[1] Jobling S, Reynolds T, White R, et al. A variety of environmentally persistent chemicals, including some phthalate plastivizers, are weakly estrogenic. Environmental Health Perspectives, 1995, 103(6): 582-587.
[2] Daughton C G, Ternes T A. Pharmaceuticals and personal care products in the environment: Agents of subtle change? Environmental Health Perspectives, 1999, 107(Suppl 6): 907-938.
[3] Gogate P R, Pandit A B. A review of imperative technologies for wastewater treatment I: oxidation technologies at ambient conditions. Advances in Environmental Research, 2004, 8(3-4): 501-551.
[4] Banat I M, Nigam P, Singh D, et al. Microbial decolorization of textile-dye-containing effluents: a review. Bioresource Technology, 1996, 58 (3): 217-227.
[5] Pera-Titus M, Garcia-Molina V, Banos M A, et al. Degradation of chlorophenols by means of advanced oxidation processes: a general review. Applied Catalysis B: Environmental, 2004, 47(4): 219-256;
[6] Klavarioti M, Mantzavinos D, Kassinos D. Removal of residual pharmaceuticals from aqueous systems by advanced oxidation processes. Environment International, 2009, 35(2): 402-417.
[7] Jiang J, Pang S Y, Ma J. Oxidation of triclosan by permanganate (Mn(VII)): Importance of ligands and in situ formed manganese oxides. Environmental Science & Technology, 2009, 43(21): 8326-8331.
[8] Kasprzyk-Hordern B, Ziolek M, Nawrocki J. Catalytic ozonation and methods of enhancing molecular ozone reactions in water treatment. Applied Catalysis B: Environmental, 2003, 46(4): 639-669;
[9] Ternes T A, Stuber J, Herrmann N, et al. Ozonation: a tool for removal of pharmaceuticals, contrast media and musk fragrances from wastewater? Water Research, 2003, 37(8): 1976-1982.
[10] Yang X, Guo W H, Zhang X, et al. Formation of disinfection by-products after pre-oxidation with chlorine dioxide or ferrate. Water Research, 2013, 47(15): 5856-5864.
[11] Wenk J, Aeschbacher M, Salhi E, et al. Chemical oxidation of dissolved organic matter by chlorine dioxide, chlorine, and ozone: effects on its optical and antioxidant properties. Environmental Science & Technology, 2013, 47(19): 11147-11156.
[12] Pignatello J J, Oliveros E, MacKay A. Advanced oxidation processes for organic contaminant destruction based on the Fenton reaction and related chemistry. Critical Reviews in Environmental Science and Technology, 2006, 36(1): 1-84.
[13] Neyens E, Baeyens J. A review of classic Fenton’s peroxidation as an advanced oxidation technique. Journal of Hazardous Materials, 2003, 98(1-3): 33-50.
[14] Magario I, Einschlag F S G, Rueda E H, et al. Mechanisms of radical generation in the removal of phenol derivatives and pigments using different Fe-based catalytic systems. Journal of Molecular Catalysis A: Chemical, 2012, 352: 1-20.
[15] Wang Q, Yang Z, Zhang X, et al. A supramolecular-hydrogel-encapsulated hemin as an artificial enzyme to mimic peroxidase. Angewandte Chemie-International Edition, 2007, 46(23): 4285-4289.
[16] Takahashi A, Kurahashi T, Fujii H. Effect of imidazole and phenolate axial ligands on the electronic structure and reactivity of oxoiron (IV) porphyrin π-cation radical complexes: drastic increase in oxo-transfer and hydrogen abstraction reactivities. Inorganic Chemistry, 2009, 48(6): 2614-2625.
[17] Breslow R. Biomimetic chemistry and artificial enzymes: catalysis by design. Accounts of Chemical Research, 1995, 28(3): 146-153.
[18] Strong P J, Claus H. Laccase: A review of its past and its future in bioremediation. Critical Reviews in Environmental Science and Technology, 2011, 41(4): 373-434.
[19] Veitch N C. Horseradish peroxidase: a modern view of a classic enzyme. Phytochemistry, 2004, 65(3): 249-259.
[20] Capaldi R A. Structure and function of cytochrome-C oxidase. Annual Review of Biochemistry, 1990, 59: 569-596.
[21] Sono M, Roach M P, Coulter E D, et al. Heme-containing oxygenases. Chemical Review, 1996, 96(7): 2841-2888.
[22] Solomon E I, Sundaram U M, Machonkin T E. Multicopper oxidases and oxygenases. Chemical Review, 1996, 96(7): 2563-2606.
[23] Meunier B, De Visser S P, Shaik S. Mechanism of oxidation reactions catalyzed by cytochrome P450 enzymes. Chemical Review, 2004, 104(9): 3947-3980.
