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Volumn 455, Issue 7211, 2008, Pages 333-340

Biologically inspired oxidation catalysis

Author keywords

[No Author keywords available]

Indexed keywords

CATECHOL; COPPER; ENZYME; HYDROCARBON; IRON; PHENOL;

EID: 52449135188     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature07371     Document Type: Review
Times cited : (1240)

References (99)
  • 1
    • 0035323783 scopus 로고    scopus 로고
    • Catalysis research of relevance to carbon management: Progress, challenges, and opportunities
    • Arakawa, H. et al. Catalysis research of relevance to carbon management: progress, challenges, and opportunities. Chem. Rev. 101, 953-996 (2001).
    • (2001) Chem. Rev , vol.101 , pp. 953-996
    • Arakawa, H.1
  • 2
    • 21944440277 scopus 로고    scopus 로고
    • Recent advances in transition metal catalyzed oxidation of organic substrates with molecular oxygen
    • Punniyamurthy, T., Velusamy, S. & Iqbal, J. Recent advances in transition metal catalyzed oxidation of organic substrates with molecular oxygen. Chem. Rev. 105, 2329-2364 (2005).
    • (2005) Chem. Rev , vol.105 , pp. 2329-2364
    • Punniyamurthy, T.1    Velusamy, S.2    Iqbal, J.3
  • 8
    • 0024294403 scopus 로고
    • Probing structure-function relations in heme-containing oxygenases and peroxidases
    • Dawson, J. H. Probing structure-function relations in heme-containing oxygenases and peroxidases. Science 240, 433-439 (1988).
    • (1988) Science , vol.240 , pp. 433-439
    • Dawson, J.H.1
  • 9
    • 4644228230 scopus 로고    scopus 로고
    • The heme paradigm revisited: Alternative reaction pathways considered
    • Que, L. The heme paradigm revisited: alternative reaction pathways considered. J. Biol. Inorg. Chem. 9, 643-690 (2004).
    • (2004) J. Biol. Inorg. Chem , vol.9 , pp. 643-690
    • Que, L.1
  • 10
    • 0035800409 scopus 로고    scopus 로고
    • Dioxygen activation and methane hydroxylation by soluble methane monooxygenase: A tale of two irons and three proteins
    • Merkx, M. et al. Dioxygen activation and methane hydroxylation by soluble methane monooxygenase: a tale of two irons and three proteins. Angew. Chem. Int. Edn Engl. 40, 2782-2807 (2001).
    • (2001) Angew. Chem. Int. Edn Engl , vol.40 , pp. 2782-2807
    • Merkx, M.1
  • 11
    • 19744365629 scopus 로고    scopus 로고
    • Reactions of the peroxo intermediate of soluble methane monooxygenase hydroxylase with ethers
    • Beauvais, L. G. & Lippard, S. J. Reactions of the peroxo intermediate of soluble methane monooxygenase hydroxylase with ethers. J. Am. Chem. Soc. 127, 7370-7378 (2005).
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 7370-7378
    • Beauvais, L.G.1    Lippard, S.J.2
  • 12
    • 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, 2625-2658 (1996).
    • (1996) Chem. Rev , vol.96 , pp. 2625-2658
    • Wallar, B.J.1    Lipscomb, J.D.2
  • 13
    • 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
  • 14
    • 27544477399 scopus 로고    scopus 로고
    • Rieske business: Structure-function of Rieske non-heme oxygenases
    • Ferraro, D. J., Gakhar, L. & Ramaswamy, S. Rieske business: structure-function of Rieske non-heme oxygenases. Biochem. Biophys. Res. Commun. 338, 175-190 (2005).
    • (2005) Biochem. Biophys. Res. Commun , vol.338 , pp. 175-190
    • Ferraro, D.J.1    Gakhar, L.2    Ramaswamy, S.3
  • 15
    • 0347264753 scopus 로고    scopus 로고
    • Side-on binding of dioxygen to iron: Implications for enzymatic cis-dihydroxylation reactions
    • Karlsson, A. et al. Side-on binding of dioxygen to iron: implications for enzymatic cis-dihydroxylation reactions. Science 299, 1039-1042 (2003).
    • (2003) Science , vol.299 , pp. 1039-1042
    • Karlsson, A.1
  • 18
    • 0038604805 scopus 로고    scopus 로고
    • Free radical catalysis by galactose oxidase
    • Whittaker, J. W. Free radical catalysis by galactose oxidase. Chem. Rev. 103, 2347-2363 (2003).
    • (2003) Chem. Rev , vol.103 , pp. 2347-2363
    • Whittaker, J.W.1
  • 19
    • 9944255706 scopus 로고    scopus 로고
    • The radical chemistry of galactose oxidase
    • Whittaker, J. W. The radical chemistry of galactose oxidase. Arch. Biochem. Biophys. 433, 227-239 (2005).
    • (2005) Arch. Biochem. Biophys , vol.433 , pp. 227-239
    • Whittaker, J.W.1
  • 20
    • 0026084786 scopus 로고
    • Novel thioether bond revealed by a 1.7 Å crystal structure of galactose oxidase
    • Ito, N. et al. Novel thioether bond revealed by a 1.7 Å crystal structure of galactose oxidase. Nature 350, 87-90 (1991).
