{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T17:44:27Z","timestamp":1777657467449,"version":"3.51.4"},"reference-count":75,"publisher":"Elsevier BV","issue":"33","license":[{"start":{"date-parts":[[2015,8,1]],"date-time":"2015-08-01T00:00:00Z","timestamp":1438387200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,3]],"date-time":"2020-09-03T00:00:00Z","timestamp":1599091200000},"content-version":"vor","delay-in-days":1860,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["R37 CA090426"],"award-info":[{"award-number":["R37 CA090426"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["T32 E5007028"],"award-info":[{"award-number":["T32 E5007028"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["jbc.org"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2015,8]]},"DOI":"10.1074\/jbc.m115.665331","type":"journal-article","created":{"date-parts":[[2015,7,9]],"date-time":"2015-07-09T00:30:14Z","timestamp":1436401814000},"page":"20200-20210","update-policy":"https:\/\/doi.org\/10.1074\/jbc.f110.005975","source":"Crossref","is-referenced-by-count":31,"title":["Cytochrome P450 3A Enzymes Catalyze the O6-Demethylation of Thebaine, a Key Step in Endogenous Mammalian Morphine Biosynthesis"],"prefix":"10.1016","volume":"290","author":[{"given":"Valerie M.","family":"Kramlinger","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M\u00f3nica","family":"Alvarado Rojas","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tatsuyuki","family":"Kanamori","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"F. Peter","family":"Guengerich","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M115.665331_bib1","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/0197-0186(94)90089-2","article-title":"\u03bc-, \u03b4-, \u03ba-Opioid receptors and their subtypes: a critical review with emphasis on radioligand binding experiments","volume":"24","author":"Fowler","year":"1994","journal-title":"Neurochem. Int"},{"key":"10.1074\/jbc.M115.665331_bib2","first-page":"161","article-title":"Biosynthesis of morphine: its importance in Parkinson's disease","volume":"56","author":"Perea-Sasiain","year":"2008","journal-title":"Rev. Fac. Med. Unal"},{"key":"10.1074\/jbc.M115.665331_bib3","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1016\/S0022-3565(25)24758-9","article-title":"Changes of endogenous morphine and codeine contents in the fasting rat","volume":"257","author":"Lee","year":"1991","journal-title":"J. Pharmacol. Exp. Ther"},{"key":"10.1074\/jbc.M115.665331_bib4","doi-asserted-by":"crossref","first-page":"5203","DOI":"10.1073\/pnas.82.15.5203","article-title":"Morphine and other opiates from beef brain and adrenal","volume":"82","author":"Goldstein","year":"1985","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.665331_bib5","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1016\/S0022-3565(25)39122-6","article-title":"Chemical characterization and regulation of endogenous morphine and codeine in the rat","volume":"242","author":"Donnerer","year":"1987","journal-title":"J. Pharmacol. Exp. Ther"},{"key":"10.1074\/jbc.M115.665331_bib6","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1097\/00024382-199909000-00001","article-title":"Mammalian opiate alkaloid synthesis: lessons derived from plant biochemistry","volume":"12","author":"Meijerink","year":"1999","journal-title":"Shock"},{"key":"10.1074\/jbc.M115.665331_bib7","doi-asserted-by":"crossref","first-page":"838","DOI":"10.1006\/bbrc.1998.9232","article-title":"Dopamine formation from tyramine by CYP2D6","volume":"249","author":"Hiroi","year":"1998","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.M115.665331_bib8","first-page":"CS45","article-title":"Identification of endogenous morphine and a \u03bc3-like opiate alkaloid receptor in human brain tissue taken from a patient with intractable complex partial epilepsy","volume":"14","author":"Fricchione","year":"2008","journal-title":"Med. Sci. Monit"},{"key":"10.1074\/jbc.M115.665331_bib9","doi-asserted-by":"crossref","first-page":"14091","DOI":"10.1073\/pnas.0405430101","article-title":"Endogenous formation of morphine in human