PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20967245-0 2010 Cytochrome P450 reductase: a harbinger of diffusible reduced oxygen species. Oxygen 61-67 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-15 20967245-1 2010 The bi-enzymatic system of cytochrome P450 (CYP, a hemoprotein) and cytochrome P450 reductase (CPR, a diflavoenzyme) mediate the redox metabolism of diverse indigenous and xenobiotic molecules in various cellular and organ systems, using oxygen and NADPH. Oxygen 238-244 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 27-42 20967245-1 2010 The bi-enzymatic system of cytochrome P450 (CYP, a hemoprotein) and cytochrome P450 reductase (CPR, a diflavoenzyme) mediate the redox metabolism of diverse indigenous and xenobiotic molecules in various cellular and organ systems, using oxygen and NADPH. Oxygen 238-244 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 44-47 20967245-7 2010 We also quantitatively demonstrate that the rate of oxygen activation and peroxide depletion by CPR accounts for the major reactivity in the CYP+CPR mixture. Oxygen 52-58 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 141-144 16914311-6 2006 These versions suggest that some cytochrome P-450"s catalyze the introduction of both oxygen atoms of dioxygen into an appropriate sterol precursor. Oxygen 86-92 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 33-49 20606811-6 2010 The formation of carbon-centered (1-hydroxyethyl) and oxygen-centered (hydroxyl) radicals during the metabolism of ethanol is considered: the generation of hydroxyethyl radicals, which occurs likely during the process of univalent reduction of dioxygen, is highlighted and is carried out by ferric cytochrome P(450) oxy-complex (P(450)-Fe(3+)O(2) (.-)) formed during the reduction of heme-oxygen. Oxygen 54-60 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 298-315 20606811-6 2010 The formation of carbon-centered (1-hydroxyethyl) and oxygen-centered (hydroxyl) radicals during the metabolism of ethanol is considered: the generation of hydroxyethyl radicals, which occurs likely during the process of univalent reduction of dioxygen, is highlighted and is carried out by ferric cytochrome P(450) oxy-complex (P(450)-Fe(3+)O(2) (.-)) formed during the reduction of heme-oxygen. Oxygen 244-252 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 298-315 20606811-6 2010 The formation of carbon-centered (1-hydroxyethyl) and oxygen-centered (hydroxyl) radicals during the metabolism of ethanol is considered: the generation of hydroxyethyl radicals, which occurs likely during the process of univalent reduction of dioxygen, is highlighted and is carried out by ferric cytochrome P(450) oxy-complex (P(450)-Fe(3+)O(2) (.-)) formed during the reduction of heme-oxygen. Oxygen 246-252 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 298-315 17109460-1 2006 The ongoing interest in very efficient systems for the imitation of cytochrome P-450-dependent monooxygenase reactions, consisting of metalloporphyrin and oxygen donor, prompted us to develop a method to compare the catalytic activity of soluble metalloporphyrins with those which have been immobilised on different silica surfaces. Oxygen 99-105 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 68-84 16914311-6 2006 These versions suggest that some cytochrome P-450"s catalyze the introduction of both oxygen atoms of dioxygen into an appropriate sterol precursor. Oxygen 102-110 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 33-49 15876406-0 2005 New assumptions about oxidative processes involved in steroid hormone biosynthesis: is the role of cytochrome P-450-activated dioxygen limited to hydroxylation reactions or are dioxygen insertion reactions also possible? Oxygen 126-134 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 99-115 16641218-1 2006 Animal studies have shown that induction of cytochrome P450 (CYP) in the lung by oxygen exposure may result in the release of free radical oxidants and arachidonic acid metabolites, which can cause lung injury that is reduced by treatment with cimetidine, a CYP inhibitor. Oxygen 81-87 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 44-59 16641218-1 2006 Animal studies have shown that induction of cytochrome P450 (CYP) in the lung by oxygen exposure may result in the release of free radical oxidants and arachidonic acid metabolites, which can cause lung injury that is reduced by treatment with cimetidine, a CYP inhibitor. Oxygen 81-87 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 61-64 16641218-1 2006 Animal studies have shown that induction of cytochrome P450 (CYP) in the lung by oxygen exposure may result in the release of free radical oxidants and arachidonic acid metabolites, which can cause lung injury that is reduced by treatment with cimetidine, a CYP inhibitor. Oxygen 81-87 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 258-261 16541400-10 2006 Fe-EDTA/H2O2 and uncoupled CYP(Fe=O) may both initiate the reaction, the latter in an attempt to reduce the ferryl oxygen to water. Oxygen 115-121 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 27-30 15922018-2 2005 FMO, like cytochrome P450 (CYP), is a monooxygenase, utilizing the reducing equivalents of NADPH to reduce 1 atom of molecular oxygen to water, while the other atom is used to oxidize the substrate. Oxygen 42-48 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 10-25 15922018-2 