PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3020022-1 1986 NADPH-cytochrome P-450 reductase-catalyzed reduction of paraquat promoted the release of iron from ferritin. Iron 89-93 cytochrome p450 oxidoreductase Homo sapiens 0-32 2823718-0 1987 Chemiluminescence studies on the generation of oxygen radicals from the interaction of NADPH-cytochrome P-450 reductase with iron. Iron 125-129 cytochrome p450 oxidoreductase Homo sapiens 87-119 2823718-1 1987 The ability of NADPH-cytochrome P-450 reductase to interact with iron and generate oxygen radicals was evaluated by assaying for low level chemiluminescence. Iron 65-69 cytochrome p450 oxidoreductase Homo sapiens 15-47 3015607-9 1986 Iron chelators inhibited the P-450-dependent lipid peroxidation, whereas iron chelate interacted with NADPH-cytochrome-P-450 reductase in the membranes giving rise to reductase-dependent lipid peroxidation. Iron 73-77 cytochrome p450 oxidoreductase Homo sapiens 102-134 3017216-3 1986 We now report that, in the presence of NADPH-cytochrome P-450 reductase, these drugs undergo redox cycling to generate superoxide which mediates a slow, reductive release of iron from ferritin, the major intracellular iron storage protein. Iron 174-178 cytochrome p450 oxidoreductase Homo sapiens 39-71 3017216-3 1986 We now report that, in the presence of NADPH-cytochrome P-450 reductase, these drugs undergo redox cycling to generate superoxide which mediates a slow, reductive release of iron from ferritin, the major intracellular iron storage protein. Iron 218-222 cytochrome p450 oxidoreductase Homo sapiens 39-71 1255-12 1975 It is concluded that iron enters the cell, then is probably reduced inside the cell by NADPH via the NADPH-cytochrome P-450 reductase, and in the reduced state initiates lipid peroxidation. Iron 21-25 cytochrome p450 oxidoreductase Homo sapiens 101-133 6438073-8 1984 The ferrous 688-nm substance was degraded to a biliverdin-iron complex much more rapidly in the presence of the NADPH-cytochrome P-450 reductase system than in its absence, indicating that a reducing equivalent is essential for the initiation of heme degradation even when starting from the ferrous 688-nm substance. Iron 58-62 cytochrome p450 oxidoreductase Homo sapiens 112-144 32788383-3 2020 We determined that H2O2-induced cytotoxicity is an iron-dependent process in HAP1 cells and conducted a CRISPR/Cas9-based survival screen that identified four genes that mediate H2O2-induced cell death: POR (encoding cytochrome P450 oxidoreductase), RETSAT (retinol saturase), KEAP1 (Kelch-like ECH-associated protein-1), and SLC52A2 (riboflavin transporter). Iron 51-55 cytochrome p450 oxidoreductase Homo sapiens 203-206 25849895-1 2015 Heme oxygenase (HO) catalyzes a key step in heme homeostasis: the O2- and NADPH-cytochrome P450 reductase-dependent conversion of heme to biliverdin, Fe, and CO through a process in which the heme participates both as a prosthetic group and as a substrate. Iron 150-152 cytochrome p450 oxidoreductase Homo sapiens 74-105 31421070-6 2019 In fact, HO1, NADPH-cytochrome P450 reductase, and PCBP2 form a functional unit that integrates the catabolism of heme with the binding and transport of iron by PCBP2. Iron 153-157 cytochrome p450 oxidoreductase Homo sapiens 14-45 28655775-1 2017 Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron. Iron 51-55 cytochrome p450 oxidoreductase Homo sapiens 116-147 28655775-1 2017 Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron. Iron 208-212 cytochrome p450 oxidoreductase Homo sapiens 116-147 25196843-1 2014 Heme oxygenase (HO) catalyzes the rate-limiting step in the O2-dependent degradation of heme to biliverdin, CO, and iron with electrons delivered from NADPH via cytochrome P450 reductase (CPR). Iron 116-120 cytochrome p450 oxidoreductase Homo sapiens 161-186 25196843-1 2014 Heme oxygenase (HO) catalyzes the rate-limiting step in the O2-dependent degradation of heme to biliverdin, CO, and iron with electrons delivered from NADPH via cytochrome P450 reductase (CPR). Iron 116-120 cytochrome p450 oxidoreductase Homo sapiens 188-191 20679134-1 2010 Heme oxygenase 1 (HO-1) uses molecular oxygen and electrons from NADPH cytochrome P450 reductase to convert heme to CO, ferrous iron, and biliverdin (BV). Iron 128-132 cytochrome p450 oxidoreductase Homo sapiens 65-96 23463547-4 2013 The present results showed that both CYP2A13 and POR were presented the highest expression levels or activity with 0.2 mM delta-aminolaevulinic acid (5-ALA), 0.02 mM Fe(3+) and 0.5-1.0 mug/ml hemin. Iron 166-168 cytochrome p450 oxidoreductase Homo sapiens 49-52 22923613-1 2012 Human heme oxygenases 1 and 2 (HO-1 and HO-2) degrade heme in the presence of oxygen and NADPH-cytochrome P450 reductase, producing ferrous iron, CO, and biliverdin. Iron 140-144 cytochrome p450 oxidoreductase Homo sapiens 89-120 20624491-2 2011 CPR shuttles electrons from NADPH through the FAD and FMN-coenzymes into the iron of the prosthetic heme-group of the CYP. Iron 77-81 cytochrome p450 oxidoreductase Homo sapiens 