PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23045068-0 2001 Detection of heme oxygenase activity by measurement of CO. Heme oxygenase (HO) is the first and rate-limiting step in degradation of heme, and in the presence of NADPH-cytochrome P-450 reductase it produces equimolar amounts of biliverdin and CO. CO produced in a closed system can be quantified as described in this unit by gas chromatography as a measure of HO activity in tissue slices, tissue homogenates, and tissue fractions. Biliverdine 228-238 cytochrome p450 oxidoreductase Homo sapiens 162-194 10942763-5 2000 Of the Gly-139 mutants investigated, only G139A catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of heme to biliverdin, but most of them exhibit a new H(2)O(2)-dependent guaiacol peroxidation activity. Biliverdine 125-135 cytochrome p450 oxidoreductase Homo sapiens 62-93 6440489-2 1984 Biliverdin IX alpha is formed by elimination of one methene bridge carbon atom as CO. Purified NADPH-cytochrome P-450 reductase alone will also degrade heme but biliverdin is a minor product (15%). Biliverdine 0-13 cytochrome p450 oxidoreductase Homo sapiens 95-127 6440489-2 1984 Biliverdin IX alpha is formed by elimination of one methene bridge carbon atom as CO. Purified NADPH-cytochrome P-450 reductase alone will also degrade heme but biliverdin is a minor product (15%). Biliverdine 161-171 cytochrome p450 oxidoreductase Homo sapiens 95-127 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. Biliverdine 47-57 cytochrome p450 oxidoreductase Homo sapiens 112-144 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. Biliverdine 167-177 cytochrome p450 oxidoreductase Homo sapiens 116-147 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. Biliverdine 138-148 cytochrome p450 oxidoreductase Homo sapiens 74-105 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). Biliverdine 96-106 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). Biliverdine 96-106 cytochrome p450 oxidoreductase Homo sapiens 188-191 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. Biliverdine 154-164 cytochrome p450 oxidoreductase Homo sapiens 89-120 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). Biliverdine 138-148 cytochrome p450 oxidoreductase Homo sapiens 65-96 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). Biliverdine 71-81 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). Biliverdine 71-81 cytochrome p450 oxidoreductase Homo sapiens 200-203 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. Biliverdine 180-190 cytochrome p450 oxidoreductase Homo sapiens 73-104 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. Biliverdine 147-157 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. Biliverdine 147-157 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. Biliverdine 105-115 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. Biliverdine 108-118 cytochrome p450 oxidoreductase Homo sapiens 45-76 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. Biliverdine 108-118 cytochrome p450 oxidoreductase Homo sapiens 44-75