2005 FMO, like cytochrome P450 (CYP), is a monooxygenase, utilizing the reducing equivalents of NADPH to reduce 1 atom of molecular oxygen to water, while the other atom is used to oxidize the substrate. Oxygen 42-48 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 27-30 15644946-1 2004 The cytochrome p450 (CYP) superfamily is responsible for the oxidation, peroxidation, and (or) reduction of vitamins, steroids, xenobiotics, and the majority of cardiovascular drugs in an oxygen- and NADPH-dependent manner. Oxygen 188-194 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 4-19 15644946-1 2004 The cytochrome p450 (CYP) superfamily is responsible for the oxidation, peroxidation, and (or) reduction of vitamins, steroids, xenobiotics, and the majority of cardiovascular drugs in an oxygen- and NADPH-dependent manner. Oxygen 188-194 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 21-24 12214668-8 2002 A study of AQ4N metabolism in vitro and ex vivo using purified CYP enzymes, phenotyped human livers and CYP transfected cell lines shows that CYP3A, 1A and 1B1 family members contribute to AQ4N bioreduction in the absence of oxygen. Oxygen 225-231 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 63-66 15669763-1 2004 Biomimetic oxidation of unactivated carbons for structurally different steroids was studied with a model of cytochrome P-450, oxorutheniumporphyrinate complex, which is generated in situ by 2,6-dichloropyridine N-oxide as an oxygen donor and (5,10,15,20-tetramesitylporphyrinate) ruthenium(II) carbonyl complex and HBr as catalysts. Oxygen 225-231 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 108-124 15237857-1 2004 Cytochrome P450 (CYP) enzymes in the brain may have a role in the activation or inactivation of centrally acting drugs, in the metabolism of endogenous compounds, and in the generation of damaging toxic metabolites and/or oxygen stress. Oxygen 222-228 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-15 15237857-1 2004 Cytochrome P450 (CYP) enzymes in the brain may have a role in the activation or inactivation of centrally acting drugs, in the metabolism of endogenous compounds, and in the generation of damaging toxic metabolites and/or oxygen stress. Oxygen 222-228 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 17-20 15379059-1 2004 Cytochrome P450 (CYP) enzymes participate in the metabolism of a variety of naturally occurring and foreign compounds by reactions requiring NADPH and O2. Oxygen 151-153 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-15 15379059-1 2004 Cytochrome P450 (CYP) enzymes participate in the metabolism of a variety of naturally occurring and foreign compounds by reactions requiring NADPH and O2. Oxygen 151-153 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 17-20 12966104-4 2003 These are reminiscent of the mechanism of cytochrome P-450, where a heme iron stabilizes the activated O2 species. Oxygen 103-105 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 42-58 12966104-9 2003 In the context of the open and fully solvent-accessible active site for the homologous peptidylglycine-alpha-hydroxylating monooxygenase and by analogy to cytochrome P-450, the accumulation of a reduced and activated oxygen species in DbetaM before C-H cleavage would be expected to give some uncoupling of oxygen and substrate consumption. Oxygen 127-133 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 155-171 12966104-9 2003 In the context of the open and fully solvent-accessible active site for the homologous peptidylglycine-alpha-hydroxylating monooxygenase and by analogy to cytochrome P-450, the accumulation of a reduced and activated oxygen species in DbetaM before C-H cleavage would be expected to give some uncoupling of oxygen and substrate consumption. Oxygen 217-223 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 155-171 12363340-2 2002 Limitation of the dissolved oxygen supplied during cultivation of various microbial strains can decrease the activity of cytochrome P-450 monooxygenases required for the processing of pathway intermediates into their final forms, resulting in the accumulation of these intermediates as the primary products. Oxygen 28-34 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 121-137 10540427-2 1999 This process is the first structural evidence for an effective method for the activation of molecular oxygen as postulated for the cytochrome P-450 system. Oxygen 102-108 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 131-147 11427068-2 2001 An initial model compound was constructed from a structure obtained by 300-ps molecular dynamics simulation of compound I-formed P-450cam under physiologic conditions, and it consisted of porphine for protoporphyrin IX, S(-)-CH(3) for the side chain of Cys357 of the fifth ligand of heme, a methane molecule for the substrate, a heme iron, and an oxygen atom of the sixth ligand of heme. Oxygen 347-353 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 111-121 10499085-1 1999 Photoexcited iron porphyrins can be used to mimic the catalytic activity of cytochrome P-450 oxygenases both in the reduction of halogenated alkanes and in the oxidation of hydrocarbons by O2 itself at room temperature and atmospheric pressure. Oxygen 189-191 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 76-92 9654063-4 1998 A reaction pathway like that of cytochrome P-450 implies oxygen transfer to the substrate from the as