cells","volume":"101","author":"Poeaknapo","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.665331_bib10","doi-asserted-by":"crossref","first-page":"8495","DOI":"10.1073\/pnas.0503244102","article-title":"How human neuroblastoma cells make morphine","volume":"102","author":"Boettcher","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.665331_bib11","doi-asserted-by":"crossref","first-page":"7357","DOI":"10.4049\/jimmunol.175.11.7357","article-title":"Human white blood cells synthesize morphine: CYP2D6 modulation","volume":"175","author":"Zhu","year":"2005","journal-title":"J. Immunol"},{"key":"10.1074\/jbc.M115.665331_bib12","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1016\/S0022-3565(25)38970-6","article-title":"Endogenous codeine and morphine in poor and extensive metabolisers of the CYP2D6 (debrisoquine\/sparteine) polymorphism","volume":"268","author":"Mikus","year":"1994","journal-title":"J. Pharmacol. Exp. Ther"},{"key":"10.1074\/jbc.M115.665331_bib13","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1002\/cpt197824160","article-title":"Plasma codeine and morphine concentrations after therapeutic oral doses of codeine-containing analgesics","volume":"24","author":"Findlay","year":"1978","journal-title":"Clin. Pharmacol. Ther"},{"key":"10.1074\/jbc.M115.665331_bib14","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1111\/j.1365-2125.2012.04199.x","article-title":"Comparison of serum and lithium-heparinate plasma for the accurate measurements of endogenous and exogenous morphine concentrations","volume":"74","author":"Laux-Biehlmann","year":"2012","journal-title":"Br. J. Clin. Pharmacol"},{"key":"10.1074\/jbc.M115.665331_bib15","doi-asserted-by":"crossref","first-page":"2321","DOI":"10.1093\/brain\/awr166","article-title":"Endogenous morphine-like compound immunoreactivity increases in Parkinsonism","volume":"134","author":"Charron","year":"2011","journal-title":"Brain"},{"key":"10.1074\/jbc.M115.665331_bib16","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0008791","article-title":"Endogenous morphine levels are increased in sepsis: a partial implication of neutrophils","volume":"5","author":"Glattard","year":"2010","journal-title":"Plos. One"},{"key":"10.1074\/jbc.M115.665331_bib17","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1111\/j.1399-5618.2009.00760.x","article-title":"The role of dopamine in bipolar disorder","volume":"11","author":"Cousins","year":"2009","journal-title":"Bipolar Disord"},{"key":"10.1074\/jbc.M115.665331_bib18","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1126\/science.155.3759.170","article-title":"Biosynthesis of the morphine alkaloids","volume":"155","author":"Kirby","year":"1967","journal-title":"Science"},{"key":"10.1074\/jbc.M115.665331_bib19","series-title":"The Alkaloids: Chemistry and Biology","first-page":"257","article-title":"Molecular genetics of plant alkaloid biosynthesis","volume":"Vol. 50","author":"Kutchan","year":"1998"},{"key":"10.1074\/jbc.M115.665331_bib20","doi-asserted-by":"crossref","first-page":"4110","DOI":"10.1105\/tpc.113.115113","article-title":"Morphine biosynthesis in opium poppy involves two cell types: sieve elements and laticifers","volume":"25","author":"Onoyovwe","year":"2013","journal-title":"Plant Cell"},{"key":"10.1074\/jbc.M115.665331_bib21","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.neuroscience.2012.12.013","article-title":"Endogenous morphine and its metabolites in mammals: history, synthesis, localization and perspectives","volume":"233","author":"Laux-Biehlmann","year":"2013","journal-title":"Neuroscience"},{"key":"10.1074\/jbc.M115.665331_bib22","doi-asserted-by":"crossref","first-page":"716","DOI":"10.1073\/pnas.86.2.716","article-title":"Identification of the convulsant opiate thebaine in mammalian brain","volume":"86","author":"Kodaira","year":"1989","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.665331_bib23","doi-asserted-by":"crossref","first-page":"9784","DOI":"10.1073\/pnas.83.24.9784","article-title":"Morphine and codeine from mammalian brain","volume":"83","author":"Weitz","year":"1986","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.665331_bib24","doi-asserted-by":"crossref","first-page":"8147","DOI":"10.1073\/pnas.1003423107","article-title":"Urinary