    • (1991) Nature , vol.350 , pp. 87-90
    • Ito, N.1
  • 21
    • 34247205791 scopus 로고    scopus 로고
    • The stacking tryptophan of galactose oxidase: A second-coordination sphere residue that has profound effects on tyrosyl radical behavior and enzyme catalysis
    • Rogers, M. S. et al. The stacking tryptophan of galactose oxidase: a second-coordination sphere residue that has profound effects on tyrosyl radical behavior and enzyme catalysis. Biochemistry 46, 4606-4618 (2007).
    • (2007) Biochemistry , vol.46 , pp. 4606-4618
    • Rogers, M.S.1
  • 22
    • 0033808699 scopus 로고    scopus 로고
    • Understanding the copper-phenoxyl radical array in galactose oxidase: Contributions from synthetic modeling studies
    • Jazdzewski, B. A. & Tolman, W. B. Understanding the copper-phenoxyl radical array in galactose oxidase: contributions from synthetic modeling studies. Coord. Chem. Rev. 200-202, 633-685 (2000).
    • (2000) Coord. Chem. Rev , vol.200-202 , pp. 633-685
    • Jazdzewski, B.A.1    Tolman, W.B.2
  • 23
    • 34250883970 scopus 로고    scopus 로고
    • Ten years of a biomimetic approach to the copper(ii) radical site of galactose oxidase
    • Fabrice, T. Ten years of a biomimetic approach to the copper(ii) radical site of galactose oxidase. Eur. J. Inorg. Chem. 2007, 2379-2404 (2007).
    • (2007) Eur. J. Inorg. Chem , vol.2007 , pp. 2379-2404
    • Fabrice, T.1
  • 24
    • 40949130075 scopus 로고    scopus 로고
    • Systematic development of computational models for the catalytic site in galactose oxidase: Impact of outer-sphere residues on the geometric and electronic structures
    • Rokhsana, D., Dooley, D. M. & Szilagyi, R. K. Systematic development of computational models for the catalytic site in galactose oxidase: impact of outer-sphere residues on the geometric and electronic structures. J. Biol. Inorg. Chem. 13, 371-383 (2008).
    • (2008) J. Biol. Inorg. Chem , vol.13 , pp. 371-383
    • Rokhsana, D.1    Dooley, D.M.2    Szilagyi, R.K.3
  • 25
    • 0035912908 scopus 로고    scopus 로고
    • Catalytic reaction profile for alcohol oxidation by galactose oxidase
    • Whittaker, M. M. & Whittaker, J. W. Catalytic reaction profile for alcohol oxidation by galactose oxidase. Biochemistry 40, 7140-7148 (2001).
    • (2001) Biochemistry , vol.40 , pp. 7140-7148
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 26
    • 0000200878 scopus 로고
    • Recent structural work on the oxygen transport protein hemocyanin
    • Magnus, K. A., Ton-That, H. & Carpenter, J. E. Recent structural work on the oxygen transport protein hemocyanin. Chem. Rev. 94, 727-735 (1994).
    • (1994) Chem. Rev , vol.94 , pp. 727-735
    • Magnus, K.A.1    Ton-That, H.2    Carpenter, J.E.3
  • 27
    • 0032525161 scopus 로고    scopus 로고
    • Crystal structure of a functional unit from octopus hemocyanin
    • Cuff, M. E., Miller, K. I., van Holde, K. E. & Hendrickson, W. A. Crystal structure of a functional unit from octopus hemocyanin. J. Mol. Biol. 278, 855-870 (1998).
    • (1998) J. Mol. Biol , vol.278 , pp. 855-870
    • Cuff, M.E.1    Miller, K.I.2    van Holde, K.E.3    Hendrickson, W.A.4
  • 28
    • 33646827679 scopus 로고    scopus 로고
    • Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis
    • Matoba, Y., Kumagai, T., Yamamoto, A., Yoshitsu, H. & Sugiyama, M. Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis. J. Biol. Chem. 281, 8981-8990 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 8981-8990
    • Matoba, Y.1    Kumagai, T.2    Yamamoto, A.3    Yoshitsu, H.4    Sugiyama, M.5
  • 29
    • 0032941536 scopus 로고    scopus 로고
    • Purification and spectroscopic studies on catechol oxidases from Lycopus europaeus and Populus nigra: Evidence for a dinuclear copper center of type 3 and spectroscopic similarities of tyrosinase and hemocyanin
    • Rompel, A. et al. Purification and spectroscopic studies on catechol oxidases from Lycopus europaeus and Populus nigra: evidence for a dinuclear copper center of type 3 and spectroscopic similarities of tyrosinase and hemocyanin. J. Biol. Inorg. Chem. 4, 56-63 (1999).