yet uncharacterized iron-oxo species formed in the reaction of the heine cofactor with H2O2. Oxygen 57-63 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 32-48 9767182-3 1998 Active oxygen species formed by cytochrome P-450 isoforms can simultaneously act as stimulators of proliferation and inhibitors of intercellular communications. Oxygen 7-13 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 32-48 9578592-1 1998 In this paper two hypotheses are tested: (i) the active oxygen species is similar in energetics for all cytochrome P450 (CYP) enzymes and (ii) linear free-energy relationships can be used to evaluate the mechanism of the reaction of these enzymes. Oxygen 56-62 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 104-119 9578592-1 1998 In this paper two hypotheses are tested: (i) the active oxygen species is similar in energetics for all cytochrome P450 (CYP) enzymes and (ii) linear free-energy relationships can be used to evaluate the mechanism of the reaction of these enzymes. Oxygen 56-62 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 121-124 9654063-6 1998 The results of the present study exclude Fenton-type chemistry and prove that the minicatalyst is able to catalyze the oxygen incorporation by both peroxidase and cytochrome P-450 types of reaction pathways, while exchange occurs between the high-valency iron-oxo species and H2O. Oxygen 119-125 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 163-179 8916898-7 1996 Assuming the carbon monoxide complex as a model for the dioxygen complex, the more loosened binding of (1S)-camphor, therefore the increased water accessibility, and the weaker contact of the iron ligand to the I-helix might explain the higher amount of uncoupling of the cytochrome P-450 reaction cycle compared to that when (1R)-camphor is used as substrate. Oxygen 56-64 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 272-288 15374139-3 1997 Although this system is an important component of the defenses that protect living organisms against toxic chemicals, some reactions catalyzed by the cytochrome P-450 system result in the formation of products that are highly reactive as well as active oxygen species. Oxygen 253-259 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 150-166 8765221-1 1996 The reaction of mammalian cytochrome P-450 2B4 with nitrogen monoxide and oxygen has been studied by surface-enhanced resonance Raman scattering (SERRS) to obtain sharp and definitive information in situ on the nature of the changes in the active site pocket. Oxygen 74-80 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 26-42 2157443-4 1990 These observations support the hypothesis that, in the micromolar concentration range, o-naphthoquinones inhibit microsomal lipid peroxidation and cytochrome P-450-catalyzed reactions, by diverting reducing equivalents from NADPH to dioxygen. Oxygen 233-241 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 147-163 8673608-2 1996 Cytochrome P450eryF is unusual in having alanine in place of this threonine and an ordered active site water molecule (Wat 519) which is hydrogen bonded to the substrate 5-hydroxyl group and is in position to operate as an acid catalyst required for cleaving dioxygen. Oxygen 259-267 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-15 8818231-0 1996 The iron(II)/reductant (DH2)-induced activation of dioxygen for the demethylation of N-methylanilines: reaction mimic for the cytochrome P-450/reductase system. Oxygen 51-59 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 126-152 8586256-7 1995 Of all oxygen containing derivatives diamantane 1,6-dicarboxylic acid dimethylester only exhibited a pronounced ligand interaction with cytochrome P-450. Oxygen 7-13 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 136-152 7864832-20 1995 The striking contrast between DBM and cytochrome P-450, which carries out both epoxidation and allylic oxidation with non-conjugated olefinic substrates, is probably a reflection of the differences in redox potential of the activated oxygen species operative for these two enzymes. Oxygen 234-240 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 38-54 7532811-7 1994 As a cytochrome P-450, NOS catalyzes a heme-mediated reduction of molecular oxygen, resulting in the formation of H2O2 in the absence of L-arginine. Oxygen 76-82 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 5-21 8175769-9 1994 Cyt P450 Fe3+ is reduced by NADPH-cyt P450 reductase to cyt P450 Fe2+, which consumes oxygen in a stoichiometric proportion to produce cyt P450 Fe2+ O2, the resonance form of which is a perferryl moiety, cyt P450 Fe3+.O2-.. Oxygen 86-92 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-8 8175769-9 1994 Cyt P450 Fe3+ is reduced by NADPH-cyt P450 reductase to cyt P450 Fe2+, which consumes oxygen in a stoichiometric proportion to produce cyt P450 Fe2+ O2, the resonance form of which is a perferryl moiety, cyt P450 Fe3+.O2-.. Oxygen 86-92 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 34-42 8175769-9 1994 Cyt P450 Fe3+ is reduced by NADPH-cyt P450 reductase to cyt P450 Fe2+, which consumes oxygen in a stoichiometric proportion to produce cyt P450 Fe2+ O2, the resonance form of which is a perferryl moiety, cyt P450 Fe3+.O2-.. Oxygen 86-92 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 56-64 8175769-9 1994 Cyt P450 Fe3+ is reduced by NADPH-cyt P450 reductase to cyt P450 Fe2+, which consumes