Complex reactions catalyzed by cytochrome P450 enzymes
Cytochrome P450 (P450) enzymes are some of the most versatile redox proteins known. The basic P450 reactions include C-hydroxylation, heteroatom oxygenation, heteroatom release (dealkylation), and epoxide formation. Mechanistic explanations for these reactions have been advanced. A number of more co...
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| Published in | Biochimica et biophysica acta Vol. 1770; no. 3; pp. 314 - 329 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
01.03.2007
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Cytochrome P450 (P450) enzymes are some of the most versatile redox proteins known. The basic P450 reactions include C-hydroxylation, heteroatom oxygenation, heteroatom release (dealkylation), and epoxide formation. Mechanistic explanations for these reactions have been advanced. A number of more complex P450 reactions also occur, and these can be understood largely in the context of the basic chemical mechanisms and subsequent rearrangements. The list discussed here updates a 2001 review and includes chlorine oxygenation, aromatic dehalogenation, formation of diindole products, dimer formation via Diels–Alder reactions of products, ring coupling and also ring formation, reductive activation (e.g., aristolochic acid), ring contraction (piperidine nitroxide radical), oxidation of troglitazone, cleavage of amino oxazoles and a 1,2,4-oxadiazole ring, bioactivation of a dihydrobenzoxathiin, and oxidative aryl migration. |
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| AbstractList | Cytochrome P450 (P450) enzymes are some of the most versatile redox proteins known. The basic P450 reactions include C-hydroxylation, heteroatom oxygenation, heteroatom release (dealkylation), and epoxide formation. Mechanistic explanations for these reactions have been advanced. A number of more complex P450 reactions also occur, and these can be understood largely in the context of the basic chemical mechanisms and subsequent rearrangements. The list discussed here updates a 2001 review and includes chlorine oxygenation, aromatic dehalogenation, formation of diindole products, dimer formation via Diels-Alder reactions of products, ring coupling and also ring formation, reductive activation (e.g., aristolochic acid), ring contraction (piperidine nitroxide radical), oxidation of troglitazone, cleavage of amino oxazoles and a 1,2,4-oxadiazole ring, bioactivation of a dihydrobenzoxathiin, and oxidative aryl migration.Cytochrome P450 (P450) enzymes are some of the most versatile redox proteins known. The basic P450 reactions include C-hydroxylation, heteroatom oxygenation, heteroatom release (dealkylation), and epoxide formation. Mechanistic explanations for these reactions have been advanced. A number of more complex P450 reactions also occur, and these can be understood largely in the context of the basic chemical mechanisms and subsequent rearrangements. The list discussed here updates a 2001 review and includes chlorine oxygenation, aromatic dehalogenation, formation of diindole products, dimer formation via Diels-Alder reactions of products, ring coupling and also ring formation, reductive activation (e.g., aristolochic acid), ring contraction (piperidine nitroxide radical), oxidation of troglitazone, cleavage of amino oxazoles and a 1,2,4-oxadiazole ring, bioactivation of a dihydrobenzoxathiin, and oxidative aryl migration. Cytochrome P450 (P450) enzymes are some of the most versatile redox proteins known. The basic P450 reactions include C-hydroxylation, heteroatom oxygenation, heteroatom release (dealkylation), and epoxide formation. Mechanistic explanations for these reactions have been advanced. A number of more complex P450 reactions also occur, and these can be understood largely in the context of the basic chemical mechanisms and subsequent rearrangements. The list discussed here updates a 2001 review and includes chlorine oxygenation, aromatic dehalogenation, formation of diindole products, dimer formation via Diels–Alder reactions of products, ring coupling and also ring formation, reductive activation (e.g., aristolochic acid), ring contraction (piperidine nitroxide radical), oxidation of troglitazone, cleavage of amino oxazoles and a 1,2,4-oxadiazole ring, bioactivation of a dihydrobenzoxathiin, and oxidative aryl migration. |
| Author | Isin, Emre M. Guengerich, F. Peter |
| Author_xml | – sequence: 1 givenname: Emre M. surname: Isin fullname: Isin, Emre M. – sequence: 2 givenname: F. Peter surname: Guengerich fullname: Guengerich, F. Peter email: f.guengerich@vanderbilt.edu |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/17239540$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1021/ja00154a008 10.1074/jbc.272.47.29643 10.1021/ja962466g 10.1021/tx0500373 10.1021/ja981990f 10.1073/pnas.80.21.6680 10.1021/cr030722j 10.1517/17425255.1.1.91 10.1016/S0021-9258(18)82162-7 10.1021/ja00483a042 10.1021/ja0171963 10.1016/S0003-9861(02)00445-9 10.1021/ja012185v 10.1093/carcin/18.5.1063 10.1517/17425255.2.1.27 10.1021/bi9719399 10.1093/carcin/15.6.1187 10.1021/tx010059z 10.1093/pcp/pce018 10.1021/ja0455188 10.1021/bi00293a005 10.1126/science.287.5458.1615 10.1074/jbc.M502632200 10.1093/oxfordjournals.jbchem.a131990 10.1021/tx049711r 10.1021/ja974367o 10.1074/jbc.M411019200 10.1146/annurev.arplant.54.031902.134921 10.1073/pnas.96.14.7831 10.1016/S0090-9556(24)14927-6 10.1016/S0021-9258(18)71478-6 10.1021/ja044716w 10.1016/j.bbrc.2005.08.091 10.1021/bi00180a039 10.1021/ja038237t 10.1105/tpc.105.033738 10.1074/jbc.M410933200 10.1038/nsmb971 10.1074/jbc.M206342200 10.1002/1521-3773(20000602)39:11<2003::AID-ANIE2003>3.0.CO;2-M 10.1021/ja00021a044 10.1016/0041-008X(80)90092-7 10.1021/tx025599q 10.1021/tx0496789 10.1016/S0021-9258(18)94132-3 10.1021/bi035944q 10.1021/tx000180q 10.1006/abbi.2001.2511 10.1016/S0021-9258(17)31235-8 10.1073/pnas.95.7.3555 10.1021/ja981157i 10.1002/rcm.1555 10.1124/dmd.32.1.49 10.1021/bi952081v 10.1021/tx0500427 10.1016/0014-5793(90)80410-K 10.1021/tx0002583 10.1021/ar00097a002 10.1021/ja01529a060 10.1021/tx015574b 10.1074/jbc.M306486200 10.1074/jbc.M203762200 10.1002/anie.200461278 10.1021/bi001229u 10.1021/bi0491393 10.2174/1389200054021799 10.1074/jbc.M508182200 10.1046/j.1365-2044.2003.02960.x 10.1515/BC.2002.175 10.1128/JB.187.23.8149-8155.2005 10.1021/ja01042a028 |