    • (1999) J. Biol. Inorg. Chem , vol.4 , pp. 56-63
    • Rompel, A.1
  • 30
    • 33644931317 scopus 로고    scopus 로고
    • Mechanistic insight into the activity of tyrosinase from variable-temperature studies in an aqueous/organic solvent
    • Granata, A., Monzani, E., Bubacco, L. & Casella, L. Mechanistic insight into the activity of tyrosinase from variable-temperature studies in an aqueous/organic solvent. Chem. Eur. J. 12, 2504-2514 (2006).
    • (2006) Chem. Eur. J , vol.12 , pp. 2504-2514
    • Granata, A.1    Monzani, E.2    Bubacco, L.3    Casella, L.4
  • 31
    • 0142214624 scopus 로고    scopus 로고
    • Kinetic evaluation of phenolase activity of tyrosinase using simplified catalytic reaction system
    • Yamazaki, S. & Itoh, S. Kinetic evaluation of phenolase activity of tyrosinase using simplified catalytic reaction system. J. Am. Chem. Soc. 125, 13034-13035 (2003).
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 13034-13035
    • Yamazaki, S.1    Itoh, S.2
  • 32
    • 1542304579 scopus 로고    scopus 로고
    • Structure and spectroscopy of copper-dioxygen complexes
    • Mirica, L. M., Ottenwaelder, X. & Stack, T. D. P. Structure and spectroscopy of copper-dioxygen complexes. Chem. Rev. 104, 1013-1045 (2004).
    • (2004) Chem. Rev , vol.104 , pp. 1013-1045
    • Mirica, L.M.1    Ottenwaelder, X.2    Stack, T.D.P.3
  • 33
    • 1542288709 scopus 로고    scopus 로고
    • Reactivity of copper-dioxygen systems
    • Lewis, E. A. & Tolman, W. B. Reactivity of copper-dioxygen systems. Chem. Rev. 104, 1047-1076 (2004).
    • (2004) Chem. Rev , vol.104 , pp. 1047-1076
    • Lewis, E.A.1    Tolman, W.B.2
  • 34
    • 33747602095 scopus 로고    scopus 로고
    • Ligand influences in copper-dioxygen complex-formation and substrate oxidations
    • Hatcher, L. Q. & Karlin, K. D. Ligand influences in copper-dioxygen complex-formation and substrate oxidations. Adv. Inorg. Chem. 58, 131-184 (2006).
    • (2006) Adv. Inorg. Chem , vol.58 , pp. 131-184
    • Hatcher, L.Q.1    Karlin, K.D.2
  • 35
    • 21344458566 scopus 로고    scopus 로고
    • Tyrosinase reactivity in a model complex: An alternative hydroxylation mechanism
    • Mirica, L. M. et al. Tyrosinase reactivity in a model complex: an alternative hydroxylation mechanism. Science 308, 1890-1892 (2005).
    • (2005) Science , vol.308 , pp. 1890-1892
    • Mirica, L.M.1
  • 36
    • 3042550172 scopus 로고    scopus 로고
    • Copper-containing amine oxidases. Biogenesis and catalysis; a structural perspective
    • Brazeau, B. J., Johnson, B. J. & Wilmot, C. M. Copper-containing amine oxidases. Biogenesis and catalysis; a structural perspective. Arch. Biochem. Biophys. 428, 22-31 (2004).
    • (2004) Arch. Biochem. Biophys , vol.428 , pp. 22-31
    • Brazeau, B.J.1    Johnson, B.J.2    Wilmot, C.M.3
  • 37
    • 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. 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).
    • (2006) J. Biol. Chem , vol.281 , pp. 3013-3016
    • Klinman, J.P.1
  • 38
    • 0346118953 scopus 로고    scopus 로고
    • Evidence that dioxygen and substrate activation are tightly coupled in dopamine β-monooxygenase: Implications for the reactive oxygen species
    • Evans, J. P., Ahn, K. & Klinman, J. P. Evidence that dioxygen and substrate activation are tightly coupled in dopamine β-monooxygenase: implications for the reactive oxygen species. J. Biol. Chem. 278, 49691-49698 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 49691-49698
    • Evans, J.P.1    Ahn, K.2    Klinman, J.P.3
  • 39
    • 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. & Solomon, E. I. 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).
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 4991-5000
    • Chen, P.1    Solomon, E.I.2
  • 40
    • 34547814764 scopus 로고    scopus 로고
    • 2 complexes: Geometries, spectroscopic properties, electronic structures, and reactivity
    • 2 complexes: geometries, spectroscopic properties, electronic structures, and reactivity. Acc. Chem. Res. 40, 601-608 (2007).
    • (2007) Acc. Chem. Res , vol.40 , pp. 601-608
    • Cramer, C.J.1    Tolman, W.B.2
  • 41
    • 2442545587 scopus 로고    scopus 로고
    • Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex
    • Prigge, S. T., Eipper, B. A., Mains, R. E. & Amzel, L. M. Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex. Science 304, 864-867 (2004).