oxygen in a stoichiometric proportion to produce cyt P450 Fe2+ O2, the resonance form of which is a perferryl moiety, cyt P450 Fe3+.O2-.. Oxygen 86-92 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 56-64 8175769-9 1994 Cyt P450 Fe3+ is reduced by NADPH-cyt P450 reductase to cyt P450 Fe2+, which consumes oxygen in a stoichiometric proportion to produce cyt P450 Fe2+ O2, the resonance form of which is a perferryl moiety, cyt P450 Fe3+.O2-.. Oxygen 86-92 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 56-64 8175769-9 1994 Cyt P450 Fe3+ is reduced by NADPH-cyt P450 reductase to cyt P450 Fe2+, which consumes oxygen in a stoichiometric proportion to produce cyt P450 Fe2+ O2, the resonance form of which is a perferryl moiety, cyt P450 Fe3+.O2-.. Oxygen 149-151 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-8 8175769-9 1994 Cyt P450 Fe3+ is reduced by NADPH-cyt P450 reductase to cyt P450 Fe2+, which consumes oxygen in a stoichiometric proportion to produce cyt P450 Fe2+ O2, the resonance form of which is a perferryl moiety, cyt P450 Fe3+.O2-.. Oxygen 149-151 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 34-42 8175769-9 1994 Cyt P450 Fe3+ is reduced by NADPH-cyt P450 reductase to cyt P450 Fe2+, which consumes oxygen in a stoichiometric proportion to produce cyt P450 Fe2+ O2, the resonance form of which is a perferryl moiety, cyt P450 Fe3+.O2-.. Oxygen 149-151 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 56-64 8175769-9 1994 Cyt P450 Fe3+ is reduced by NADPH-cyt P450 reductase to cyt P450 Fe2+, which consumes oxygen in a stoichiometric proportion to produce cyt P450 Fe2+ O2, the resonance form of which is a perferryl moiety, cyt P450 Fe3+.O2-.. Oxygen 149-151 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 56-64 8175769-9 1994 Cyt P450 Fe3+ is reduced by NADPH-cyt P450 reductase to cyt P450 Fe2+, which consumes oxygen in a stoichiometric proportion to produce cyt P450 Fe2+ O2, the resonance form of which is a perferryl moiety, cyt P450 Fe3+.O2-.. Oxygen 149-151 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 56-64 8082573-6 1994 Certain amines appear to regulate O2 association with cytochrome P-450 and stabilize the various oxy species formed. Oxygen 34-36 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 54-70 8082573-8 1994 Small differences in protein structure between the various cytochrome P-450 subforms might serve to stabilize aminium radicals to permit oxygen rebound. Oxygen 137-143 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 59-75 8386241-4 1993 Covalent binding required oxygen and NADPH, and was decreased by the nucleophile glutathione and by the cytochrome P-450 inhibitors SKF 525-A, piperonyl butoxide and troleandomycin (an inhibitor of the cytochrome P-450 3A subfamily). Oxygen 26-32 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 104-120 8386241-4 1993 Covalent binding required oxygen and NADPH, and was decreased by the nucleophile glutathione and by the cytochrome P-450 inhibitors SKF 525-A, piperonyl butoxide and troleandomycin (an inhibitor of the cytochrome P-450 3A subfamily). Oxygen 26-32 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 202-218 8422907-4 1993 The LXA4 omega-hydroxylation requires both molecular oxygen and NADPH, and is inhibited by carbon monoxide, by antibodies raised against NADPH-cytochrome P-450 reductase, or competitively by leukotriene B4 (LTB4) and LTB5, substrates of LTB4 omega-hydroxylase. Oxygen 53-59 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 237-259 1328295-6 1992 This cytochrome P-450 mediated activity was oxygen- and NADPH-dependent and was inhibited 68% by 5 microM ketoconazole (P = 0.0035, n = 8) and 51% by carbon monoxide (P = 0.02, n = 6). Oxygen 44-50 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 5-21 1812974-3 1991 The first hypothesis concerns the role of the oxygen binding hemoprotein cytochrome P-450. Oxygen 46-52 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 73-89 2162582-2 1990 To exemplify the first-group reactions, cytochrome P-450 was studied, which is capable of generating different active forms of oxygen during the catalytic cycle. Oxygen 127-133 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 40-56 2162582-4 1990 In the course of the reaction, cytochrome P-450 also became inactivated under the effect of active oxygen. Oxygen 99-105 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 31-47 34163706-4 2021 The reaction of 2 with a triphenylcarbon radical further gives triphenylmethanol and mimics the so-called oxygen rebound step of Cpd II of cytochrome P450. Oxygen 106-112 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 139-154 2917971-2 1989 Cytochrome P-450 is known to catalyze the following oxygen transfer reaction: RH + PhIO----ROH + PhI where RH represents a variety of hydroxylatable substrates and PhIO a variety of iodosobenzene derivatives that serve as oxygen donors, and neither molecular oxygen nor an external electron donor is required. Oxygen 52-58 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-16 2555360-12 1989 Secondary amine mono-oxygenase is unique in its ability to function as cytochrome P-450 in activating molecular oxygen but to do so with a myoglobin-like active site. Oxygen 21-27 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 71-87 2600595-0 1989 Demethylation of tertiary amines by a reconstituted cytochrome P-450 enzyme system: kinetics of oxygen