • Yin, G.1
  • 45
    • 77951688219 scopus 로고    scopus 로고
    • Observed enhancement of the catalytic activity of a biomimetic diiron complex by the addition of water - Mechanistic insights from theoretical modeling
    • Johansson, A. J., Noack, H., Siegbahn, P. E. M., Xue, G. & Que, L., Jr. Observed enhancement of the catalytic activity of a biomimetic diiron complex by the addition of water - mechanistic insights from theoretical modeling. Dalton Trans. 4741-4750 (2009).
    • (2009) Dalton Trans. , pp. 4741-4750
    • Johansson, A.J.1    Noack, H.2    Siegbahn, P.E.M.3    Xue, G.4    Que Jr., L.5
  • 46
    • 0030986743 scopus 로고    scopus 로고
    • Mechanism of C-H Activation by diiron methane monooxygenases: Quantum chemical studies
    • Siegbahn, P. E. M. & Crabtree, R. H. Mechanism of C-H Activation by diiron methane monooxygenases: quantum chemical studies. J. Am. Chem. Soc. 119, 3103-3113 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3103-3113
    • Siegbahn, P.E.M.1    Crabtree, R.H.2
  • 47
    • 33947413978 scopus 로고    scopus 로고
    • Intermediates in dioxygen activation by methane monooxygenase: A QM/MM study
    • Rinaldo, D., Philipp, D. M., Lippard, S. J. & Friesner, R. A. Intermediates in dioxygen activation by methane monooxygenase: A QM/MM study. J. Am. Chem. Soc. 129, 3135-3147 (2007).
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 3135-3147
    • Rinaldo, D.1    Philipp, D.M.2    Lippard, S.J.3    Friesner, R.A.4


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