    • (2004) Science , vol.304 , pp. 864-867
    • Prigge, S.T.1    Eipper, B.A.2    Mains, R.E.3    Amzel, L.M.4
  • 42
    • 33645871857 scopus 로고    scopus 로고
    • Catalytic mechanism of dopamine β-monooxygenase mediated by Cu(iii)-oxo
    • Yoshizawa, K., Kihara, N., Kamachi, T. & Shiota, Y. Catalytic mechanism of dopamine β-monooxygenase mediated by Cu(iii)-oxo. Inorg. Chem. 45, 3034-3041 (2006).
    • (2006) Inorg. Chem , vol.45 , pp. 3034-3041
    • Yoshizawa, K.1    Kihara, N.2    Kamachi, T.3    Shiota, Y.4
  • 43
    • 33749526867 scopus 로고    scopus 로고
    • The catalytic mechanism of peptidylglycine α-hydroxylating monooxygenase investigated by computer simulation
    • Crespo, A., Marti, M. A., Roitberg, A. E., Amzel, L. M. & Estrin, D. A. The catalytic mechanism of peptidylglycine α-hydroxylating monooxygenase investigated by computer simulation. J. Am. Chem. Soc. 128, 12817-12828 (2006).
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 12817-12828
    • Crespo, A.1    Marti, M.A.2    Roitberg, A.E.3    Amzel, L.M.4    Estrin, D.A.5
  • 44
    • 42449131766 scopus 로고    scopus 로고
    • How do copper enzymes hydroxylate aliphatic substrates? Recent insights from the chemistry of model systems
    • Rolff, M. & Tuczek, F. How do copper enzymes hydroxylate aliphatic substrates? Recent insights from the chemistry of model systems. Angew. Chem. Int. Edn Engl. 47, 2344-2347 (2008).
    • (2008) Angew. Chem. Int. Edn Engl , vol.47 , pp. 2344-2347
    • Rolff, M.1    Tuczek, F.2
  • 45
    • 36849002980 scopus 로고    scopus 로고
    • Recent advances in copper-catalyzed oxidation of organic compounds
    • Punniyamurthy, T. & Rout, L. Recent advances in copper-catalyzed oxidation of organic compounds. Coord. Chem. Rev. 252, 134-154 (2008).
    • (2008) Coord. Chem. Rev , vol.252 , pp. 134-154
    • Punniyamurthy, T.1    Rout, L.2
  • 46
    • 33646579600 scopus 로고    scopus 로고
    • Green oxidation of alcohols using biomimetic Cu complexes and Cu enzymes as catalysts
    • This review surveys progress in the use of biologically inspired copper-ligand radical complexes as alcohol oxidation catalysts
    • Arends, I., Gamez, P. & Sheldon, R. A. Green oxidation of alcohols using biomimetic Cu complexes and Cu enzymes as catalysts. Adv. Inorg. Chem. 58, 235-279 (2006). This review surveys progress in the use of biologically inspired copper-ligand radical complexes as alcohol oxidation catalysts.
    • (2006) Adv. Inorg. Chem , vol.58 , pp. 235-279
    • Arends, I.1    Gamez, P.2    Sheldon, R.A.3
  • 47
    • 44049092112 scopus 로고    scopus 로고
    • Catalytic oxidation of organic substrates by molecular oxygen and hydrogen peroxide by multistep electron transfer - a biomimetic approach
    • This topical review on biologically inspired oxidation catalysis emphasizes systems that use electron-transfer mediators to couple reduction and oxidation steps in biomimetic catalytic cycles
    • Piera, J. & Bäckvall, J. E. Catalytic oxidation of organic substrates by molecular oxygen and hydrogen peroxide by multistep electron transfer - a biomimetic approach. Angew. Chem. Int. Edn Engl. 47, 3506-3523 (2008). This topical review on biologically inspired oxidation catalysis emphasizes systems that use electron-transfer mediators to couple reduction and oxidation steps in biomimetic catalytic cycles.
    • (2008) Angew. Chem. Int. Edn Engl , vol.47 , pp. 3506-3523
    • Piera, J.1    Bäckvall, J.E.2
  • 48
    • 0030476115 scopus 로고    scopus 로고
    • Galactose oxidase model complexes: Catalytic reactivities
    • Wang, Y. & Stack, T. D. P. Galactose oxidase model complexes: catalytic reactivities. J. Am. Chem. Soc. 118, 13097-13098 (1996).
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 13097-13098
    • Wang, Y.1    Stack, T.D.P.2
  • 49
    • 0032559208 scopus 로고    scopus 로고
    • Catalytic galactose oxidase models: Biomimetic Cu(ii)-phenoxyl-radical reactivity
    • Wang, Y., DuBois, J. L., Hedman, B., Hodgson, K. O. & Stack, T. D. P. Catalytic galactose oxidase models: biomimetic Cu(ii)-phenoxyl-radical reactivity. Science 279, 537-540 (1998).
    • (1998) Science , vol.279 , pp. 537-540
    • Wang, Y.1    DuBois, J.L.2    Hedman, B.3    Hodgson, K.O.4    Stack, T.D.P.5
  • 50
    • 27644433564 scopus 로고    scopus 로고
    • Biomimetic metal-radical reactivity: Aerial oxidation of alcohols, amines, aminophenols and catechols catalyzed by transition metal complexes
    • Chaudhuri, P. et al. Biomimetic metal-radical reactivity: aerial oxidation of alcohols, amines, aminophenols and catechols catalyzed by transition metal complexes. J. Biol. Chem. 386, 1023-1033 (2005).