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| References | Hackett, Brueggemeier, Hadad (bib25) 2005; 127 Doss, Miller, Zhang, Teffera, Nargund, Palucki, Park, Tang, Evans, Baillie, Stearns (bib57) 2005; 18 He, Cryle, De Voss, de Montellano (bib36) 2005; 280 Gillam, Notley, Cai, DeVoss, Guengerich (bib40) 2000; 39 Ha-Duong, Marques-Soares, Dijols, Sari, Dansette, Mansuy (bib48) 2001; 394 Kalgutkar, Gardner, Obach, Shaffer, Callegari, Henne, Mutlib, Dalvie, Lee, Nakai, O'Donnell, Boer, Harriman (bib30) 2005; 6 Yun, Kim, Calcutt, Guengerich (bib10) 2005; 280 Zerbe, Woithe, Li, Vitali, Bigler, Robinson (bib53) 2004; 43 Lamb, Guengerich, Kelly, Waterman (bib3) 2006; 2 Guengerich (bib4) 2002; 383 Newcomb, Le Tadic-Biadatti, Chestney, Roberts, Hollenberg (bib21) 1995; 117 Kalgutkar, Soglia (bib29) 2005; 1 Ogliaro, de Visser, Cohen, Sharma, Shaik (bib18) 2002; 124 Cole, Robinson (bib24) 1991; 113 Funa, Funabashi, Ohnishi, Horinouchi (bib49) 2005; 187 Chen, Christopher, Jones, Bell, Guo, Xu, Rao, Wong (bib38) 2002; 277 Yin, Mitra, Stearns, Baillie, Kumar (bib65) 2004; 43 Schlichting, Berendzen, Chu, Stock, Maves, Benson, Sweet, Ringe, Petsko, Sligar (bib7) 2000; 287 Liebler, Guengerich (bib82) 1983; 22 Reddy, Karanam, Gruber, Wallace, Vincent, Franklin, Baillie (bib69) 2005; 18 Kim, Hwang, Kim, Joo, Chang, Lee, Takatsuto, Kim (bib78) 2005; 17 Guengerich (bib12) 2001; 14 Yano, Hsu, Griffin, Stout, Johnson (bib42) 2005; 12 Reich, Peake (bib37) 1978; 100 Poulos, Johnson (bib8) 2005 Tang, Subramanian, Kuo, Krymgold, Lu, Kuduk, Ng, Feng, Elmore, Soli, Ho, Bock, Baillie, Prueksaritanont (bib58) 2005; 18 Guengerich (bib35) 1989; 264 Bell, Guengerich (bib6) 1997; 272 Zerbe, Pylypenko, Vitali, Zhang, Rouset, Heck, Vrijbloed, Bischoff, Bister, Sussmuth, Pelzer, Wohlleben, Robinson, Schlichting (bib2) 2002; 277 Guengerich, Krauser, Johnson (bib5) 2004; 43 Dalvie, O'Connell (bib46) 2004; 32 Bieler, Stiborova, Wiessler, Cosyns, deStrihou, Schmeiser (bib62) 1997; 18 Fujioka, Yokota (bib79) 2003; 54 Treiber, Dansette, El Amri, Girault, Ginderow, Mornon, Mansuy (bib44) 1997; 119 Henry, Townsend (bib76) 2005; 127 Walsh (bib75) 1979 Chandrasena, Vatsis, Coon, Hollenberg, Newcomb (bib17) 2004; 126 Bondon, Macdonald, Harris, Guengerich (bib32) 1989; 264 Chang, Boeglin, Guengerich, Brash (bib27) 1996; 35 Maurer, Kleff (bib71) 1988; 38 Shaik, Kumar, de Visser, Altun, Thiel (bib15) 2005; 105 Ortiz de Montellano (bib84) 1986 Lee, La, Ahn, Jeong, Kim (bib55) 2004; 18 Akhtar, Corina, Miller, Shyadehi, Wright (bib23) 1994; 33 Zhao, Guengerich, Bellamine, Lamb, Izumikawa, Funa, Lei, Podust, Sundamoorthy, Reddy, Kelly, Stec, Voehler, Falck, Moore, Shimada, Waterman (bib50) 2005; 280 Kassahun, Pearson, Tang, McIntosh, Leung, Elmore, Dean, Wang, Doss, Baillie (bib67) 2001; 14 Guengerich, Johnson (bib9) 1997; 36 Dalvie, Kalgutkar, Khojasteh-Bakht, Obach, O'Donnell (bib28) 2002; 15 Egger, Itterly, John, Rodebaugh, Shimanskas, Stancato, Kapoor (bib56) 1988; 16 Yabuki, Shono, Nakatsuka, Yoshitake (bib72) 1993; 21 Zenk, Gerardy, Stadler (bib51) 1989; 22 Fukushima, Kim, Iyanagi, Oae (bib31) 1978; 83 Bishop, Yokota (bib80) 2001; 42 Toy, Newcomb, Coon, Vaz (bib16) 1998; 120 Watanabe, Townsend (bib77) 1998; 120 Hartmann, Hultschig, Eisenreich, Fuchs, Bacher, Ghisla (bib39) 1999; 96 Chae, Thomas, Guengerich, Fu, El-Bayoumy (bib64) 1999; 59 Marchetti, Mattalia, Bergesi (bib70) 1973; 23 Guengerich, Macdonald (bib11) 1984; 17 Hashim, Hakamatsuka, Ebizuka, Sankawa (bib81) 1990; 271 Hecker, Ullrich (bib26) 1989; 264 Dansette, Bertho, Mansuy (bib47) 2005; 338 Reilly, Ehlhardt, Jackson, Kulanthaivel, Mutlib, Espina, Moody, Crouch, Yost (bib59) 2003; 16 Guengerich, Crawford, Domoradzki, Macdonald, Watanabe (bib33) 1980; 55 Pylypenko, Vitali, Zerbe, Robinson, Schlichting (bib52) 2003; 278 Seto, Guengerich (bib66) 1993; 268 Bradshaw, Conrad, Corey, Gunsalus, Lednicer (bib1) 1959; 81 Harris, Cohen, Filatov, Ogliaro, Shaik (bib14) 2000; 39 Kam, Nethery (bib45) 2003; 58 Stiborova, Frei, Wiessler, Schmeiser (bib63) 2001; 14 Burka, Plucinski, Macdonald (bib34) 1983; 80 Toy, Newcomb, Hollenberg (bib22) 1998; 120 Udwary, Casillas, Townsend (bib74) 2002; 124 Russell, Kaupp (bib43) 1969; 91 Stiborova, Fernando, Schmeiser, Frei, Pfau, Wiessler (bib61) 1994; 15 Gordon, Huitric, Seth, McClanahan, Nelson (bib54) 1987; 15 Yamazaki, Shibata, Suzuki, Nakajima, Shimada, Guengerich, Yokoi (bib68) 1999; 27 Wu, Podust, Guengerich (bib41) 2005; 280 Vaz, McGinnity, Coon (bib20) 1998; 95 Zhang, Chen, Li, Doss, Dean, Ngui, Silva Elipe, Kim, Wu, Dininno, Hammond, Stearns, Evans, Baillie, Tang (bib73) 2005; 18 Newcomb, Hollenberg, Coon (bib19) 2003; 409 Ortiz de Montellano (bib83) 1995 Ortiz De Montellano, De Voss (bib13) 2005 Baek, Kim, Myung, Yim, Jeong, Kim (bib60) 2001; 29 Udwary (10.1016/j.bbagen.2006.07.003_bib74) 2002; 124 Schlichting (10.1016/j.bbagen.2006.07.003_bib7) 2000; 287 Yun (10.1016/j.bbagen.2006.07.003_bib10) 2005; 280 Toy (10.1016/j.bbagen.2006.07.003_bib16) 1998; 120 Shaik (10.1016/j.bbagen.2006.07.003_bib15) 2005; 105 Ha-Duong (10.1016/j.bbagen.2006.07.003_bib48) 2001; 394 Newcomb (10.1016/j.bbagen.2006.07.003_bib21) 1995; 117 Guengerich (10.1016/j.bbagen.2006.07.003_bib9) 1997; 36 Zhang (10.1016/j.bbagen.2006.07.003_bib73) 2005; 18 Marchetti (10.1016/j.bbagen.2006.07.003_bib70) 1973; 23 Guengerich (10.1016/j.bbagen.2006.07.003_bib4) 2002; 383 Zenk (10.1016/j.bbagen.2006.07.003_bib51) 1989; 22 Guengerich (10.1016/j.bbagen.2006.07.003_bib11) 1984; 17 Maurer (10.1016/j.bbagen.2006.07.003_bib71) 1988; 38 He (10.1016/j.bbagen.2006.07.003_bib36) 2005; 280 Guengerich (10.1016/j.bbagen.2006.07.003_bib12) 2001; 14 Zhao (10.1016/j.bbagen.2006.07.003_bib50) 2005; 280 Hashim (10.1016/j.bbagen.2006.07.003_bib81) 1990; 271 Akhtar (10.1016/j.bbagen.2006.07.003_bib23) 1994; 33 Hackett (10.1016/j.bbagen.2006.07.003_bib25) 2005; 127 Dalvie (10.1016/j.bbagen.2006.07.003_bib28) 2002; 15 Gillam (10.1016/j.bbagen.2006.07.003_bib40) 2000; 39 Kam (10.1016/j.bbagen.2006.07.003_bib45) 2003; 58 Seto (10.1016/j.bbagen.2006.07.003_bib66) 1993; 268 Bradshaw (10.1016/j.bbagen.2006.07.003_bib1) 1959; 81 Bell (10.1016/j.bbagen.2006.07.003_bib6) 1997; 272 Yamazaki (10.1016/j.bbagen.2006.07.003_bib68) 1999; 27 Newcomb (10.1016/j.bbagen.2006.07.003_bib19) 2003; 409 Cole (10.1016/j.bbagen.2006.07.003_bib24) 1991; 113 Yabuki (10.1016/j.bbagen.2006.07.003_bib72) 1993; 21 Ortiz De Montellano (10.1016/j.bbagen.2006.07.003_bib13) 2005 Hartmann (10.1016/j.bbagen.2006.07.003_bib39) 1999; 96 Kassahun (10.1016/j.bbagen.2006.07.003_bib67) 2001; 14 Ortiz de Montellano (10.1016/j.bbagen.2006.07.003_bib84) 1986 Poulos (10.1016/j.bbagen.2006.07.003_bib8) 2005 Egger (10.1016/j.bbagen.2006.07.003_bib56) 1988; 16 Kalgutkar (10.1016/j.bbagen.2006.07.003_bib30) 2005; 6 Lamb (10.1016/j.bbagen.2006.07.003_bib3) 2006; 2 Kalgutkar (10.1016/j.bbagen.2006.07.003_bib29) 2005; 1 Dalvie (10.1016/j.bbagen.2006.07.003_bib46) 2004; 32 Harris (10.1016/j.bbagen.2006.07.003_bib14) 2000; 39 Vaz (10.1016/j.bbagen.2006.07.003_bib20) 1998; 95 Chen (10.1016/j.bbagen.2006.07.003_bib38) 2002; 277 Bieler (10.1016/j.bbagen.2006.07.003_bib62) 1997; 18 Stiborova (10.1016/j.bbagen.2006.07.003_bib63) 2001; 14 Bondon (10.1016/j.bbagen.2006.07.003_bib32) 1989; 264 Ortiz de Montellano (10.1016/j.bbagen.2006.07.003_bib83) 1995 Yano (10.1016/j.bbagen.2006.07.003_bib42) 2005; 12 Ogliaro (10.1016/j.bbagen.2006.07.003_bib18) 2002; 124 Kim (10.1016/j.bbagen.2006.07.003_bib78) 2005; 17 Reilly (10.1016/j.bbagen.2006.07.003_bib59) 2003; 16 Lee (10.1016/j.bbagen.2006.07.003_bib55) 2004; 18 Stiborova (10.1016/j.bbagen.2006.07.003_bib61) 1994; 15 Hecker (10.1016/j.bbagen.2006.07.003_bib26) 1989; 264 Guengerich (10.1016/j.bbagen.2006.07.003_bib35) 1989; 264 Russell (10.1016/j.bbagen.2006.07.003_bib43) 1969; 91 Henry (10.1016/j.bbagen.2006.07.003_bib76) 2005; 127 Fukushima (10.1016/j.bbagen.2006.07.003_bib31) 1978; 83 Reich (10.1016/j.bbagen.2006.07.003_bib37) 1978; 100 Toy (10.1016/j.bbagen.2006.07.003_bib22) 