consumption and hydrogen peroxide formation. Oxygen 96-102 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 52-68 2600595-1 1989 Initial reaction rates of oxygen consumption and hydrogen peroxide formation in a cytochrome P-450 catalyzed reaction are practically independent of the nature of tertiary amines that were used as substrates. Oxygen 26-32 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 82-98 2690426-1 1989 Cytochrome P-450 appears to catalyse most monooxygenation reactions by sequential one-electron steps rather than by a single, concerted transfer of the ferryl oxygen to the substrate. Oxygen 46-52 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-16 2504483-4 1989 Thiotepa was shown to be metabolized under these conditions in a NADPH- and O2-dependent reaction that was catalyzed by one or more microsomal cytochrome P-450 enzymes that were present in the S-9 fraction. Oxygen 76-78 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 143-159 2504483-9 1989 These findings establish that the cytotoxic effects of thiotepa are oxygen dependent and may involve, at least in part, metabolic processes catalyzed by cytochrome P-450 enzymes. Oxygen 68-74 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 153-169 2753040-1 1989 Heme compounds, in combination with a reducing agent and oxygen, can express various activities of cytochrome P-450 enzymes. Oxygen 57-63 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 99-115 2917971-2 1989 Cytochrome P-450 is known to catalyze the following oxygen transfer reaction: RH + PhIO----ROH + PhI where RH represents a variety of hydroxylatable substrates and PhIO a variety of iodosobenzene derivatives that serve as oxygen donors, and neither molecular oxygen nor an external electron donor is required. Oxygen 222-228 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-16 2917971-2 1989 Cytochrome P-450 is known to catalyze the following oxygen transfer reaction: RH + PhIO----ROH + PhI where RH represents a variety of hydroxylatable substrates and PhIO a variety of iodosobenzene derivatives that serve as oxygen donors, and neither molecular oxygen nor an external electron donor is required. Oxygen 222-228 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-16 2854994-1 1988 Schemes are presented summarizing current knowledge of the mechanism of action of cytochrome P-450 when it functions either as a monooxygenase with molecular oxygen as the oxygen donor or as a peroxygenase with peroxy compounds as the oxygen donor. Oxygen 133-139 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 82-98 2854994-1 1988 Schemes are presented summarizing current knowledge of the mechanism of action of cytochrome P-450 when it functions either as a monooxygenase with molecular oxygen as the oxygen donor or as a peroxygenase with peroxy compounds as the oxygen donor. Oxygen 158-164 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 82-98 2663083-4 1989 Besides, some enzymes catalyzing the interconversions of active oxygen species (catalase superoxide dismutase, cytochrome P-450) are also inactivated in the course of catalysis under the oxidative action of active oxygen species. Oxygen 64-70 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 111-127 2663083-4 1989 Besides, some enzymes catalyzing the interconversions of active oxygen species (catalase superoxide dismutase, cytochrome P-450) are also inactivated in the course of catalysis under the oxidative action of active oxygen species. Oxygen 214-220 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 111-127 2519233-2 1989 A simplified model for cytochrome P-450 has been used by substituting the proposed biologically active ferric-oxene state of cytochrome P-450 by a singlet oxygen atom. Oxygen 155-161 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 23-39 2643542-3 1989 Release of oxidants during pseudosubstrate interaction with cytochrome P450s may be responsible for loss of enzymatic activity observed; enzyme activity can be protected by cytochrome P450 inhibitors, antioxidants, and lowered oxygen concentration. Oxygen 227-233 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 60-75 3127205-2 1988 The reaction required molecular oxygen and NADPH, and was significantly inhibited by carbon monoxide, suggesting that a cytochrome P-450 is involved. Oxygen 32-38 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 120-136 3127205-9 1988 These observations provide direct evidence that the oxygen-activating component of the LTB4 omega-hydroxylase system is a cytochrome P-450. Oxygen 52-58 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 87-109 3127205-9 1988 These observations provide direct evidence that the oxygen-activating component of the LTB4 omega-hydroxylase system is a cytochrome P-450. Oxygen 52-58 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 122-138 2854994-1 1988 Schemes are presented summarizing current knowledge of the mechanism of action of cytochrome P-450 when it functions either as a monooxygenase with molecular oxygen as the oxygen donor or as a peroxygenase with peroxy compounds as the oxygen donor. Oxygen 158-164 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 82-98 3039885-7 1987 Cytochrome P-450-dependent monooxygenases are also present in the lung where, in their suggested capacity as oxygen sensors, they generate metabolites of AA that modify pulmonary vasomotion. Oxygen 31-37 