[24] Solomon E I, Ginsbach J W, Heppner D E, et al. Copper dioxygen (bio)inorganic chemistry. Faraday Discussions, 2011, 148(0): 11-39.
[25] Kjaergaard C H, Durand F, Tasca F, et al. Spectroscopic and crystallographic characterization of “alternative resting” and “resting oxidized” enzyme forms of bilirubin oxidase: implications for activity and electrochemical behavior of multicopper oxidases. Journal of the American Chemical Society, 2012, 134(12): 5548-5551.
[26] Magnus K A, Hazes B, Ton-That H, et al. Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences. Proteins: Structure, Function, and Bioinformatics, 1994, 19(4): 302-309.
[27] Messerschmidt A, Luecke H, Huber R. X-ray structures and mechanistic implications of three functional derivatives of ascorbate oxidase from zucchini: Reduced, peroxide and azide forms. Journal of molecular biology, 1993, 230(3): 997-1014.
[28] Lowery M D, Guckert J A, Gebhard M S, et al. Active-site electronic structure contributions to electron-transfer pathways in rubredoxin and plastocyanin: direct versus superexchange. Journal of the American Chemical Society, 1993, 115(7): 3012-3013.
[29] Xu F, Shin W, Brown S H, et al. A study of a series of recombinant fungal laccases and bilirubin oxidase that exhibit significant differences in redox potential, substrate specificity, and stability. Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology, 1996, 1292(2): 303-311.
[30] Augustine A J, Kjaergaard C, Qayyum M, et al. Systematic perturbation of the trinuclear copper cluster in the multicopper oxidases: the role of active site asymmetry in its reduction of O2 to H2O. Journal of the American Chemical Society, 2010, 132(17): 6057-6067.
[31] Solomon E I, Augustine A J, Yoon J. O2 reduction to H2O by the multicopper oxidases. Dalton Transactions, 2008, (30): 3921-3932.
[32] Woertink J S, Tian L, Maiti D, et al. Spectroscopic and computational studies of an end-on bound superoxo-Cu(II) complex: geometric and electronic factors that determine the ground state. Inorganic Chemistry, 2010, 49(20): 9450-9459.
[33] Shin W, Sundaram U M, Cole J L, et al. Chemical and spectroscopic definition of the peroxide-level intermediate in the multicopper oxidases: Relevance to the catalytic mechanism of dioxygen reduction to water. Journal of the American Chemical Society, 1996, 118(13): 3202-3215.
[34] Yoon J, Fujii S, Solomon E I. Geometric and electronic structure differences between the type 3 copper sites of the multicopper oxidases and hemocyanin/tyrosinase. Proceedings of the National Academy of Sciences, 2009, 106(16): 6585-6590.
[35] Solomon E I, Chen P, Metz M, et al. Oxygen binding, activation, and reduction to water by copper proteins. Angewandte Chemie-International Edition, 2001, 40(24): 4570-4590.
[36] Cole J L, Tan G O, Yang E K, et al. Reactivity of the laccase trinuclear copper active site with dioxygen: an X-ray absorption Edge Study. Journal of the American Chemical Society, 1990, 112(6): 2243-2249.
[37] Clark P A, Solomon E I. Magnetic circular dichroism spectroscopic definition of the intermediate produced in the reduction of dioxygen to water by native laccase. Journal of the American Chemical Society, 1992, 114(3): 1108-1110.
[38] Bach R D, Ayala P Y, Schlegel H. A reassessment of the bond dissociation energies of peroxides. An ab initio study. Journal of the American Chemical Society, 1996, 118(50): 12758-12765.
[39] Farver O, Pecht I. Low activation barriers characterize intramolecular electron transfer in ascorbate oxidase. Proceedings of the National Academy of Sciences, 1992, 89(17): 8283-8287.
[40] Kyritsis P, Messerschmidt A, Huber R, et al. Pulse-radiolysis studies on the oxidised form of the multicopper enzyme ascorbate oxidase: evidence for two intramolecular electron-transfer steps. Journal of the Chemical Society, Dalton Transactions. 1993, (5): 731-735.
[41] Shul’pin G B. Metal-catalyzed hydrocarbon oxygenations in solutions: The dramatic role of additives: a review. Journal of Molecular Catalysis A: Chemical, 2002, 189(1): 39-66.
[42] Abu-Omar M M, Loaiza A, Hontzeas N. Reaction Mechanisms of Mononuclear Non-Heme Iron Oxygenases. Chemical Review, 2005, 105(6): 2227-2252.
[43] Denisov I G, Makris T M, Sligar S G, et al. Structure and Chemistry of Cytochrome P450. Chemical Review, 2005, 105(6): 2253-2278.
[44] Veitch N C. Horseradish peroxidase: a modern view of a classic enzyme. Phytochemistry, 2004, 65(3): 249-259.