    • (2005) J. Biol. Chem , vol.386 , pp. 1023-1033
    • Chaudhuri, P.1
  • 51
    • 0031678724 scopus 로고    scopus 로고
    • From structural models of galactose oxidase to homogeneous catalysis: Efficient aerobic oxidation of alcohols
    • Chaudhuri, P., Hess, H., Flörke, U. & Wieghardt, K. From structural models of galactose oxidase to homogeneous catalysis: efficient aerobic oxidation of alcohols. Angew. Chem. Int. Edn Engl. 37, 2217-2220 (1998).
    • (1998) Angew. Chem. Int. Edn Engl , vol.37 , pp. 2217-2220
    • Chaudhuri, P.1    Hess, H.2    Flörke, U.3    Wieghardt, K.4
  • 52
    • 0033583557 scopus 로고    scopus 로고
    • Aerobic oxidation of primary alcohols by a new mononuclear Cu(ii)-radical catalyst
    • Chaudhuri, P., Hess, M., Weyhermüller, T. & Wieghardt, K. Aerobic oxidation of primary alcohols by a new mononuclear Cu(ii)-radical catalyst. Angew. Chem. Int. Edn Engl. 38, 1095-1098 (1999).
    • (1999) Angew. Chem. Int. Edn Engl , vol.38 , pp. 1095-1098
    • Chaudhuri, P.1    Hess, M.2    Weyhermüller, T.3    Wieghardt, K.4
  • 53
    • 0032732642 scopus 로고    scopus 로고
    • Aerobic oxidation of primary alcohols (including methanol) by copper(ii)- and zinc(ii)-phenoxyl radical catalysts
    • Chem. Soc
    • Chaudhuri, P. et al. Aerobic oxidation of primary alcohols (including methanol) by copper(ii)- and zinc(ii)-phenoxyl radical catalysts. J. Am. Chem. Soc. 121, 9599-9610 (1999).
    • (1999) J. Am , vol.121 , pp. 9599-9610
    • Chaudhuri, P.1
  • 54
    • 3342895064 scopus 로고    scopus 로고
    • Aerial oxidation of primary alcohols and amines catalyzed by Cu(ii) complexes of 2,2′-selenobis(4,6-di-tert-butylphenol) providing [O,Se,O]-donor atoms
    • Paine, T. K., Weyhermüller, T., Wieghardt, K. & Chaudhuri, P. Aerial oxidation of primary alcohols and amines catalyzed by Cu(ii) complexes of 2,2′-selenobis(4,6-di-tert-butylphenol) providing [O,Se,O]-donor atoms. Dalton Trans. 2092-2101 (2004).
    • (2004) Dalton Trans , pp. 2092-2101
    • Paine, T.K.1    Weyhermüller, T.2    Wieghardt, K.3    Chaudhuri, P.4
  • 55
    • 33646087884 scopus 로고    scopus 로고
    • Catalytic oxidations mediated by metal ions and nitroxyl radicals
    • Sheldon, R. & Arends, I. Catalytic oxidations mediated by metal ions and nitroxyl radicals. J. Mol. Catal. A 251, 200-214 (2006).
    • (2006) J. Mol. Catal. A , vol.251 , pp. 200-214
    • Sheldon, R.1    Arends, I.2
  • 57
    • 0037071234 scopus 로고    scopus 로고
    • Copper-catalysed aerobic oxidation of alcohols using fluorous biphasic catalysis
    • Ragagnin, G., Betzemeier, B., Quici, S. & Knochel, P. Copper-catalysed aerobic oxidation of alcohols using fluorous biphasic catalysis. Tetrahedron 58, 3985-3991 (2002).
    • (2002) Tetrahedron , vol.58 , pp. 3985-3991
    • Ragagnin, G.1    Betzemeier, B.2    Quici, S.3    Knochel, P.4
  • 58
    • 27644586813 scopus 로고    scopus 로고
    • Efficient, ecologically benign, aerobic oxidation of alcohols
    • Markó, I. E. et al. Efficient, ecologically benign, aerobic oxidation of alcohols. Adv. Inorg. Chem. 56, 211-240 (2004).
    • (2004) Adv. Inorg. Chem , vol.56 , pp. 211-240
    • Markó, I.E.1
  • 59
    • 4544344165 scopus 로고    scopus 로고
    • Efficient, copper-catalyzed, aerobic oxidation of primary alcohols
    • Markó, I. et al. Efficient, copper-catalyzed, aerobic oxidation of primary alcohols. Angew. Chem. Int. Edn Engl. 43, 1588-1591 (2004).