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-16 3111319-6 1987 Arachidonic acid (the precursor of PGE2) may inactivates cytochrome P-450, completely reverses the contractile tension of the DA at both low (4 to 12 torr) and high (511 to 712 torr) oxygen tension and is equally effective in the presence and absence of indomethacin. Oxygen 183-189 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 57-73 3030331-0 1987 Role of hepatic microsomal and purified cytochrome P-450 in one-electron reduction of two quinone imines and concomitant reduction of molecular oxygen. Oxygen 144-150 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 40-56 3549274-7 1986 The high content of antioxidant compounds in the adrenal cortex, principally ascorbate, may serve to protect cytochrome P-450 enzymes from the damaging effects of oxygen radical species formed as a result of cytochrome P-450/pseudosubstrate interactions. Oxygen 163-169 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 109-125 3030331-6 1987 Both the reduction of the quinone imines and the reduction of oxygen were found to be cytochrome P-450 dependent. Oxygen 62-68 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 86-102 3600619-0 1987 [Electron factors in the properties of cytochrome P-450 and mechanism of activation of molecular oxygen]. Oxygen 97-103 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 39-55 3449750-2 1987 The first proposed step is enzymatic alpha-hydroxylation by the active oxygen species of cytochrome P-450, followed by nonenzymatic N-dealkylation and formation of diazohydroxides (RNNOH). Oxygen 71-77 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 89-105 3021236-1 1986 A mitochondrial preparation from duck adrenal gland was used, under aerobic conditions, to show that the oxygen requirement for the last step of aldosterone biosynthesis (transformation of 18-hydroxycorticosterone into aldosterone) is at the cytochrome P-450 level only. Oxygen 105-111 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 242-258 3021236-2 1986 Vitamin C and tetramethyl-p-phenylene-diamine (TMPD) were used to increase oxygen consumption at the cytochrome a3 level, thereby decreasing its availability to cytochrome P-450. Oxygen 75-81 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 161-177 3021236-8 1986 According to polarographic and electron microscopy studies, the reversal of inhibition can only be explained by an increased availability of oxygen at the cytochrome P-450 level. Oxygen 141-147 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 155-171 3021236-9 1986 Experiments performed under aerobic conditions, without a nitrogen atmosphere, show that oxygen is required in the transformation of 18-hydroxycorticosterone into aldosterone, at the cytochrome P-450 level. Oxygen 89-95 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 183-199 22283296-0 1986 Oxygen activation by metalloporphyrins related to peroxidase and cytochrome P-450. Oxygen 0-6 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 65-81 3018103-2 1986 The ability of different IFN species to induce xanthine oxidase correlated with their ability to depress liver cytochrome P-450-dependent drug metabolism, supporting the hypothesis that reactive oxygen metabolites generated by xanthine oxidase might be responsible for this impairment of liver function by IFN. Oxygen 195-201 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 111-127 3549274-7 1986 The high content of antioxidant compounds in the adrenal cortex, principally ascorbate, may serve to protect cytochrome P-450 enzymes from the damaging effects of oxygen radical species formed as a result of cytochrome P-450/pseudosubstrate interactions. Oxygen 163-169 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 208-224 2985426-3 1985 CO, which inhibits the cytochrome P-450-dependent oxygen radical formation, had no effect on the oxidation reaction, suggesting that the source of the reactive oxygen species is not the microsomal mixed-function oxidase. Oxygen 50-56 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 23-39 2997155-5 1985 Consistent with a suicidal process, inactivation of the LTB4 omega-hydroxylase requires molecular oxygen and NADPH, is time-dependent, and follows pseudo-first-order kinetics. Oxygen 98-104 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 56-78 4053242-0 1985 Oxygen activation and olefin oxygenation by iron(III)porphyrin as a model of cytochrome P-450. Oxygen 0-6 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 77-93 4044832-6 1985 LTB4 omega-hydroxylase activity in isolated PMN membranes was linear with respect to duration of incubation and protein concentration, was maximal at pH 7.4, had a Km for LTB4 of 0.6 microM, and was dependent on oxygen and on reduced pyridine nucleotides (apparent Km for NADPH = 0.5 microM; apparent Km for NADH = 223 microM). Oxygen 212-218 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-22 6096874-0 1984 Base (O.