0-3 16115609-1 2005 The microsomal heme oxygenase system consists of heme oxygenase (HO) and NADPH-cytochrome P450 reductase, and plays a key role in the physiological catabolism of heme which yields biliverdin, carbon monoxide, and iron as the final products. Iron 213-217 cytochrome p450 oxidoreductase Homo sapiens 73-104 19123922-1 2009 Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR). Iron 109-113 cytochrome p450 oxidoreductase Homo sapiens 167-198 19123922-1 2009 Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR). Iron 109-113 cytochrome p450 oxidoreductase Homo sapiens 200-203 17915953-2 2007 In the process of heme degradation, HO-1 receives the electrons necessary for catalysis from the flavoprotein NADPH cytochrome P450 reductase (CPR), releasing free iron and carbon monoxide. Iron 164-168 cytochrome p450 oxidoreductase Homo sapiens 116-141 17915953-2 2007 In the process of heme degradation, HO-1 receives the electrons necessary for catalysis from the flavoprotein NADPH cytochrome P450 reductase (CPR), releasing free iron and carbon monoxide. Iron 164-168 cytochrome p450 oxidoreductase Homo sapiens 143-146 16769893-7 2006 Furthermore, the ET rate from NADPH/CPR to the composite is 3.5-fold faster than that of Fe(Schiff-base).HO, although the redox potential of Fe(10-CH(2)CH(2)COOH-Schiff-base).HO (-79 mV vs. NHE) is lower than that of Fe(Schiff-base).HO (+15 mV vs. NHE), where NHE is normal hydrogen electrode. Iron 89-91 cytochrome p450 oxidoreductase Homo sapiens 36-39 16769893-7 2006 Furthermore, the ET rate from NADPH/CPR to the composite is 3.5-fold faster than that of Fe(Schiff-base).HO, although the redox potential of Fe(10-CH(2)CH(2)COOH-Schiff-base).HO (-79 mV vs. NHE) is lower than that of Fe(Schiff-base).HO (+15 mV vs. NHE), where NHE is normal hydrogen electrode. Iron 141-143 cytochrome p450 oxidoreductase Homo sapiens 36-39 15589375-1 2005 Heme oxygenases (HO-1 and HO-2) catalyze the NADPH-cytochrome P(450) reductase (CPR)-dependent degradation of heme into iron, carbon monoxide, and biliverdin, which is reduced into bilirubin. Iron 120-124 cytochrome p450 oxidoreductase Homo sapiens 45-78 15589375-1 2005 Heme oxygenases (HO-1 and HO-2) catalyze the NADPH-cytochrome P(450) reductase (CPR)-dependent degradation of heme into iron, carbon monoxide, and biliverdin, which is reduced into bilirubin. Iron 120-124 cytochrome p450 oxidoreductase Homo sapiens 80-83 14692760-1 2003 Heme oxygenase (HO) catalyzes the O2 and NADPH/cytochrome P450 reductase-dependent conversion of heme to biliverdin, free iron ion, and CO through a process in which the heme participates as both dioxygen-activating prosthetic group and substrate. Iron 122-126 cytochrome p450 oxidoreductase Homo sapiens 41-72 12626517-1 2003 Human heme oxygenase-1 (hHO-1) catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of heme to biliverdin, CO, and free iron. Iron 133-137 cytochrome p450 oxidoreductase Homo sapiens 45-76 7741258-0 1995 The role of iron chelators and oxygen in the reduced nicotinamide adenine dinucleotide phosphate-cytochrome P450 oxidoreductase-dependent chromium(VI) reduction. Iron 12-16 cytochrome p450 oxidoreductase Homo sapiens 97-127 11457014-4 2001 The radical intermediates exist in two electromers that differ in the oxidation state of iron; Por(+)(*)Fe(III)OCH(2)CH(2)(*) and PorFe(IV)OCH(2)CH(2)(*) (Por = porphyrin). Iron 89-93 cytochrome p450 oxidoreductase Homo sapiens 95-98 11853459-1 2002 Heme oxygenase (HO) catalyzes the O(2)- and NADPH-cytochrome P450 reductase-dependent conversion of heme to biliverdin, Fe, and CO through a process in which the heme participates both as a prosthetic group and as a substrate. Iron 120-122 cytochrome p450 oxidoreductase Homo sapiens 44-75 7633562-0 1995 NADPH-cytochrome-P450 reductase promotes hydroxyl radical production by the iron complex of ADR-925, the hydrolysis product of ICRF-187 (dexrazoxane). Iron 76-80 cytochrome p450 oxidoreductase Homo sapiens 0-31 7633562-3 1995 The ability of NADPH-cytochrome-P450 reductase to promote hydroxyl radical formation by iron complexes of ADR-925 and EDTA was compared by EPR spin trapping. Iron 88-92 cytochrome p450 oxidoreductase Homo sapiens 15-46 7864645-5 1995 The released iron may promote microsomal phospholipid peroxidation in the presence of endogenous ascorbate or NADPH-dependent cytochrome P-450 reductase because ascorbate oxidase and p-chloromercuribenzoic acid (an inhibitor of sulfhydryl enzymes) inhibited metHb- or HbO2-induced lipid peroxidation. Iron 13-17 cytochrome p450 oxidoreductase Homo sapiens 110-152 34604659-3 2021 In contrast, NO binding to the ferric center in ((por)Fe(L))+ to give the {FeNO}6 ((por)Fe(NO)(L))+ product results in a shortening of the trans Fe-L bond. Iron 145-147 cytochrome p450 oxidoreductase Homo sapiens 50-53 34604659-3 2021 In contrast, NO binding to the ferric center in ((por)Fe(L))+ to give the {FeNO}6 ((por)Fe(NO)(L))+ product results in a shortening of the trans Fe-L bond. Iron 145-147 cytochrome p450 oxidoreductase Homo sapiens 84-87