[45] Howes B D, Feis A, Raimondi L, et al. The critical role of the proximal calcium ion in the structural properties of horseradish peroxidase. Journal of Biological Chemistry, 2001, 276(44): 40704-40711.
[46] Dawson J, Holm R, Trudell J, et al. Letter: Oxidized cytochrome P-450. Magnetic circular dichroism evidence for thiolate ligation in the substrate-bound form. Implications for the catalytic mechanism. Journal of the American Chemical Society, 1976, 98(12), 3707-8.
[47] Pylypenko O, Vitali F, Zerbe K, et al. Crystal structure of OxyC, a cytochrome P450 implicated in an oxidative C-C coupling reaction during vancomycin biosynthesis. Journal of Biological Chemistry, 2003, 278(47): 46727-46733.
[48] Halime Z, Kotani H, Li Y, et al. Homogeneous catalytic O2 reduction to water by a cytochrome C oxidase model with trapping of intermediates and mechanistic insights. Proceedings of the National Academy of Sciences, 2011, 108(34): 13990-13994.
[49] Gómez J L, Bódalo A Gómez E, et al. A new method to estimate intrinsic parameters in the ping-pong bisustrate kinetic: Application to the oxipolymerization of phenol. American Journal of Biochemistry and Biotechnology, 2005, 1(2): 115-120.
[50] Berglund G I, Carlsson G H, Smith A T, et al. The catalytic pathway of horseradish peroxidase at high resolution. Nature, 2002, 417(6887): 463-468.
[51] Rodríguez-López J N, Lowe D J, Hernández-Ruiz J, et al. Mechanism of reaction of hydrogen peroxide with horseradish peroxidase: identification of intermediates in the catalytic cycle. Journal of the American Chemical Society, 2001, 123(48): 11838-11847.
[52] Yamaguchi K, Watanabe Y, Morishima I. Direct observation of the push effect on the oxygen-oxygen bond cleavage of acylperoxoiron(III) porphyrin complexes. Journal of the American Chemical Society, 1993, 115(10): 4058-4065.
[53] Dawson J H. Probing structure-function relations in heme-containing oxygenases and peroxidases. Science, 1988, 240(4851): 433-439.
[54] Momenteau M, Reed C A. Synthetic heme-dioxygen complexes. Chemical Review, 1994, 94(3): 659-698.
[55] Groves J T. The bioinorganic chemistry of iron in oxygenases and supramolecular assemblies. Proceedings of the National Academy of Sciences, 2003, 100(7): 3569-3574.
[56] Guengerich F P. Mechanisms of cytochrome P450 substrate oxidation: MiniReview. Journal of Biochemical and Molecular Toxicology, 2007, 21(4): 163-168.
[57] Guengerich F. Reactions and significance of cytochrome P-450 enzymes. Journal of Biological Chemistry, 1991, 266(16): 10019-10022.
[58] Stillman M. Formation and electronic properties of ring-oxidized and ring-reduced radical species of the phthalocyanines and porphyrins. Journal of Porphyrins and Phthalocyanines, 2000, 4(4): 374-376.
[59] Fukuzumi S. Electron transfer chemistry of metalloporphyrins and related metal complexes. Journal of Porphyrins and Phthalocyanines, 2000, 4(4): 398-400.
[60] Dey A, Jiang Y, Ortiz de Montellano P, et al. S K-edge XAS and DFT calculations on cytochrome P450: covalent and ionic contributions to the cysteine-Fe bond and their contribution to reactivity. Journal of the American Chemical Society, 2009, 131(22): 7869-7878.
[61] Auclai K, Moënne-Loccoz P, Ortiz de Montellano P R. Roles of the proximal heme thiolate ligand in cytochrome P450cam. Journal of the American Chemical Society, 2001, 123(21): 4877-4885.
[62] Solomon E I, Brunold T C, Davis M I, et al. Geometric and electronic structure/function correlations in non-heme iron enzymes. Chemical Review, 1999, 100(1): 235-350.
[63] Boerjan W, Ralph J, Baucher M. Lignin biosynthesis. Annual Review of Plant Biology, 2003, 54(1): 519-546.
[64] Romano M, Clària J. Cyclooxygenase-2 and 5-lipoxygenase converging functions on cell proliferation and tumor angiogenesis: implications for cancer therapy. The FASEB Journal, 2003, 17(14): 1986-1995.
[65] Broderick J. Catechol dioxygenases. Essays in Biochemistry, 1999, 34: 173-189.
[66] Sato N, Uragami Y, Nishizaki T, et al. Crystal structures of the reaction intermediate and its homologue of an extradiol-cleaving catecholic dioxygenase. Journal of Molecular Biology, 2002, 321(4): 621-636.
[67] Sanvoisin J, Langley G J, Bugg T D. Mechanism of extradiol catechol dioxygenases: Evidence for a lactone intermediate in the 2,3-dihydroxyphenylpropionate 1,2-dioxygenase reaction. Journal of the American Chemical Society, 1995, 117(29): 7836-7837.