-2, e-, or OH-)-induced autoxygenation of organic substrates: a model chemical system for cytochrome P-450-catalyzed monoxygenation and dehydrogenation by dioxygen. Oxygen 163-171 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 98-114 3890847-5 1985 The formation of the cytochrome P-450-reductase-complex necessary for oxygen activation by transfer of electrons is dependent on the charge of the phospholipids. Oxygen 70-76 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 21-37 6326394-0 1984 The influence of oxygen donor ligation on the spectroscopic properties of ferric cytochrome P-450: ester, ether and ketone co-ordination to the haem iron. Oxygen 17-23 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 81-97 6208195-3 1984 The monooxygenase is dependent upon NADPH plus oxygen, insensitive to CN-, and sensitive to CO. Microsomal oxidation is also sensitive to trypsin digestion, and reactivation is dependent upon the addition of purified, detergent-solubilized cytochrome P-450 reductase. Oxygen 8-14 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 240-256 6725272-2 1984 This laboratory has recently reported that, in a reconstituted enzyme system containing alcohol-induced isozyme 3a of liver microsomal cytochrome P-450, the sum of acetaldehyde generated by the monooxygenation of ethanol and of hydrogen peroxide produced by the NADPH oxidase activity is inadequate to account for the O2 and NADPH consumed. Oxygen 318-320 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 135-151 6587349-0 1984 Epoxidation of olefins by cytochrome P-450 model compounds: mechanism of oxygen atom transfer. Oxygen 73-79 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 26-42 6326394-8 1984 Anomalous spectral and substrate binding properties have been reported in the study of cytochrome P-450 under conditions employing solvents and non-phosphate buffers containing oxygen functionalities, and have been attributed to "solvent effects". Oxygen 177-183 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 87-103 6326394-9 1984 The present work, in combination with our previous report of alcohol, amide and carboxylate oxygen donor complexes of cytochrome P-450, is evidence that a wide variety of oxygen-donor species are capable of direct ligation to the haem iron of cytochrome P-450. Oxygen 92-98 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 118-134 6326394-9 1984 The present work, in combination with our previous report of alcohol, amide and carboxylate oxygen donor complexes of cytochrome P-450, is evidence that a wide variety of oxygen-donor species are capable of direct ligation to the haem iron of cytochrome P-450. Oxygen 92-98 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 243-259 6326394-9 1984 The present work, in combination with our previous report of alcohol, amide and carboxylate oxygen donor complexes of cytochrome P-450, is evidence that a wide variety of oxygen-donor species are capable of direct ligation to the haem iron of cytochrome P-450. Oxygen 171-177 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 118-134 6326394-9 1984 The present work, in combination with our previous report of alcohol, amide and carboxylate oxygen donor complexes of cytochrome P-450, is evidence that a wide variety of oxygen-donor species are capable of direct ligation to the haem iron of cytochrome P-450. Oxygen 171-177 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 243-259 6326394-10 1984 This leads us to suggest oxygen-donor ligation to cytochrome P-450 as the origin of spectral and substrate binding anomalies previously attributed to solvent effects. Oxygen 25-31 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 50-66 6372267-1 1984 This review presents current ideas, models and experimental data relating to the precise chemistry that links the transition metal active centre of cytochrome P-450 systems, the unactivated alkane substrate and the triplet atmospheric dioxygen molecule. Oxygen 235-243 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 148-164 6872096-5 1983 BHA addition effectively discharged the activated oxygen complex of cytochrome P-450 (liver microsomes) as well as Comp. Oxygen 50-56 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 68-84 6626210-1 1983 The filamentous fungus Aspergillus ochraceus TS produces an inducible microsomal cytochrome P-450 linked monooxygenase which is capable of hydroxylating benzo(a)pyrene in presence of O2 and NADPH. Oxygen 183-185 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 81-97 7217086-6 1981 Strong support is provided by the structure of this porphyrin for our contention that the prosthetic heme of cytochrome P-450 is alkylated during attempted transfer of the catalytically-activated oxygen to the pi-bond of destructive unsaturated substrates. Oxygen 196-202 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 109-125 6185486-10 1983 Although iron bleomycin does not have a polyaromatic structure like heme, many features of its electronic structure at the iron are very similar to those produced by the sulfur-coordinated heme iron of ferric cytochrome P-450, a protein that catalyzes a similar oxygen-dependent reaction. Oxygen 262-268 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 209-225 7161599-11 1982 Similarities between the hemin-mediated peroxide-supported reactions reported here, and the cytochrome P-450-mediated peroxide-supported reactions reinforce our earlier contentions that the alkaline hemin system appears to be a good model for the in vivo activation of oxygen by hemoproteins. Oxygen 269-275 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 92-108 6803786-0 1982 Mechanisms of hydroxylation by cytochrome P-450: exchange of iron-oxygen intermediates with water. Oxygen 66-72 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 31-47 7262071-4 1981 This establishes a role for cytochrome b5 in donating electrons for