excretion of morphine and biosynthetic precursors in mice","volume":"107","author":"Grobe","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.665331_bib25","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1038\/330674a0","article-title":"Synthesis of the skeleton of the morphine molecule by mammalian liver","volume":"330","author":"Weitz","year":"1987","journal-title":"Nature"},{"key":"10.1074\/jbc.M115.665331_bib26","doi-asserted-by":"crossref","first-page":"1267","DOI":"10.1073\/pnas.85.4.1267","article-title":"Transformation of thebaine to oripavine, codeine, and morphine by rat liver, kidney, and brain microsomes","volume":"85","author":"Kodaira","year":"1988","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.665331_bib27","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1038\/nchembio.317","article-title":"Dioxygenases catalyze the O-demethylation steps of morphine biosynthesis in opium poppy","volume":"6","author":"Hagel","year":"2010","journal-title":"Nat. Chem. Biol"},{"key":"10.1074\/jbc.M115.665331_bib28","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/S0006-291X(88)80729-0","article-title":"Bioactivation of the narcotic drug codeine in human liver is mediated by the polymorphic monooxygenase catalyzing debrisoquine 4-hydroxylation (cytochrome P-450 dbl\/bufI)","volume":"152","author":"Dayer","year":"1988","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.M115.665331_bib29","series-title":"Cytochrome P450: Structure, Mechanism, and Biochemistry","first-page":"111","article-title":"Substrate oxidation by cytochrome P450 enzymes","author":"Ortiz de Montellano","year":"2015"},{"key":"10.1074\/jbc.M115.665331_bib30","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1021\/tx0002583","article-title":"Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity","volume":"14","author":"Guengerich","year":"2001","journal-title":"Chem. Res. Toxicol"},{"key":"10.1074\/jbc.M115.665331_bib31","doi-asserted-by":"crossref","first-page":"816","DOI":"10.1111\/j.1742-4658.2012.08473.x","article-title":"The Fe(II)\/\u03b1-ketoglutarate-dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers","volume":"279","author":"Knauer","year":"2012","journal-title":"FEBS J"},{"key":"10.1074\/jbc.M115.665331_bib32","doi-asserted-by":"crossref","first-page":"1022","DOI":"10.1021\/ja039113j","article-title":"Direct detection of oxygen intermediates in the non-heme Fe enzyme taurine\/\u03b1-ketoglutarate dioxygenase","volume":"126","author":"Proshlyakov","year":"2004","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M115.665331_bib33","doi-asserted-by":"crossref","first-page":"28997","DOI":"10.1074\/jbc.M113.488585","article-title":"Dioxygenases catalyze O-demethylation and O,O-demethylenation with widespread roles in benzylisoquinoline alkaloid metabolism in opium poppy","volume":"288","author":"Farrow","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.665331_bib34","doi-asserted-by":"crossref","first-page":"7598","DOI":"10.1021\/bi980345i","article-title":"Reductive and oxidative half-reactions of morphinone reductase from Pseudomonas putida M10: a kinetic and thermodynamic analysis","volume":"37","author":"Craig","year":"1998","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M115.665331_bib35","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1111\/j.1574-6968.1999.tb08836.x","article-title":"Transformations of codeine to important semisynthetic opiate derivatives by Pseudomonas putida m10","volume":"181","author":"Lister","year":"1999","journal-title":"FEMS Microbiol. Lett"},{"key":"10.1074\/jbc.M115.665331_bib36","series-title":"Hayes' Principles and Methods of Toxicology","first-page":"1905","article-title":"Analysis and characterization of enzymes and nucleic acids relevant to toxicology","author":"Guengerich","year":"2014"},{"key":"10.1074\/jbc.M115.665331_bib37","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1042\/bj3010097","article-title":"Purification and characterization of morphinone reductase from Pseudomonas putida