[68] Kovaleva E G, Lipscomb J D. Versatility of biological non-heme Fe(II) centers in oxygen activation reactions. Nature Chemical Biology, 2008, 4(3): 186-193.
[69] Hausinger R P. Fe(II)/α-ketoglutarate-dependent hydroxylases and related enzymes. Critical Reviews in Biochemistry and Molecular Biology, 2004, 39(1): 21-68.
[70] Costas M, Mehn M P, Jensen M P, et al. Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates. Chemical Review, 2004, 104(2): 939-986.
[71] Hanauske-Abel H M, Popowicz A M. The HAG mechanism: a molecular rationale for the therapeutic application of iron chelators in human diseases involving the 2-oxoacid utilizing dioxygenases. Current Medicinal Chemistry, 2003, 10(12): 1005-1019.
[72] Kryatov S V, Rybak-Akimova E V, Schindler S. Kinetics and mechanisms of formation and reactivity of non-heme iron oxygen intermediates. Chemical Review, 2005, 105(6): 2175-2226.
[73] Krajewska B. Application of chitin- and chitosan-based materials for enzyme immobilizations: a review. Enzyme and Microbial Technology, 2004, 35(2-3): 126-139.
[74] Groothaert M H, Smeets P J, Sels B F, et al. Selective oxidation of methane by the bis (μ-oxo) dicopper core stabilized on ZSM-5 and mordenite zeolites. Journal of the American Chemical Society, 2005, 127(5): 1394-1395.
[75] Smeets P J, Hadt R G, Woertink J S, et al. Oxygen precursor to the reactive intermediate in methanol synthesis by Cu-ZSM-5. Journal of the American Chemical Society, 2010, 132(42): 14736-14738.
[76] Woertink J S, Smeets P J, Groothaert M H, et al. A [Cu2O]2+ core in Cu-ZSM-5, the active site in the oxidation of methane to methanol. Proceedings of the National Academy of Sciences, 2009, 106(45): 18908-18913.
[77] Vanelderen P, Hadt R G, Smeets P J, et al. Cu-ZSM-5: A biomimetic inorganic model for methane oxidation. Journal of Catalysis 2011, 284(2): 157-164.
[78] Almarsson O, Bruice T C. A homolytic mechanism of O-O bond scission prevails in the reactions of alkyl hydroperoxides with an octacationic tetraphenylporphinato-iron(III) complex in aqueous solution. Journal of the American Chemical Society, 1995, 117(16): 4533-4544.
[79] Christoforidis K C, Louloudi M, Deligiannakis Y. Complete dechlorination of pentachlorophenol by a heterogeneous SiO2-Fe-porphyrin catalyst. Applied Catalysis B: Environmental, 2010, 95(3): 297-302.
[80] Cho J, Jeon S, Wilson S A, et al. Structure and reactivity of a mononuclear non-haem iron(III)–peroxo complex. Nature, 2011, 478(7370): 502-505.
[81] Cho J, Sarangi R, Kang H Y, et al. Synthesis, structural, and spectroscopic characterization and reactivities of mononuclear cobalt(III)-peroxo complexes. Journal of the American Chemical Society, 2010, 132(47): 16977-16986.
[82] Bedioui F. Zeolite-encapsulated and clay-intercalated metal porphyrin, phthalocyanine and Schiff-base complexes as models for biomimetic oxidation catalysts: an overview. Coordination Chemistry Reviews, 1995, 144(0): 39-68.
[83] Nazari K, Shokrollahzadeh S, Mahmoudi A, et al. Iron(III)protoporphyrin/MCM41 catalyst as a peroxidase enzyme model: Preparation and typical test reactions. Journal of Molecular Catalysis A: Chemical, 2005, 239(1-2): 1-9.
[84] Novoselov K S, Geim A K, Morozov S V, et al. Electric field effect in atomically thin carbon films. Science, 2004, 306(5696): 666-669.
[85] Geim A K. Graphene: status and prospects. Science, 2009, 324(5934): 1530-1534.
[86] Xue T, Jiang S, Qu Y, et al. Graphene-supported hemin as a highly active biomimetic oxidation catalyst. Angewandte Chemie 2012, 124(16): 3888-3891.
[87] Itoh T, Yamada T, Kodera Y, et al. Hemin (Fe3+)- and heme (Fe2+)-smectite conjugates as a model of hemoprotein based on spectrophotometry. Bioconjugate Chemistry, 2001, 12(1): 3-6.
[88] Kurosawa M, Itoh T, Kodera Y, et al. Formation of a bioconjugate composed of hemin, smectite, and quaternary ammonium chloride that is soluble and active in hydrophobic media. Bioconjugate Chemistry, 2002, 13(2): 167-171.