    • (2004) Angew. Chem. Int. Edn Engl , vol.43 , pp. 1588-1591
    • Markó, I.1
  • 61
    • 33747855171 scopus 로고    scopus 로고
    • Synthetic models of the active site of catechol oxidase: Mechanistic studies
    • References 60 and 61 review the catalytic oxidations of phenols and catechols by synthetic models of the dicopper active sites of tyrosinase and catechol oxidase from a mechanistic perspective
    • Koval, I. A., Gamez, P., Belle, C., Selmeczi, K. & Reedijk, J. Synthetic models of the active site of catechol oxidase: mechanistic studies. Chem. Soc. Rev. 35, 814-840 (2006). References 60 and 61 review the catalytic oxidations of phenols and catechols by synthetic models of the dicopper active sites of tyrosinase and catechol oxidase from a mechanistic perspective.
    • (2006) Chem. Soc. Rev , vol.35 , pp. 814-840
    • Koval, I.A.1    Gamez, P.2    Belle, C.3    Selmeczi, K.4    Reedijk, J.5
  • 62
    • 0032569209 scopus 로고    scopus 로고
    • Highly regioselective oxidative polymerization of 4-phenoxyphenol to poly(1,4-phenylene oxide) catalyzed by tyrosinase model complexes
    • Higashimura, H. et al. Highly regioselective oxidative polymerization of 4-phenoxyphenol to poly(1,4-phenylene oxide) catalyzed by tyrosinase model complexes. J. Am. Chem. Soc. 120, 8529-8530 (1998).
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 8529-8530
    • Higashimura, H.1
  • 63
    • 0033890677 scopus 로고    scopus 로고
    • Radical-controlled' oxidative polymerization of 4-phenoxyphenol by a tyrosinase model complex catalyst to poly(1,4-phenylene oxide)
    • Higashimura, H. et al. 'Radical-controlled' oxidative polymerization of 4-phenoxyphenol by a tyrosinase model complex catalyst to poly(1,4-phenylene oxide). Macromolecules 33, 1986-1995 (2000).
    • (2000) Macromolecules , vol.33 , pp. 1986-1995
    • Higashimura, H.1
  • 64
    • 0033702594 scopus 로고    scopus 로고
    • 2-peroxo dicopper(ii) complex
    • 2-peroxo dicopper(ii) complex. Appl. Catal. A 194, 427-433 (2000).
    • (2000) Appl. Catal. A , vol.194 , pp. 427-433
    • Higashimura, H.1
  • 65
    • 19944382496 scopus 로고    scopus 로고
    • Radical-controlled' oxidative polymerization of phenol: Comparison with that of 4-phenoxyphenol
    • Higashimura, H., Fujisawa, K., Kubota, M. & Kobayashi, S. 'Radical-controlled' oxidative polymerization of phenol: Comparison with that of 4-phenoxyphenol. J. Polym. Sci. Polym. Chem. 43, 1955-1962 (2005).
    • (2005) J. Polym. Sci. Polym. Chem , vol.43 , pp. 1955-1962
    • Higashimura, H.1    Fujisawa, K.2    Kubota, M.3    Kobayashi, S.4
  • 66
    • 34547652671 scopus 로고    scopus 로고
    • Copper-catalyzed regio-controlled oxidative coupling polymerization of 2,5-dimethylphenol
    • Shibasaki, Y., Suzuki, Y. & Ueda, M. Copper-catalyzed regio-controlled oxidative coupling polymerization of 2,5-dimethylphenol. Macromolecules 40, 5322-5325 (2007).
    • (2007) Macromolecules , vol.40 , pp. 5322-5325
    • Shibasaki, Y.1    Suzuki, Y.2    Ueda, M.3
  • 67
    • 0001361316 scopus 로고
    • Dioxygen independent oxygenation of hydrocarbons by methane monooxygenase hydroxylase component
    • Andersson, K. K., Froland, W. A., Lee, S.-K. & Lipscomb, J. D. Dioxygen independent oxygenation of hydrocarbons by methane monooxygenase hydroxylase component. New J. Chem. 15, 411-415 (1991).
    • (1991) New J. Chem , vol.15 , pp. 411-415
    • Andersson, K.K.1    Froland, W.A.2    Lee, S.-K.3    Lipscomb, J.D.4
  • 68
    • 0037428401 scopus 로고    scopus 로고
    • Hydrogen peroxide-coupled cis-diol formation catalyzed by naphthalene 1,2-dioxygenase
    • Wolfe, M. D. & Lipscomb, J. D. Hydrogen peroxide-coupled cis-diol formation catalyzed by naphthalene 1,2-dioxygenase. J. Biol. Chem. 278, 829-835 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 829-835
    • Wolfe, M.D.1    Lipscomb, J.D.2
  • 69
    • 18544384019 scopus 로고
    • Oxidation of tartaric acid in the presence of iron
    • Fenton, H. J. H. Oxidation of tartaric acid in the presence of iron. J. Chem. Soc. 65, 889-910 (1894).
    • (1894) J. Chem. Soc , vol.65 , pp. 889-910
    • Fenton, H.J.H.1
  • 71
    • 0141431036 scopus 로고    scopus 로고
    • 2 in protic solvents
    • 2 in protic solvents. J. Org. Chem. 68, 7903-7906 (2007).