M10","volume":"301","author":"French","year":"1994","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.M115.665331_bib38","doi-asserted-by":"crossref","first-page":"30976","DOI":"10.1074\/jbc.M202846200","article-title":"Crystal structure of bacterial morphinone reductase and properties of the C191A mutant enzyme","volume":"277","author":"Barna","year":"2002","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.665331_bib39","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1016\/0003-2697(69)90067-0","article-title":"A method for titrating oxygen-sensitive organic redox systems with reducing agents in solution","volume":"27","author":"Burleigh","year":"1969","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.M115.665331_bib40","doi-asserted-by":"crossref","first-page":"2811","DOI":"10.1021\/bi00281a007","article-title":"Oxidation-reduction properties of rat liver cytochromes P-450 and NADPH-cytochrome P-450 reductase related to catalysis in reconstituted systems","volume":"22","author":"Guengerich","year":"1983","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M115.665331_bib41","doi-asserted-by":"crossref","first-page":"10775","DOI":"10.1021\/bi0491393","article-title":"Rate-limiting steps in oxidations catalyzed by rabbit cytochrome P450 1A2","volume":"43","author":"Guengerich","year":"2004","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M115.665331_bib42","doi-asserted-by":"crossref","first-page":"1252","DOI":"10.1038\/nprot.2009.122","article-title":"Chromatographic assays of drug oxidation by human cytochrome P450 3A4","volume":"4","author":"Sohl","year":"2009","journal-title":"Nat. Protoc"},{"key":"10.1074\/jbc.M115.665331_bib43","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.ejps.2004.10.006","article-title":"Multiple P450 substrates in a single run: rapid and comprehensive in vitro interaction assay","volume":"24","author":"Turpeinen","year":"2005","journal-title":"Eur. J. Pharm. Sci"},{"key":"10.1074\/jbc.M115.665331_bib44","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1016\/S0928-0987(00)00190-1","article-title":"High-throughput cytochrome P450 (CYP) inhibition screening via a cassette probe-dosing strategy. V. Validation of a direct injection\/on-line guard cartridge extraction: tandem mass spectrometry method for CYP1A2 inhibition assessment","volume":"12","author":"Bu","year":"2001","journal-title":"Eur. J. Pharm. Sci"},{"key":"10.1074\/jbc.M115.665331_bib45","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1080\/004982500237749","article-title":"Automated high throughput human CYP isoform activity assay using SPE-LC\/MS method: application in CYP inhibition evaluation","volume":"30","author":"Yin","year":"2000","journal-title":"Xenobiotica"},{"key":"10.1074\/jbc.M115.665331_bib46","first-page":"897","article-title":"Evaluation of methoxsalen, tranylcypromine, and tryptamine as specific and selective CYP2A6 inhibitors in vitro","volume":"29","author":"Zhang","year":"2001","journal-title":"Drug. Metab. Dispos"},{"key":"10.1074\/jbc.M115.665331_bib47","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1124\/jpet.103.056127","article-title":"Potent mechanism-based inhibition of human CYP2B6 by clopidogrel and ticlopidine","volume":"308","author":"Richter","year":"2004","journal-title":"J. Pharmacol. Exp. Ther"},{"key":"10.1074\/jbc.M115.665331_bib48","series-title":"Cytochrome P450: Structure, Mechanism, and Biochemistry","first-page":"247","article-title":"Inhibition of cytochrome P450 enzymes","author":"Correia","year":"2005"},{"key":"10.1074\/jbc.M115.665331_bib49","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1124\/dmd.31.7.833","article-title":"Selectivities of human cytochrome P450 inhibitors toward rat P450 isoforms: study with cDNA-expressed systems of the rat","volume":"31","author":"Kobayashi","year":"2003","journal-title":"Drug. Metab. Dispos"},{"key":"10.1074\/jbc.M115.665331_bib50","doi-asserted-by":"crossref","first-page":"10695","DOI":"10.1074\/jbc.M410595200","article-title":"Reaction of morphinone reductase with 2-cyclohexen-1-one and 1-nitrocyclohexene: proton donation, ligand binding, and the role of residues histidine 186 and asparagine 