1998; 120 Guengerich (10.1016/j.bbagen.2006.07.003_bib33) 1980; 55 Pylypenko (10.1016/j.bbagen.2006.07.003_bib52) 2003; 278 Zerbe (10.1016/j.bbagen.2006.07.003_bib2) 2002; 277 Chae (10.1016/j.bbagen.2006.07.003_bib64) 1999; 59 Fujioka (10.1016/j.bbagen.2006.07.003_bib79) 2003; 54 Funa (10.1016/j.bbagen.2006.07.003_bib49) 2005; 187 Zerbe (10.1016/j.bbagen.2006.07.003_bib53) 2004; 43 Tang (10.1016/j.bbagen.2006.07.003_bib58) 2005; 18 Chang (10.1016/j.bbagen.2006.07.003_bib27) 1996; 35 Bishop (10.1016/j.bbagen.2006.07.003_bib80) 2001; 42 Baek (10.1016/j.bbagen.2006.07.003_bib60) 2001; 29 Treiber (10.1016/j.bbagen.2006.07.003_bib44) 1997; 119 Watanabe (10.1016/j.bbagen.2006.07.003_bib77) 1998; 120 Dansette (10.1016/j.bbagen.2006.07.003_bib47) 2005; 338 Gordon (10.1016/j.bbagen.2006.07.003_bib54) 1987; 15 Guengerich (10.1016/j.bbagen.2006.07.003_bib5) 2004; 43 Chandrasena (10.1016/j.bbagen.2006.07.003_bib17) 2004; 126 Doss (10.1016/j.bbagen.2006.07.003_bib57) 2005; 18 Liebler (10.1016/j.bbagen.2006.07.003_bib82) 1983; 22 Burka (10.1016/j.bbagen.2006.07.003_bib34) 1983; 80 Wu (10.1016/j.bbagen.2006.07.003_bib41) 2005; 280 Reddy (10.1016/j.bbagen.2006.07.003_bib69) 2005; 18 Yin (10.1016/j.bbagen.2006.07.003_bib65) 2004; 43 Walsh (10.1016/j.bbagen.2006.07.003_bib75) 1979 |
| References_xml | – volume: 100 start-page: 4888 year: 1978 end-page: 4889 ident: bib37 article-title: Hypervalent organoiodine chemistry. Syn elimination of alkyl iodoso compounds publication-title: J. Am. Chem. Soc. – volume: 81 start-page: 5007 year: 1959 ident: bib1 article-title: Degradation of (+)-camphor publication-title: J. Am. Chem. Soc. – volume: 280 start-page: 22697 year: 2005 end-page: 22705 ident: bib36 article-title: Calibration of the channel that Determines the ω-hydroxylation regiospecificity of cytochrome P450 4A1: catalytic oxidation of 12-halododecanoic acids publication-title: J. Biol. Chem. – volume: 12 start-page: 822 year: 2005 end-page: 823 ident: bib42 article-title: Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen publication-title: Nat. Struct. Biol. – volume: 287 start-page: 1615 year: 2000 end-page: 1622 ident: bib7 article-title: The catalytic pathway of cytochrome P450cam at atomic resolution publication-title: Science – volume: 280 start-page: 12279 year: 2005 end-page: 12291 ident: bib10 article-title: Kinetic analysis of oxidation of coumarins by human cytochrome P450 2A6 publication-title: J. Biol. Chem. – volume: 80 start-page: 6680 year: 1983 end-page: 6684 ident: bib34 article-title: Mechanisms of hydroxylation by cytochrome P-450: metabolism of monohalobenzenes by phenobarbital-induced microsomes publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 126 start-page: 115 year: 2004 end-page: 126 ident: bib17 article-title: Hydroxylation by the hydroperoxy–iron species in cytochrome P450 enzymes publication-title: J. Am. Chem. Soc. – volume: 15 start-page: 1187 year: 1994 end-page: 1192 ident: bib61 article-title: Characterization of DNA-adducts formed by aristolochic acids in the target organ (forestomach) of rats by P-32 postlabeling analysis using different chromatographic procedures publication-title: Carcinogenesis – volume: 14 start-page: 1128 year: 2001 end-page: 1137 ident: bib63 article-title: Human enzymes involved in the metabolic activation of carcinogenic aristolochic acids: evidence for reductive activation by cytochromes P450 1A1 and 1A2 publication-title: Chem. Res. Toxicol. – volume: 120 start-page: 6231 year: 1998 end-page: 6239 ident: bib77 article-title: The in vitro conversion of norsolorinic acid to Aflatoxin B1. An improved method of cell-free enzyme preparation and stabilization publication-title: J. Am. Chem. Soc. – volume: 277 start-page: 37519 year: 2002 end-page: 37526 ident: bib38 article-title: Crystal structure of the F87W/Y96F/V247L mutant of cytochrome P-450cam with 1,3,5-trichlorobenzene bound and further protein engineering for the oxidation of pentachlorobenzene and hexachlorobenzene publication-title: J. Biol. Chem. – volume: 18 start-page: 934 year: 2005 end-page: 945 ident: bib58 article-title: Bioactivation of 2,3-diaminopyridine-containing bradykinin B1 receptor antagonists: irreversible binding to liver microsomal proteins and formation of glutathione conjugates publication-title: Chem. Res. Toxicol. – volume: 18 start-page: 1063 year: 1997 end-page: 1067 ident: bib62 article-title: P-32-post-labelling analysis of DNA adducts formed by aristolochic acid in tissues from patients with Chinese herbs nephropathy publication-title: Carcinogenesis – volume: 21 start-page: 1167 year: 1993 end-page: 1169 ident: bib72 article-title: Novel cleavage of the 1,2,4-oxadiazole ring in rat metabolism of SM-6586, a dihydropyridine calcium antagonist publication-title: Drug Metab. Dispos. – volume: 22 start-page: 5482 year: 1983 end-page: 5489 ident: bib82 article-title: Olefin oxidation by cytochrome P-450: evidence for group migration in catalytic intermediates formed with vinylidene chloride and trans-1-phenyl-1-butene publication-title: Biochemistry – start-page: 87 year: 2005 end-page: 114 ident: bib8 article-title: Structures of cytochrome P450 enzymes publication-title: Cytochrome P450: Structure Mechanism, and Biochemistry – volume: 264 start-page: 141 year: 1989 end-page: 150 ident: bib26 article-title: On the mechanism of prostacyclin and thromboxane A publication-title: J. Biol. Chem. – volume: 39 start-page: 13817 year: 2000 end-page: 13824 ident: bib40 article-title: Oxidation of indole by cytochrome P450 enzymes publication-title: Biochemistry – volume: 54 start-page: 137 year: 2003 end-page: 164 ident: bib79 article-title: Biosynthesis and metabolism of brassinosteroids publication-title: Annu. Rev. Plant Biol. – volume: 120 start-page: 9718 year: 1998 end-page: 9719 ident: bib16 article-title: Two distinct electrophilic oxidants effect hydroxylation in cytochrome P-450-catalyzed reactions publication-title: J. Am. Chem. Soc. – volume: 38 start-page: 1843 year: 1988 end-page: 1845 ident: bib71 article-title: On the metabolism of ditazole in man publication-title: Arzneim. Forsch. – volume: 264 start-page: 1988 year: 1989 end-page: 1997 ident: bib32 article-title: Oxidation of cycloalkylamines by cytochrome P-450. Mechanism-based inactivation, adduct formation, ring expansion, and nitrone formation publication-title: J. Biol. Chem. – volume: 14 start-page: 62 year: 2001 end-page: 70 ident: bib67 article-title: Studies on the metabolism of troglitazone to reactive intermediates in vitro and in vivo. Evidence for novel biotransformation pathways involving quinone methide formation and thiazolidinedione ring scission publication-title: Chem. Res. Toxicol. – volume: 95 start-page: 3555 year: 1998 end-page: 3560 ident: bib20 article-title: Epoxidation of olefins by cytochrome P450: evidence from site-specific mutagenesis for hydroperoxo-iron as an electrophilic oxidant publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 268 start-page: 9986 year: 1993 end-page: 9997 ident: bib66 article-title: Partitioning between publication-title: J. Biol. Chem. – volume: 39 start-page: 2003 year: 2000 end-page: 2007 ident: bib14 article-title: Two-state reactivity in the rebound step of alkane hydroxylation by cytochrome P-450: origins of free radicals with finite lifetimes publication-title: Angew. Chem., Int. Ed. Engl. – volume: 42 start-page: 114 year: 2001 end-page: 120 ident: bib80 article-title: Plants steroid hormones, brassinosteroids: current highlights of molecular aspects on their synthesis/metabolism, transport, perception and response publication-title: Plant Cell Physiol. – volume: 83 start-page: 1019 year: 1978 end-page: 1027 ident: bib31 article-title: Enzymatic oxidation of disulfides and thiolsulfinates by both rabbit liver microsomes and a reconstituted system with purified cytochrome P-450 publication-title: J. Biochem. (Tokyo) – volume: 119 start-page: 1565 year: 1997 end-page: 1571 ident: bib44 article-title: Chemical and biological oxidation of thiophene: preparation and complete characterization of thiophene S-oxide dimers and evidence for thiophene publication-title: J. Am. Chem. Soc. – volume: 91 start-page: 3851 year: 1969 end-page: 3859 ident: bib43 article-title: Oxidation of carbanions: IV. Oxidation of indoxyl to indigo in basic solution publication-title: J. Am. Chem. Soc. – volume: 22 start-page: 1725 year: 1989 end-page: 1727 ident: bib51 article-title: Phenol oxidative coupling of benzylisoquinoline alkoids catalyzed by regio- and stereoselective cytochrome P-450 linked plant enzymes: salutaridine and berbamunine publication-title: J. Chem. Soc. – volume: 264 start-page: 17198 year: 1989 end-page: 17205 ident: bib35 article-title: Oxidation of halogenated compounds by cytochrome P-450, peroxidases, and model metalloporphyrins publication-title: J. Biol. Chem. – volume: 187 start-page: 8149 year: 2005 end-page: 8155 ident: bib49 article-title: Biosynthesis of hexahydroxyperylenequinone melanin via oxidative aryl coupling by cytochrome P-450 in publication-title: J. Bacteriol. – volume: 338 start-page: 450 year: 2005 end-page: 455 ident: bib47 article-title: First evidence that cytochrome P450 may catalyze both S-oxidation and epoxidation of thiophene derivatives publication-title: Biochem. Biophys. Res. Commun. – volume: 271 start-page: 219 year: 1990 end-page: 222 ident: bib81 article-title: Reaction mechanism of oxidative rearrangement of flavanone in isoflavone biosynthesis publication-title: FEBS Lett. – volume: 32 start-page: 49 year: 2004 end-page: 57 ident: bib46 article-title: Characterization of novel dihydrothienofigurepyridinium and thienopyridinium metabolites of ticlopidine in vitro: role of peroxidases, cytochromes P450, and monoamine oxidases publication-title: Drug Metab. Dispos. – volume: 35 start-page: 464 year: 1996 end-page: 471 ident: bib27 article-title: P450-dependent transformations of 15 publication-title: Biochemistry – volume: 29 start-page: 381 year: 2001 end-page: 388 ident: bib60 article-title: Metabolism of dimethyl-4,4′-dimethoxy-5,6,5′, 6′-dimethylene dioxybiphenyl-2,2′-dicarboxylate (DDB) by human liver microsomes: Characterization of metabolic pathways and of cytochrome P450 isoforms involved publication-title: Drug Metab. Dispos. – volume: 127 start-page: 5224 year: 2005 end-page: 5237 ident: bib25 article-title: The final catalytic step of cytochrome P450 aromatase: a density functional theory study publication-title: J. Am. Chem. Soc. – volume: 55 start-page: 303 year: 1980 end-page: 317 ident: bib33 article-title: In vitro activation of 1,2-dichloroethane by microsomal and cytosolic enzymes publication-title: Toxicol. Appl. Pharmacol. – volume: 96 start-page: 7831 year: 1999 end-page: 7836 ident: bib39 article-title: NIH shift in flavin-dependent monooxygenation: mechanistic studies with 2-aminobenzoyl-CoA monooxygenase reductase publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 280 start-page: 41090 year: 2005 end-page: 41100 ident: bib41 article-title: Expansion of substrate specificity of cytochrome P450 2A6 by mutagenesis publication-title: J. Biol. Chem. – start-page: 183 year: 2005 end-page: 245 ident: bib13 article-title: Substrate oxidation by cytochrome P450 enzymes publication-title: Cytochrome P450: Structure, Mechanism, and Biochemistry – volume: 124 start-page: 2806 year: 2002 end-page: 2817 ident: bib18 article-title: Searching for the second oxidant in the catalytic cycle of cytochrome P450: a theoretical investigation of the iron(III)-hydroperoxo species and its epoxidation pathways publication-title: J. Am. Chem. Soc. – volume: 127 start-page: 3724 year: 2005 end-page: 3733 ident: bib76 article-title: Ordering the reductive and cytochrome P450 oxidative steps in demethylsterigmatocystin formation yields general insights into the biosynthesis of aflatoxin and related fungal metabolites publication-title: J. Am. Chem. Soc. – volume: 409 start-page: 72 year: 2003 end-page: 79 ident: bib19 article-title: Multiple mechanisms and multiple oxidants in P450-catalyzed hydroxylations publication-title: Arch. Biochem. Biophys. – volume: 16 start-page: 568 year: 1988 end-page: 575 ident: bib56 article-title: Disposition and metabolism of prinomide in laboratory animals publication-title: Drug Metab. Dispos. – volume: 1 start-page: 91 year: 2005 end-page: 141 ident: bib29 article-title: Minimising the potential for metabolic activation in drug discovery publication-title: Expert Opin. Drug Metab. Toxicol. – volume: 18 start-page: 880 year: 2005 end-page: 888 ident: bib69 article-title: Mechanistic studies on the metabolic scission of thiazolidinedione derivatives to acyclic thiols publication-title: Chem. Res. Toxicol. – volume: 280 start-page: 11599 year: 2005 end-page: 11607 ident: bib50 article-title: Bindings of two flaviolin substrate molecules, oxidative coupling, and crystal structure of publication-title: J. Biol. Chem. – volume: 43 start-page: 5455 year: 2004 end-page: 5466 ident: bib65 article-title: Conversion of the 2,2,6,6-tetramethylpiperidine moiety to a 2,2-dimethylpyrrolidine by cytochrome P450: evidence for a mechanism involving nitroxide radicals and heme iron publication-title: Biochemistry – volume: 278 start-page: 46727 year: 2003 end-page: 46733 ident: bib52 article-title: Crystal structure of OxyC, a cytochrome P450 implicated in an oxidative C–C coupling reaction during vancomycin biosynthesis publication-title: J. Biol. Chem. – year: 1979 ident: bib75 article-title: Enzymatic Reaction Mechanisms – volume: 277 start-page: 47476 year: 2002 end-page: 47485 ident: bib2 article-title: Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis publication-title: J. Biol. Chem. – volume: 17 start-page: 2397 year: 2005 end-page: 2412 ident: bib78 article-title: Arabidopsis CYP85A2, a cytochrome P450, mediates the Baeyer–Villiger oxidation of castasterone to brassinolide in brassinosteroid biosynthesis publication-title: Plant Cell – volume: 59 start-page: 1473 year: 1999 end-page: 1480 ident: bib64 article-title: Comparative metabolism of 1-, 2-, and 4-nitropyrene by human hepatic and pulmonary microsomes publication-title: Cancer Res. – volume: 117 start-page: 12085 year: 1995 end-page: 12091 ident: bib21 article-title: A nonsynchronous concerted mechanism for cytochrome P-450 catalyzed hydroxylation