    • (2007) J. Org. Chem , vol.68 , pp. 7903-7906
    • Nam, W.1
  • 72
    • 0036407531 scopus 로고    scopus 로고
    • Epoxidation of alkenes with hydrogen peroxide catalyzed by iron(iii) porphyrins in ionic liquids
    • Srinivas, K. A., Kumar, A. & Chauhan, M. S. Epoxidation of alkenes with hydrogen peroxide catalyzed by iron(iii) porphyrins in ionic liquids. Chem. Commun. 2456-2457 (2002).
    • (2002) Chem. Commun , vol.2456-2457
    • Srinivas, K.A.1    Kumar, A.2    Chauhan, M.S.3
  • 73
    • 20944432319 scopus 로고    scopus 로고
    • A study of the mechanism and kinetics of cyclooctene epoxidation catalyzed by iron(iii) tetrakispentafluorophenyl porphyrin
    • Stephenson, N. A. & Bell, A. T. A study of the mechanism and kinetics of cyclooctene epoxidation catalyzed by iron(iii) tetrakispentafluorophenyl porphyrin J. Am. Chem. Soc. 127, 8635-8643 (2005).
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 8635-8643
    • Stephenson, N.A.1    Bell, A.T.2
  • 75
    • 21844455928 scopus 로고    scopus 로고
    • Reaction mechanisms of mononuclear non-heme iron oxygenases
    • Abu-Omar, M. M., Loaiza, A. & Hontzeas, N. Reaction mechanisms of mononuclear non-heme iron oxygenases. Chem. Rev. 105, 2227-2252 (2005).
    • (2005) Chem. Rev , vol.105 , pp. 2227-2252
    • Abu-Omar, M.M.1    Loaiza, A.2    Hontzeas, N.3
  • 76
    • 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
  • 77
    • 0033802342 scopus 로고    scopus 로고
    • Biomimetic nonheme iron catalysts for alkane hydroxylation
    • Costas, M., Chen, K. & Que, L. Jr. Biomimetic nonheme iron catalysts for alkane hydroxylation. Coord. Chem. Rev. 200-202, 517-544 (2000).
    • (2000) Coord. Chem. Rev , vol.200-202 , pp. 517-544
    • Costas, M.1    Chen, K.2    Que Jr., L.3
  • 78
    • 0042205710 scopus 로고    scopus 로고
    • Metal-catalyzed epoxidations of alkenes with hydrogen peroxide
    • Lane, B. S. & Burgess, K. Metal-catalyzed epoxidations of alkenes with hydrogen peroxide. Chem. Rev. 103, 2457-2474 (2003).
    • (2003) Chem. Rev , vol.103 , pp. 2457-2474
    • Lane, B.S.1    Burgess, K.2
  • 79
    • 33747589451 scopus 로고    scopus 로고
    • 2 using biomimetic non-heme iron and manganese oxidation catalysts
    • 2 using biomimetic non-heme iron and manganese oxidation catalysts. Adv. Inorg. Chem. 58, 29-75 (2006).
    • (2006) Adv. Inorg. Chem , vol.58 , pp. 29-75
    • Tanase, S.1    Bouwman, E.2
  • 82
    • 0037181365 scopus 로고    scopus 로고
    • 2 that are catalysed by non-haem iron complexes.
    • 2 that are catalysed by non-haem iron complexes.
  • 85
    • 37549012599 scopus 로고    scopus 로고
    • Iron-catalyzed olefin epoxidation in the presence of acetic acid: Insights into the nature of the metal-based oxidant
    • Mas-Ballesté, R. & Que, L. Jr. Iron-catalyzed olefin epoxidation in the presence of acetic acid: Insights into the nature of the metal-based oxidant J. Am. Chem. Soc. 129, 15964-15972 (2007).
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 15964-15972
    • Mas-Ballesté, R.1    Que Jr., L.2
  • 86
    • 41349092782 scopus 로고    scopus 로고
    • High-valent iron-mediated cis-hydroxyacetoxylation of olefins
    • Mas-Ballesté, R., Fujita, M., Que, L. Jr. High-valent iron-mediated cis-hydroxyacetoxylation of olefins. Dalton Trans. 1828-1830 (2008).
    • (2008) Dalton Trans , vol.1828-1830
    • Mas-Ballesté, R.1    Fujita, M.2    Que Jr., L.3
  • 87
    • 34247100166 scopus 로고    scopus 로고
    • Synthesis and catalytic properties in olefin epoxidation of novel iron(ii) complexes with pyridine-containing macrocycles bearing an aminopropyl pendant arm
    • Taktak, S., Ye, W., Herrera, A. M. & Rybak-Akimova, E. V. Synthesis and catalytic properties in olefin epoxidation of novel iron(ii) complexes with pyridine-containing macrocycles bearing an aminopropyl pendant arm. Inorg. Chem. 46, 2929-2942 (2007).