189","volume":"280","author":"Messiha","year":"2005","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.665331_bib51","doi-asserted-by":"crossref","first-page":"24425","DOI":"10.1074\/jbc.M109.011320","article-title":"Mammalian cytochrome P450 enzymes catalyze the phenol-coupling step in endogenous morphine biosynthesis","volume":"284","author":"Grobe","year":"2009","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.665331_bib52","doi-asserted-by":"crossref","first-page":"20","DOI":"10.2174\/138920008783331121","article-title":"Comparison of kinetic parameters for drug oxidation rates and substrate inhibition potential mediated by cytochrome P450 3A4 and 3A5","volume":"9","author":"Niwa","year":"2008","journal-title":"Curr. Drug. Metab"},{"key":"10.1074\/jbc.M115.665331_bib53","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1124\/dmd.114.057000","article-title":"Relative contributions of cytochrome CYP3A4 versus CYP3A5 for CYP3A-cleared drugs assessed in vitro using a CYP3A4-selective inactivator (CYP3cide)","volume":"42","author":"Tseng","year":"2014","journal-title":"Drug. Metab. Dispos"},{"key":"10.1074\/jbc.M115.665331_bib54","doi-asserted-by":"crossref","first-page":"1686","DOI":"10.1124\/dmd.112.045302","article-title":"Selective mechanism-based inactivation of CYP3A4 by CYP3cide (PF-04981517) and its utility as an in vitro tool for delineating the relative roles of CYP3A4 versus CYP3A5 in the metabolism of drugs","volume":"40","author":"Walsky","year":"2012","journal-title":"Drug. Metab. Dispos"},{"key":"10.1074\/jbc.M115.665331_bib55","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/S0026-895X(25)11539-3","article-title":"Immunological comparison of hepatic and extrahepatic cytochromes P-450","volume":"15","author":"Guengerich","year":"1979","journal-title":"Mol. Pharmacol"},{"key":"10.1074\/jbc.M115.665331_bib56","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/0024-3205(87)90347-X","article-title":"Morphine and codeine are endogenous components of human cerebrospinal fluid","volume":"40","author":"Cardinale","year":"1987","journal-title":"Life Sci"},{"key":"10.1074\/jbc.M115.665331_bib57","doi-asserted-by":"crossref","first-page":"4566","DOI":"10.1073\/pnas.83.12.4566","article-title":"Presence and formation of codeine and morphine in the rat","volume":"83","author":"Donnerer","year":"1986","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M115.665331_bib58","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.abb.2010.11.010","article-title":"An (R)-specific N-methyltransferase involved in human morphine biosynthesis","volume":"506","author":"Grobe","year":"2011","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1074\/jbc.M115.665331_bib59","doi-asserted-by":"crossref","first-page":"1182","DOI":"10.1021\/tx400096m","article-title":"Removal of N-alkyl modifications from N2-alkylguanine and N4-alkylcytosine in DNA by the adaptive response protein AlkB","volume":"26","author":"Li","year":"2013","journal-title":"Chem. Res. Toxicol"},{"key":"10.1074\/jbc.M115.665331_bib60","doi-asserted-by":"crossref","first-page":"2083","DOI":"10.1128\/jb.175.7.2083-2086.1993","article-title":"Alcaligenes eutrophus JMP134 \u201c2,4-dichlorophenoxyacetate monooxygenase\u201d is an \u03b1-ketoglutarate-dependent dioxygenase","volume":"175","author":"Fukumori","year":"1993","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M115.665331_bib61","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1016\/S0891-5849(02)01006-7","article-title":"The labile iron pool: characterization, measurement, and participation in cellular processes","volume":"33","author":"Kakhlon","year":"2002","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/jbc.M115.665331_bib62","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1016\/0378-4274(95)03532-X","article-title":"Toxicity of iron and hydrogen peroxide: the Fenton reaction","volume":"82\u201383","author":"Winterbourn","year":"1995","journal-title":"Toxicol. Lett"},{"key":"10.1074\/jbc.M115.665331_bib63","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1021\/ar9800789","article-title":"Comments on the mechanism of \u201cFenton-Like\u201d reaction","volume":"32","author":"Goldstein","year":"1999","journal-title":"Acc. Chem. Res"},{"key":"10.1074\/jbc.M115.665331_bib64","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1021\/ar970057z","article-title":"A radical account of \u201cOxygenated Fenton Chemistry.