Correction to NADH:Cytochrome b5 Reductase and Cytochrome b5 Can Act as Sole Electron Donors to Human Cytochrome P450 1A1-Mediated Oxidation and DNA Adduct Formation by Benzo[a]pyrene
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چکیده
Can Act as Sole Electron Donors to Human Cytochrome P450 1A1Mediated Oxidation and DNA Adduct Formation by Benzo[a]pyrene Marie Stiborova,́*,† Radek Indra,† Michaela Moserova,́† Eva Frei,† Heinz H. Schmeiser,‡ Klaus Kopka,† David H. Phillips, and Volker M. Arlt †Department of Biochemistry, Faculty of Science, Charles University, Albertov 2030, 128 40, Prague 2, Czech Republic ‡Division of Radiopharmaceutical Chemistry, German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, 69120 Heidelberg, Germany Analytical and Environmental Sciences Division, MRC-PHE Centre for Environment and Health, King’s College London, Franklin-Wilkins Building, 150 Stamford Street, London SE1 9NH, United Kingdom NIHR Health Protection Research Unit in Health Impact of Environmental Hazards at King’s College London in Partnership with Public Health England, Franklin-Wilkins Building, 150 Stamford Street, London SE1 9NH, United Kingdom
منابع مشابه
NADH:Cytochrome b5 Reductase and Cytochrome b5 Can Act as Sole Electron Donors to Human Cytochrome P450 1A1-Mediated Oxidation and DNA Adduct Formation by Benzo[a]pyrene
Benzo[a]pyrene (BaP) is a human carcinogen that covalently binds to DNA after activation by cytochrome P450 (P450). Here, we investigated whether NADH:cytochrome b5 reductase (CBR) in the presence of cytochrome b5 can act as sole electron donor to human P450 1A1 during BaP oxidation and replace the canonical NADPH:cytochrome P450 reductase (POR) system. We also studied the efficiencies of the c...
متن کاملComparison of human cytochrome P450 1A1-catalysed oxidation of benzo[a]pyrene in prokaryotic and eukaryotic expression systems
Abstract Cytochrome P450 (CYP) 1A1 is the most important enzyme activating and detoxifying the human carcinogen benzo[a]pyrene (BaP). In the previous studies, we had shown that not only the canonic NADPH:CYP oxidoreductase (POR) can act as electron donor but also cytochrome b5 and its reductase, NADH:cytochrome b5 reductase. Here, we studied the role of the expression system used on the metabol...
متن کاملModulation of human cytochrome P450 1A1-mediated oxidation of benzo[a]pyrene by NADPH:cytochrome P450 oxidoreductase and cytochrome b5.
OBJECTIVES Cytochrome P450 (CYP) 1A1 located in the membrane of endoplasmic reticulum is the most important enzyme in both activation and detoxification of carcinogenic benzo[a]pyrene (BaP), in combination with microsomal epoxide hydrolase (mEH). However, it is still not clearly explained how the electron transfer is mediated by NADPH:CYP oxidoreductase (POR), another component of the microsoma...
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Abstract Ellipticine is an anticancer agent that forms covalent DNA adducts after enzymatic activation by cytochrome P450 (CYP) enzymes, mainly by CYP3A4. This process is one of the most important ellipticine DNA-damaging mechanisms for its antitumor action. Here, we investigated the efficiencies of human hepatic microsomes and human recombinant CYP3A4 expressed with its reductase, NADPH:CYP ox...
متن کاملEvidence That Cytochrome b5 and Cytochrome b5 Reductase Can Act as Sole Electron Donors to the Hepatic Cytochrome P450 Systems
We previously described the development of genetic models to study the in vivo functions of the hepatic cytochrome P450 (P450) system, through the hepatic deletion of either cytochrome P450 oxidoreductase [POR; HRN (hepatic reductase null) line] or cytochrome b5 [HBN (hepatic cytochrome b5 null) line]. However, HRN mice still exhibit low levels of mono-oxygenase activity in spite of the absence...
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