    • (2007) Inorg. Chem , vol.46 , pp. 2929-2942
    • Taktak, S.1    Ye, W.2    Herrera, A.M.3    Rybak-Akimova, E.V.4
  • 88
    • 40949096433 scopus 로고    scopus 로고
    • A predictably selective aliphatic C-H oxidation reaction for complex molecule synthesis
    • 2 that selectively hydroxylates particular tertiary C-H bonds in complex organic molecules
    • 2 that selectively hydroxylates particular tertiary C-H bonds in complex organic molecules.
    • (2007) Science , vol.318 , pp. 783-787
    • Chen, M.S.1    White, M.C.2
  • 89
    • 33845974070 scopus 로고    scopus 로고
    • An efficient biomimetic Fe-catalyzed epoxidation of olefins using hydrogen peroxide
    • Anilkumar, G., Bitterlich, B., Gelalcha, F. G., Tse, M. K. & Beller, M. An efficient biomimetic Fe-catalyzed epoxidation of olefins using hydrogen peroxide. Chem. Commun. 289-291 (2007).
    • (2007) Chem. Commun , vol.289-291
    • Anilkumar, G.1    Bitterlich, B.2    Gelalcha, F.G.3    Tse, M.K.4    Beller, M.5
  • 90
    • 34948835849 scopus 로고    scopus 로고
    • Iron-catalyzed asymmetric epoxidation of aromatic alkenes using hydrogen peroxide
    • This paper reports the highest enantioselectivity so far for the epoxidation of an alkene by a non-haem iron catalyst
    • Gelalcha, F. G., Bitterlich, B., Anilkumar, A., Tse, M. K. & Beller, M. Iron-catalyzed asymmetric epoxidation of aromatic alkenes using hydrogen peroxide. Angew. Chem. Int. Edn Engl. 46, 7293-7296 (2007). This paper reports the highest enantioselectivity so far for the epoxidation of an alkene by a non-haem iron catalyst.
    • (2007) Angew. Chem. Int. Edn Engl , vol.46 , pp. 7293-7296
    • Gelalcha, F.G.1    Bitterlich, B.2    Anilkumar, A.3    Tse, M.K.4    Beller, M.5
  • 91
    • 41949125347 scopus 로고    scopus 로고
    • Suzuki, K., Oldenburg, P. D. & Que, L. Jr. Iron-catalyzed asymmetric olefin cis-dihydroxylation with 97% enantiomeric excess. Angew. Chem. Int. Edn Engl. 47, 1887-1889 (2008). This paper reports the highest enantioselectivity so far for the cis-dihydroxylation of an alkene by a non-haem iron catalyst.
    • Suzuki, K., Oldenburg, P. D. & Que, L. Jr. Iron-catalyzed asymmetric olefin cis-dihydroxylation with 97% enantiomeric excess. Angew. Chem. Int. Edn Engl. 47, 1887-1889 (2008). This paper reports the highest enantioselectivity so far for the cis-dihydroxylation of an alkene by a non-haem iron catalyst.
  • 92
    • 0037048608 scopus 로고    scopus 로고
    • Manganese-catalyzed epoxidations of alkenes in bicarbonate solutions
    • Lane, B. S., Vogt, M., DeRose, V. J. & Burgess, K. Manganese-catalyzed epoxidations of alkenes in bicarbonate solutions. J. Am. Chem. Soc.124, 11946-11954 (2002).
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 11946-11954
    • Lane, B.S.1    Vogt, M.2    DeRose, V.J.3    Burgess, K.4
  • 93
    • 20444417131 scopus 로고    scopus 로고
    • 2-efficient catalyst
    • 2-efficient catalyst. J. Am. Chem. Soc. 127, 7990-7991 (2005).
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 7990-7991
    • de Boer, J.W.1
  • 94
    • 34548029175 scopus 로고    scopus 로고
    • 2 efficient dinuclear manganese catalysts
    • 2 efficient dinuclear manganese catalysts. Inorg. Chem. 46, 6353-6372 (2007).
    • (2007) Inorg. Chem , vol.46 , pp. 6353-6372
    • de Boer, J.W.1
  • 95
    • 44349133404 scopus 로고    scopus 로고
    • 2 at relatively mild temperatures (<100 °C).
    • 2 at relatively mild temperatures (<100 °C).
  • 96
    • 0036739958 scopus 로고    scopus 로고
    • 2 activation in the treatment of waste water from paper and textile mills.
    • 2 activation in the treatment of waste water from paper and textile mills.
  • 97
    • 44149085893 scopus 로고    scopus 로고
    • IV=O complex in aqueous solution: Synthesis and spectroscopic and computational characterization
    • IV=O complex in aqueous solution: Synthesis and spectroscopic and computational characterization. Inorg. Chem. 47, 3669-3678 (2008).
    • (2008) Inorg. Chem , vol.47 , pp. 3669-3678
    • Chanda, A.1
  • 99
    • 34547752024 scopus 로고    scopus 로고
    • Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase
    • Balasubramanian, R. & Rosenzweig, A. Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase. Acc. Chem. Res. 40, 573-580 (2007).
    • (2007) Acc. Chem. Res , vol.40 , pp. 573-580
    • Balasubramanian, R.1    Rosenzweig, A.2


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