publication-title: J. Am. Chem. Soc. – volume: 58 start-page: 28 year: 2003 end-page: 35 ident: bib45 article-title: The thienopyridine derivatives (platelet adenosine diphosphate receptor antagonists), pharmacology and clinical developments publication-title: Anaesthesia – volume: 43 start-page: 6709 year: 2004 end-page: 6713 ident: bib53 article-title: An oxidative phenol coupling reaction catalyzed by oxyB, a cytochrome P450 from the vancomycin-producing microorganism publication-title: Angew. Chem., Int. Ed. Engl. – volume: 43 start-page: 10775 year: 2004 end-page: 10788 ident: bib5 article-title: Rate-limiting steps in oxidations catalyzed by rabbit cytochrome P450 1A2 publication-title: Biochemistry – volume: 6 start-page: 161 year: 2005 end-page: 225 ident: bib30 article-title: A comprehensive listing of bioactivation pathways of organic functional groups publication-title: Curr. Drug Metab. – volume: 120 start-page: 7719 year: 1998 end-page: 7729 ident: bib22 article-title: Hypersenstive mechanistic probe studies of cytochrome P450-catalyzed hydroxylation reactions. Implications for the cationic pathway publication-title: J. Am. Chem. Soc. – volume: 18 start-page: 271 year: 2005 end-page: 276 ident: bib57 article-title: Metabolic activation of a 1,3-disubstituted piperazine derivative: evidence for a novel ring contraction to an imidazoline publication-title: Chem. Res. Toxicol. – volume: 36 start-page: 14741 year: 1997 end-page: 14750 ident: bib9 article-title: Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: rapid reduction in absence of substrate and variations among cytochrome P450 systems publication-title: Biochemistry – volume: 18 start-page: 675 year: 2005 end-page: 685 ident: bib73 article-title: In vitro bioactivation of dihydrobenzoxathiin selective estrogen receptor modulators by cytochrome P450 3A4 in human liver microsomes: formation of reactive iminium and quinone type metabolites publication-title: Chem. Res. Toxicol. – volume: 33 start-page: 4410 year: 1994 end-page: 4418 ident: bib23 article-title: Mechanism of the acyl-carbon cleavage and related reactions catalyzed by multifunctional P-450s: studies on cytochrome P45017a publication-title: Biochemistry – volume: 14 start-page: 611 year: 2001 end-page: 650 ident: bib12 article-title: Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity publication-title: Chem. Res. Toxicol. – volume: 383 start-page: 1553 year: 2002 end-page: 1564 ident: bib4 article-title: Rate-limiting steps in cytochrome P450 catalysis publication-title: Biol. Chem. – volume: 16 start-page: 336 year: 2003 end-page: 349 ident: bib59 article-title: Metabolism of capsaicin by cytochrome P450 produces novel dehydrogenated metabolites and decreases cytotoxicity to lung and liver cells publication-title: Chem. Res. Toxicol. – start-page: 217 year: 1986 end-page: 271 ident: bib84 article-title: Oxygen activation and transfer publication-title: Cytochrome P-450 – volume: 105 start-page: 2279 year: 2005 end-page: 2328 ident: bib15 article-title: Theoretical perspective on the structure and mechanism of cytochrome P450 enzymes publication-title: Chem. Rev. – volume: 2 start-page: 27 year: 2006 end-page: 40 ident: bib3 article-title: Streptomyces P450s as a model for drug discovery publication-title: Expert Opin. Drug Metab. Toxicol. – start-page: 245 year: 1995 end-page: 303 ident: bib83 article-title: Oxygen activation and reactivity publication-title: Cytochrome P450: Structure, Mechanism, and Biochemistry – volume: 15 start-page: 589 year: 1987 end-page: 594 ident: bib54 article-title: The metabolism of the abortifacient terpene, (R)-(+)-pulegone, to a proximate toxin, menthofuran publication-title: Drug Metab. Dispos. – volume: 272 start-page: 29643 year: 1997 end-page: 29651 ident: bib6 article-title: Oxidation kinetics of ethanol by human cytochrome P450 2E1. Rate-limiting product release accounts for effects of isotopic hydrogen substitution and cytochrome b5 on steady-state kinetics publication-title: J. Biol. Chem. – volume: 18 start-page: 1901 year: 2004 end-page: 1910 ident: bib55 article-title: Metabolism of 1-(3-[3-(4-cyanobenzyl)-3H-imidazol-4-yl]-propyl)-3-(6-methoxypyridin-3-yl)-1-(2-trifluoromethylbenzyl)thiourea (YH3945), a novel anti-cancer drug, in rats using the 14C-labeled compound publication-title: Rapid Commun. Mass Spectrom. – volume: 113 start-page: 8130 year: 1991 end-page: 8137 ident: bib24 article-title: Mechanistic studies on a placental aromatase model reaction publication-title: J. Am. Chem. Soc. – volume: 27 start-page: 1260 year: 1999 end-page: 1266 ident: bib68 article-title: Oxidation of troglitazone to a quinone-type metabolite catalyzed by cytochrome P450 2C8 and 3A4 in human liver microsomes publication-title: Drug Metab. Dispos. – volume: 124 start-page: 5294 year: 2002 end-page: 5303 ident: bib74 article-title: Synthesis of 11-hydroxyl O-methylsterigmatocystin and the role of a cytochrome P-450 in the final step of aflatoxin biosynthesis publication-title: J. Am. Chem. Soc. – volume: 394 start-page: 189 year: 2001 end-page: 200 ident: bib48 article-title: Interaction of new sulfaphenazole derivatives with human liver cytochrome P4502Cs: Structural determinants required for selective recognition by CYP2C9 and for inhibition of human CYP2Cs publication-title: Arch. Biochem. Biophys. – volume: 17 start-page: 9 year: 1984 end-page: 16 ident: bib11 article-title: Chemical mechanisms of catalysis by cytochromes P-450: a unified view publication-title: Acct. Chem. Res. – volume: 15 start-page: 269 year: 2002 end-page: 299 ident: bib28 article-title: Biotransformation reactions of five-membered aromatic heterocyclic rings publication-title: Chem. Res. Toxicol. – volume: 23 start-page: 1291 year: 1973 end-page: 1295 ident: bib70 article-title: Ditazol metabolism in rat, rabbit and man publication-title: Arzneim. Forsch. – volume: 117 start-page: 12085 year: 1995 ident: 10.1016/j.bbagen.2006.07.003_bib21 article-title: A nonsynchronous concerted mechanism for cytochrome P-450 catalyzed hydroxylation publication-title: J. Am. Chem. Soc. doi: 10.1021/ja00154a008 – volume: 272 start-page: 29643 year: 1997 ident: 10.1016/j.bbagen.2006.07.003_bib6 article-title: Oxidation kinetics of ethanol by human cytochrome P450 2E1. Rate-limiting product release accounts for effects of isotopic hydrogen substitution and cytochrome b5 on steady-state kinetics publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.47.29643 – volume: 15 start-page: 589 year: 1987 ident: 10.1016/j.bbagen.2006.07.003_bib54 article-title: The metabolism of the abortifacient terpene, (R)-(+)-pulegone, to a proximate toxin, menthofuran publication-title: Drug Metab. Dispos. – volume: 119 start-page: 1565 year: 1997 ident: 10.1016/j.bbagen.2006.07.003_bib44 article-title: Chemical and biological oxidation of thiophene: preparation and complete characterization of thiophene S-oxide dimers and evidence for thiophene S-oxide as an intermediate in thiophene metabolism in vivo and in vitro publication-title: J. Am. Chem. Soc. doi: 10.1021/ja962466g – volume: 18 start-page: 880 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib69 article-title: Mechanistic studies on the metabolic scission of thiazolidinedione derivatives to acyclic thiols publication-title: Chem. Res. Toxicol. doi: 10.1021/tx0500373 – volume: 120 start-page: 9718 year: 1998 ident: 10.1016/j.bbagen.2006.07.003_bib16 article-title: Two distinct electrophilic oxidants effect hydroxylation in cytochrome P-450-catalyzed reactions publication-title: J. Am. Chem. Soc. doi: 10.1021/ja981990f – volume: 80 start-page: 6680 year: 1983 ident: 10.1016/j.bbagen.2006.07.003_bib34 article-title: Mechanisms of hydroxylation by cytochrome P-450: metabolism of monohalobenzenes by phenobarbital-induced microsomes publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.80.21.6680 – volume: 105 start-page: 2279 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib15 article-title: Theoretical perspective on the structure and mechanism of cytochrome P450 enzymes publication-title: Chem. Rev. doi: 10.1021/cr030722j – volume: 22 start-page: 1725 year: 1989 ident: 10.1016/j.bbagen.2006.07.003_bib51 article-title: Phenol oxidative coupling of benzylisoquinoline alkoids catalyzed by regio- and stereoselective cytochrome P-450 linked plant enzymes: salutaridine and berbamunine publication-title: J. Chem. Soc. – year: 1979 ident: 10.1016/j.bbagen.2006.07.003_bib75 – volume: 1 start-page: 91 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib29 article-title: Minimising the potential for metabolic activation in drug discovery publication-title: Expert Opin. Drug Metab. Toxicol. doi: 10.1517/17425255.1.1.91 – volume: 268 start-page: 9986 year: 1993 ident: 10.1016/j.bbagen.2006.07.003_bib66 article-title: Partitioning between N-dealkylation and N-oxygenation in the oxidation of N,N-dialkylarylamines catalyzed by cytochrome P450 2B1 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)82162-7 – volume: 100 start-page: 4888 year: 1978 ident: 10.1016/j.bbagen.2006.07.003_bib37 article-title: Hypervalent organoiodine chemistry. Syn elimination of alkyl iodoso compounds publication-title: J. Am. Chem. Soc. doi: 10.1021/ja00483a042 – volume: 124 start-page: 2806 year: 2002 ident: 10.1016/j.bbagen.2006.07.003_bib18 article-title: Searching for the second oxidant in the catalytic cycle of cytochrome P450: a theoretical investigation of the iron(III)-hydroperoxo species and its epoxidation pathways publication-title: J. Am. Chem. Soc. doi: 10.1021/ja0171963 – volume: 409 start-page: 72 year: 2003 ident: 10.1016/j.bbagen.2006.07.003_bib19 article-title: Multiple mechanisms and multiple oxidants in P450-catalyzed hydroxylations publication-title: Arch. Biochem. Biophys. doi: 10.1016/S0003-9861(02)00445-9 – volume: 124 start-page: 5294 year: 2002 ident: 10.1016/j.bbagen.2006.07.003_bib74 article-title: Synthesis of 11-hydroxyl O-methylsterigmatocystin and the role of a cytochrome P-450 in the final step of aflatoxin biosynthesis publication-title: J. Am. Chem. Soc. doi: 10.1021/ja012185v – volume: 18 start-page: 1063 year: 1997 ident: 10.1016/j.bbagen.2006.07.003_bib62 article-title: P-32-post-labelling analysis of DNA adducts formed by aristolochic acid in tissues from patients with Chinese herbs nephropathy publication-title: Carcinogenesis doi: 10.1093/carcin/18.5.1063 – volume: 2 start-page: 27 year: 2006 ident: 10.1016/j.bbagen.2006.07.003_bib3 article-title: Streptomyces P450s as a model for drug discovery publication-title: Expert Opin. Drug Metab. Toxicol. doi: 10.1517/17425255.2.1.27 – volume: 36 start-page: 14741 year: 1997 ident: 10.1016/j.bbagen.2006.07.003_bib9 article-title: Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: rapid reduction in absence of substrate and variations among cytochrome P450 systems publication-title: Biochemistry doi: 10.1021/bi9719399 – volume: 15 start-page: 1187 year: 1994 ident: 10.1016/j.bbagen.2006.07.003_bib61 article-title: Characterization of DNA-adducts formed by aristolochic acids in the target organ (forestomach) of rats by P-32 postlabeling analysis using different chromatographic procedures publication-title: Carcinogenesis doi: 10.1093/carcin/15.6.1187 – volume: 38 start-page: 1843 year: 1988 ident: 10.1016/j.bbagen.2006.07.003_bib71 article-title: On the metabolism of ditazole in man publication-title: Arzneim. Forsch. – volume: 14 start-page: 1128 year: 2001 ident: 10.1016/j.bbagen.2006.07.003_bib63 article-title: Human enzymes involved in the metabolic activation of carcinogenic aristolochic acids: evidence for reductive activation by cytochromes P450 1A1 and 1A2 publication-title: Chem. Res. Toxicol. doi: 10.1021/tx010059z – volume: 42 start-page: 114 year: 2001 ident: 10.1016/j.bbagen.2006.07.003_bib80 article-title: Plants steroid hormones, brassinosteroids: current highlights of molecular aspects on their synthesis/metabolism, transport, perception and response publication-title: Plant Cell Physiol. doi: 10.1093/pcp/pce018 – volume: 127 start-page: 3724 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib76 article-title: Ordering the reductive and cytochrome P450 oxidative steps in demethylsterigmatocystin formation yields general insights into the biosynthesis of aflatoxin and related fungal metabolites publication-title: J. Am. Chem. Soc. doi: 10.1021/ja0455188 – volume: 22 start-page: 5482 year: 1983 ident: 10.1016/j.bbagen.2006.07.003_bib82 article-title: Olefin oxidation by cytochrome P-450: evidence for group migration in catalytic intermediates formed with vinylidene chloride and trans-1-phenyl-1-butene publication-title: Biochemistry doi: 10.1021/bi00293a005 – volume: 287 start-page: 1615 year: 2000 ident: 10.1016/j.bbagen.2006.07.003_bib7 article-title: The catalytic pathway of cytochrome P450cam at atomic resolution publication-title: Science doi: 10.1126/science.287.5458.1615 – volume: 280 start-page: 22697 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib36 article-title: Calibration of the channel that Determines the ω-hydroxylation regiospecificity of cytochrome P450 4A1: catalytic oxidation of 12-halododecanoic acids publication-title: J. Biol. Chem. doi: 10.1074/jbc.M502632200 – volume: 83 start-page: 1019 year: 1978 ident: 10.1016/j.bbagen.2006.07.003_bib31 article-title: Enzymatic oxidation of disulfides and thiolsulfinates by both rabbit liver microsomes and a reconstituted system with purified cytochrome P-450 publication-title: J. Biochem. (Tokyo) doi: 10.1093/oxfordjournals.jbchem.a131990 – volume: 18 start-page: 271 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib57 article-title: Metabolic activation of a 1,3-disubstituted piperazine derivative: evidence for a novel ring contraction to an imidazoline publication-title: Chem. Res. Toxicol. doi: 10.1021/tx049711r – volume: 120 start-page: 6231 year: 1998 ident: 10.1016/j.bbagen.2006.07.003_bib77 article-title: The in vitro conversion of norsolorinic acid to Aflatoxin B1. An improved method of cell-free enzyme preparation and stabilization publication-title: J. Am. Chem. Soc. doi: 10.1021/ja974367o – volume: 280 start-page: 12279 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib10 article-title: Kinetic analysis of oxidation of coumarins by human cytochrome P450 2A6 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M411019200 – volume: 54 start-page: 137 year: 2003 ident: 10.1016/j.bbagen.2006.07.003_bib79 article-title: Biosynthesis and metabolism of brassinosteroids publication-title: Annu. Rev. Plant Biol. doi: 10.1146/annurev.arplant.54.031902.134921 – volume: 96 start-page: 7831 year: 1999 ident: 10.1016/j.bbagen.2006.07.003_bib39 article-title: NIH shift in flavin-dependent monooxygenation: mechanistic studies with 2-aminobenzoyl-CoA monooxygenase reductase publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.96.14.7831 – volume: 27 start-page: 1260 year: 1999 ident: 10.1016/j.bbagen.2006.07.003_bib68 article-title: Oxidation of troglitazone to a quinone-type metabolite catalyzed by cytochrome P450 2C8 and 3A4 in human liver microsomes publication-title: Drug Metab. Dispos. doi: 10.1016/S0090-9556(24)14927-6 – volume: 264 start-page: 17198 year: 1989 ident: 10.1016/j.bbagen.2006.07.003_bib35 article-title: Oxidation of halogenated compounds by cytochrome P-450, peroxidases, and model metalloporphyrins publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)71478-6 – volume: 127 start-page: 5224 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib25 article-title: The final catalytic step of cytochrome P450 aromatase: a density functional theory study publication-title: J. Am. Chem. Soc. doi: 10.1021/ja044716w – volume: 338 start-page: 450 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib47 article-title: First evidence that cytochrome P450 may catalyze both S-oxidation and epoxidation of thiophene derivatives publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2005.08.091 – volume: 23 start-page: 1291 year: 1973 ident: 10.1016/j.bbagen.2006.07.003_bib70 article-title: Ditazol metabolism in rat, rabbit and man publication-title: Arzneim. Forsch. – volume: 33 start-page: 4410 year: 1994 ident: 10.1016/j.bbagen.2006.07.003_bib23 article-title: Mechanism of the acyl-carbon cleavage and related reactions catalyzed by multifunctional P-450s: studies on cytochrome P45017a publication-title: Biochemistry doi: 10.1021/bi00180a039 – volume: 126 start-page: 115 year: 2004 ident: 10.1016/j.bbagen.2006.07.003_bib17 article-title: Hydroxylation by the hydroperoxy–iron species in cytochrome P450 enzymes publication-title: J. Am. Chem. Soc. doi: 10.1021/ja038237t – volume: 17 start-page: 2397 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib78 article-title: Arabidopsis CYP85A2, a cytochrome P450, mediates the Baeyer–Villiger oxidation of castasterone to brassinolide in brassinosteroid biosynthesis publication-title: Plant Cell doi: 10.1105/tpc.105.033738 – volume: 280 start-page: 11599 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib50 article-title: Bindings of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M410933200 – volume: 12 start-page: 822 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib42 article-title: Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen publication-title: Nat. Struct. Biol. doi: 10.1038/nsmb971 – volume: 277 start-page: 47476 year: 2002 ident: 10.1016/j.bbagen.2006.07.003_bib2 article-title: Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis publication-title: J. Biol. Chem. doi: 10.1074/jbc.M206342200 – volume: 39 start-page: 2003 year: 2000 ident: 10.1016/j.bbagen.2006.07.003_bib14 article-title: Two-state reactivity in the rebound step of alkane hydroxylation by cytochrome P-450: origins of free radicals with finite lifetimes publication-title: Angew. Chem., Int. Ed. Engl. doi: 10.1002/1521-3773(20000602)39:11<2003::AID-ANIE2003>3.0.CO;2-M – volume: 113 start-page: 8130 year: 1991 ident: 10.1016/j.bbagen.2006.07.003_bib24 article-title: Mechanistic studies on a placental aromatase model reaction publication-title: J. Am. Chem. Soc. doi: 10.1021/ja00021a044 – volume: 55 start-page: 303 year: 1980 ident: 10.1016/j.bbagen.2006.07.003_bib33 article-title: In vitro activation of 1,2-dichloroethane by microsomal and cytosolic enzymes publication-title: Toxicol. Appl. Pharmacol. doi: 10.1016/0041-008X(80)90092-7 – volume: 16 start-page: 336 year: 2003 ident: 10.1016/j.bbagen.2006.07.003_bib59 article-title: Metabolism of capsaicin by cytochrome P450 produces novel dehydrogenated metabolites and decreases cytotoxicity to lung and liver cells publication-title: Chem. Res. Toxicol. doi: 10.1021/tx025599q – volume: 18 start-page: 675 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib73 article-title: In vitro bioactivation of dihydrobenzoxathiin selective estrogen receptor modulators by cytochrome P450 3A4 in human liver microsomes: formation of reactive iminium and quinone type metabolites publication-title: Chem. Res. Toxicol. doi: 10.1021/tx0496789 – start-page: 87 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib8 article-title: Structures of cytochrome P450 enzymes – volume: 264 start-page: 1988 year: 1989 ident: 10.1016/j.bbagen.2006.07.003_bib32 article-title: Oxidation of cycloalkylamines by cytochrome P-450. Mechanism-based inactivation, adduct formation, ring expansion, and nitrone formation publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)94132-3 – volume: 43 start-page: 5455 year: 2004 ident: 10.1016/j.bbagen.2006.07.003_bib65 article-title: Conversion of the 2,2,6,6-tetramethylpiperidine moiety to a 2,2-dimethylpyrrolidine by cytochrome P450: evidence for a mechanism involving nitroxide radicals and heme iron publication-title: Biochemistry doi: 10.1021/bi035944q – volume: 14 start-page: 62 year: 2001 ident: 10.1016/j.bbagen.2006.07.003_bib67 article-title: Studies on the metabolism of troglitazone to reactive intermediates in vitro and in vivo. Evidence for novel biotransformation pathways involving quinone methide formation and thiazolidinedione ring scission publication-title: Chem. Res. Toxicol. doi: 10.1021/tx000180q – volume: 59 start-page: 1473 year: 1999 ident: 10.1016/j.bbagen.2006.07.003_bib64 article-title: Comparative metabolism of 1-, 2-, and 4-nitropyrene by human hepatic and pulmonary microsomes publication-title: Cancer Res. – volume: 394 start-page: 189 year: 2001 ident: 10.1016/j.bbagen.2006.07.003_bib48 article-title: Interaction of new sulfaphenazole derivatives with human liver cytochrome P4502Cs: Structural determinants required for selective recognition by CYP2C9 and for inhibition of human CYP2Cs publication-title: Arch. Biochem. Biophys. doi: 10.1006/abbi.2001.2511 – volume: 264 start-page: 141 year: 1989 ident: 10.1016/j.bbagen.2006.07.003_bib26 article-title: On the mechanism of prostacyclin and thromboxane A2 biosynthesis publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)31235-8 – volume: 95 start-page: 3555 year: 1998 ident: 10.1016/j.bbagen.2006.07.003_bib20 article-title: Epoxidation of olefins by cytochrome P450: evidence from site-specific mutagenesis for hydroperoxo-iron as an electrophilic oxidant publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.95.7.3555 – volume: 120 start-page: 7719 year: 1998 ident: 10.1016/j.bbagen.2006.07.003_bib22 article-title: Hypersenstive mechanistic probe studies of cytochrome P450-catalyzed hydroxylation reactions. Implications for the cationic pathway publication-title: J. Am. Chem. Soc. doi: 10.1021/ja981157i – volume: 18 start-page: 1901 year: 2004 ident: 10.1016/j.bbagen.2006.07.003_bib55 article-title: Metabolism of 1-(3-[3-(4-cyanobenzyl)-3H-imidazol-4-yl]-propyl)-3-(6-methoxypyridin-3-yl)-1-(2-trifluoromethylbenzyl)thiourea (YH3945), a novel anti-cancer drug, in rats using the 14C-labeled compound publication-title: Rapid Commun. Mass Spectrom. doi: 10.1002/rcm.1555 – volume: 32 start-page: 49 year: 2004 ident: 10.1016/j.bbagen.2006.07.003_bib46 article-title: Characterization of novel dihydrothienofigurepyridinium and thienopyridinium metabolites of ticlopidine in vitro: role of peroxidases, cytochromes P450, and monoamine oxidases publication-title: Drug Metab. Dispos. doi: 10.1124/dmd.32.1.49 – volume: 29 start-page: 381 year: 2001 ident: 10.1016/j.bbagen.2006.07.003_bib60 article-title: Metabolism of dimethyl-4,4′-dimethoxy-5,6,5′, 6′-dimethylene dioxybiphenyl-2,2′-dicarboxylate (DDB) by human liver microsomes: Characterization of metabolic pathways and of cytochrome P450 isoforms involved publication-title: Drug Metab. Dispos. – start-page: 183 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib13 article-title: Substrate oxidation by cytochrome P450 enzymes – volume: 35 start-page: 464 year: 1996 ident: 10.1016/j.bbagen.2006.07.003_bib27 article-title: P450-dependent transformations of 15R- and 15S-hydroperoxyeicosatetraenoic acids: stereoselective formation of epoxyalcohol products publication-title: Biochemistry doi: 10.1021/bi952081v – volume: 21 start-page: 1167 year: 1993 ident: 10.1016/j.bbagen.2006.07.003_bib72 article-title: Novel cleavage of the 1,2,4-oxadiazole ring in rat metabolism of SM-6586, a dihydropyridine calcium antagonist publication-title: Drug Metab. Dispos. – volume: 18 start-page: 934 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib58 article-title: Bioactivation of 2,3-diaminopyridine-containing bradykinin B1 receptor antagonists: irreversible binding to liver microsomal proteins and formation of glutathione conjugates publication-title: Chem. Res. Toxicol. doi: 10.1021/tx0500427 – volume: 271 start-page: 219 year: 1990 ident: 10.1016/j.bbagen.2006.07.003_bib81 article-title: Reaction mechanism of oxidative rearrangement of flavanone in isoflavone biosynthesis publication-title: FEBS Lett. doi: 10.1016/0014-5793(90)80410-K – volume: 14 start-page: 611 year: 2001 ident: 10.1016/j.bbagen.2006.07.003_bib12 article-title: Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity publication-title: Chem. Res. Toxicol. doi: 10.1021/tx0002583 – volume: 17 start-page: 9 year: 1984 ident: 10.1016/j.bbagen.2006.07.003_bib11 article-title: Chemical mechanisms of catalysis by cytochromes P-450: a unified view publication-title: Acct. Chem. Res. doi: 10.1021/ar00097a002 – volume: 81 start-page: 5007 year: 1959 ident: 10.1016/j.bbagen.2006.07.003_bib1 article-title: Degradation of (+)-camphor publication-title: J. Am. Chem. Soc. doi: 10.1021/ja01529a060 – start-page: 217 year: 1986 ident: 10.1016/j.bbagen.2006.07.003_bib84 article-title: Oxygen activation and transfer – start-page: 245 year: 1995 ident: 10.1016/j.bbagen.2006.07.003_bib83 article-title: Oxygen activation and reactivity – volume: 15 start-page: 269 year: 2002 ident: 10.1016/j.bbagen.2006.07.003_bib28 article-title: Biotransformation reactions of five-membered aromatic heterocyclic rings publication-title: Chem. Res. Toxicol. doi: 10.1021/tx015574b – volume: 278 start-page: 46727 year: 2003 ident: 10.1016/j.bbagen.2006.07.003_bib52 article-title: Crystal structure of OxyC, a cytochrome P450 implicated in an oxidative C–C coupling reaction during vancomycin biosynthesis publication-title: J. Biol. Chem. doi: 10.1074/jbc.M306486200 – volume: 277 start-page: 37519 year: 2002 ident: 10.1016/j.bbagen.2006.07.003_bib38 article-title: Crystal structure of the F87W/Y96F/V247L mutant of cytochrome P-450cam with 1,3,5-trichlorobenzene bound and further protein engineering for the oxidation of pentachlorobenzene and hexachlorobenzene publication-title: J. Biol. Chem. doi: 10.1074/jbc.M203762200 – volume: 43 start-page: 6709 year: 2004 ident: 10.1016/j.bbagen.2006.07.003_bib53 article-title: An oxidative phenol coupling reaction catalyzed by oxyB, a cytochrome P450 from the vancomycin-producing microorganism publication-title: Angew. Chem., Int. Ed. Engl. doi: 10.1002/anie.200461278 – volume: 16 start-page: 568 year: 1988 ident: 10.1016/j.bbagen.2006.07.003_bib56 article-title: Disposition and metabolism of prinomide in laboratory animals publication-title: Drug Metab. Dispos. – volume: 39 start-page: 13817 year: 2000 ident: 10.1016/j.bbagen.2006.07.003_bib40 article-title: Oxidation of indole by cytochrome P450 enzymes publication-title: Biochemistry doi: 10.1021/bi001229u – volume: 43 start-page: 10775 year: 2004 ident: 10.1016/j.bbagen.2006.07.003_bib5 article-title: Rate-limiting steps in oxidations catalyzed by rabbit cytochrome P450 1A2 publication-title: Biochemistry doi: 10.1021/bi0491393 – volume: 6 start-page: 161 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib30 article-title: A comprehensive listing of bioactivation pathways of organic functional groups publication-title: Curr. Drug Metab. doi: 10.2174/1389200054021799 – volume: 280 start-page: 41090 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib41 article-title: Expansion of substrate specificity of cytochrome P450 2A6 by mutagenesis publication-title: J. Biol. Chem. doi: 10.1074/jbc.M508182200 – volume: 58 start-page: 28 year: 2003 ident: 10.1016/j.bbagen.2006.07.003_bib45 article-title: The thienopyridine derivatives (platelet adenosine diphosphate receptor antagonists), pharmacology and clinical developments publication-title: Anaesthesia doi: 10.1046/j.1365-2044.2003.02960.x – volume: 383 start-page: 1553 year: 2002 ident: 10.1016/j.bbagen.2006.07.003_bib4 article-title: Rate-limiting steps in cytochrome P450 catalysis publication-title: Biol. Chem. doi: 10.1515/BC.2002.175 – volume: 187 start-page: 8149 year: 2005 ident: 10.1016/j.bbagen.2006.07.003_bib49 article-title: Biosynthesis of hexahydroxyperylenequinone melanin via oxidative aryl coupling by cytochrome P-450 in Streptomyces griseus publication-title: J. Bacteriol. doi: 10.1128/JB.187.23.8149-8155.2005 – volume: 91 start-page: 3851 year: 1969 ident: 10.1016/j.bbagen.2006.07.003_bib43 article-title: Oxidation of carbanions: IV. Oxidation of indoxyl to indigo in basic solution publication-title: J. Am. Chem. Soc. doi: 10.1021/ja01042a028 |
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| Snippet | Cytochrome P450 (P450) enzymes are some of the most versatile redox proteins known. The basic P450 reactions include C-hydroxylation, heteroatom oxygenation,... |
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| SubjectTerms | Animals Bioactivation Catalysis Cytochrome P-450 Enzyme System - chemistry Cytochrome P-450 Enzyme System - metabolism Cytochrome P450 Dimerization Humans Hydroxylation Metabolism of drugs Mixed Function Oxygenases - metabolism Oxidation reactions Oxidation-Reduction Rearrangement reactions Substrate Specificity |
| Title | Complex reactions catalyzed by cytochrome P450 enzymes |
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