\u201d","volume":"31","author":"MacFaul","year":"1998","journal-title":"Acc. Chem. Res"},{"key":"10.1074\/jbc.M115.665331_bib65","doi-asserted-by":"crossref","first-page":"1008","DOI":"10.1039\/C0OB01021A","article-title":"Further investigations into the N-demethylation of oripavine using iron and stainless steel","volume":"9","author":"Kok","year":"2011","journal-title":"Org. Biomol. Chem"},{"key":"10.1074\/jbc.M115.665331_bib66","doi-asserted-by":"crossref","first-page":"24311","DOI":"10.1016\/S0021-9258(20)80527-4","article-title":"Purification and characterization of 2,4-dichlorophenoxyacetate\/\u03b1-ketoglutarate dioxygenase","volume":"268","author":"Fukumori","year":"1993","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M115.665331_bib67","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1080\/10409230490440541","article-title":"FeII\/\u03b1-ketoglutarate-dependent hydroxylases and related enzymes","volume":"39","author":"Hausinger","year":"2004","journal-title":"Crit. Rev. Biochem. Mol. Biol"},{"key":"10.1074\/jbc.M115.665331_bib68","series-title":"2-Oxoglutarate-Dependent Oxygenases","author":"Hausinger","year":"2015"},{"key":"10.1074\/jbc.M115.665331_bib69","doi-asserted-by":"crossref","first-page":"13","DOI":"10.2165\/00003088-200645010-00002","article-title":"Significance of the minor cytochrome P450 3A isoforms","volume":"45","author":"Daly","year":"2006","journal-title":"Clin. Pharmacokinet"},{"key":"10.1074\/jbc.M115.665331_bib70","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1016\/j.drudis.2006.03.002","article-title":"New perspectives on the impact of cytochrome P450 3A expression for pediatric pharmacology","volume":"11","author":"Stevens","year":"2006","journal-title":"Drug Discov. Today"},{"key":"10.1074\/jbc.M115.665331_bib71","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1021\/tx500444e","article-title":"Survey of human oxidoreductases and cytochrome P450 enzymes involved in the metabolism of chemicals","volume":"28","author":"Rendic","year":"2015","journal-title":"Chem. Res. Toxicol"},{"key":"10.1074\/jbc.M115.665331_bib72","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1097\/FPC.0b013e32830054ac","article-title":"Pharmacogenetics of P450 oxidoreductase: effect of sequence variants on activities of CYP1A2 and CYP2C19","volume":"18","author":"Agrawal","year":"2008","journal-title":"Pharmacogenet. Genomics"},{"key":"10.1074\/jbc.M115.665331_bib73","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1016\/S0090-9556(24)15243-9","article-title":"Characterization of cytochrome P-450 2D1 activity in rat brain: high-affinity kinetics for dextromethorphan","volume":"27","author":"Tyndale","year":"1999","journal-title":"Drug Metab. Dispos"},{"key":"10.1074\/jbc.M115.665331_bib74","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1038\/86882","article-title":"Sequence diversity in CYP3A promoters and characterization of the genetic basis of polymorphic CYP3A5 expression","volume":"27","author":"Kuehl","year":"2001","journal-title":"Nat. Genet"},{"key":"10.1074\/jbc.M115.665331_bib75","first-page":"193","article-title":"Genotyping for cytochrome P450 polymorphisms","volume":"320","author":"Daly","year":"2006","journal-title":"Methods Mol. Biol"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820421593?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820421593?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M115.665331","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,5,29]],"date-time":"2025-05-29T03:02:18Z","timestamp":1748487738000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820421593"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,8]]},"references-count":75,"journal-issue":{"issue":"33","published-print":{"date-parts":[[2015,8]]}},"alternative-id":["S0021925820421593"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m115.665331","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2015,8]]}}}