the reduction of oxy-cytochrome P-450 to the active oxygen complex of cytochrome P-450 but also points to large variations in the importance of this role depending on the experimental conditions, the species of P-450 involved and the substrates employed. Oxygen 120-126 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 89-105 7262071-4 1981 This establishes a role for cytochrome b5 in donating electrons for the reduction of oxy-cytochrome P-450 to the active oxygen complex of cytochrome P-450 but also points to large variations in the importance of this role depending on the experimental conditions, the species of P-450 involved and the substrates employed. Oxygen 120-126 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 138-154 7297957-1 1981 Hemoglobin and cytochrome P-450 have in common heme structure (i.e. protoporphyrin (IX), binding ability to molecular oxygen or carbon monoxide and enzyme-like activity (i.e. aniline hydroxylation; J.B.C. Oxygen 118-124 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 15-31 6773745-2 1980 This activity employs cytochrome P-450 as an oxygen donor. Oxygen 45-51 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 22-38 6929480-1 1980 Using isotopic tracer methods, we have shown that dihydrolipoic acid (2,3-thioctic acid) acylates the distal oxygen of ferrous oxygenated Pseudomonas cytochrome P-450, forming a transient acyl peroxide intermediate that facilitates oxygen-oxygen bond cleavage. Oxygen 127-133 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 150-166 7379213-5 1980 The finding that singlet oxygen will oxidise a cell constituent into a powerful inducer is compatible with the hypothesis that excited states of oxygen and their oxidation products may play a central role in the induction of cytochrome P-450 and associated enzyme activities by many chemically unrelated inducers. Oxygen 25-31 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 225-241 6929480-1 1980 Using isotopic tracer methods, we have shown that dihydrolipoic acid (2,3-thioctic acid) acylates the distal oxygen of ferrous oxygenated Pseudomonas cytochrome P-450, forming a transient acyl peroxide intermediate that facilitates oxygen-oxygen bond cleavage. Oxygen 127-133 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 150-166 6929480-0 1980 Chemical mechanisms for cytochrome P-450 hydroxylation: evidence for acylation of heme-bound dioxygen. Oxygen 93-101 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 24-40 517008-0 1979 Quantum chemical interpretation of the spectral properties of the CO and O2 complexes of hemoglobin and cytochrome P-450. Oxygen 73-75 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 104-120 6929480-1 1980 Using isotopic tracer methods, we have shown that dihydrolipoic acid (2,3-thioctic acid) acylates the distal oxygen of ferrous oxygenated Pseudomonas cytochrome P-450, forming a transient acyl peroxide intermediate that facilitates oxygen-oxygen bond cleavage. Oxygen 109-115 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 150-166 223025-7 1979 These effects are important from the point of view that the primary role of the heme of cytochrome P450 is the activation of molecular oxygen. Oxygen 135-141 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 88-103 42252-0 1979 Electrochemical investigations on the oxygen activation by cytochrome P-450. Oxygen 38-44 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 59-75 42252-7 1979 In contrast the cytochrome P-450 catalyzed NADPH-dependent reaction with the same substrate gives corticosterone, O2- represents only an intermediate in the activation of oxygen and is not the "activated oxygen" species. Oxygen 114-116 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 16-32 42252-7 1979 In contrast the cytochrome P-450 catalyzed NADPH-dependent reaction with the same substrate gives corticosterone, O2- represents only an intermediate in the activation of oxygen and is not the "activated oxygen" species. Oxygen 171-177 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 16-32 42252-9 1979 The interaction of adsorbed cytochrome P-450 on the electrode surface with the reduced oxygen species in the absence of NADPH was studied. Oxygen 87-93 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 28-44 517008-1 1979 The electronic transitions of CO and O2 complexes of hemoglobin and cytochrome P-450 were calculated using a PPP method extended for metal complexes. Oxygen 37-39 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 68-84 42252-12 1979 In a model of electro-enzyme-reactor several substrates were hydroxylated by microsomal cytochrome P-450 with cathodically reduced oxygen which substitutes NADPH. Oxygen 131-137 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 88-104 202259-0 1977 Relationship between the reduction of oxygen, artificial acceptors and cytochrome P-450 by NADPH--cytochrome c reductase. Oxygen 38-44 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 71-87 206545-0 1978 Studies of the oxygen binding site of cytochrome P-450. Oxygen 15-21 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 38-54 1160997-0 1975 Early role during chemical evolution for cytochrome P450 in oxygen detoxification. Oxygen 60-66 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 41-56 198028-6 1977 On the basis of the data obtained it is suggested that the reactions of NADPH-cytochrome c reductase interaction with oxygen and artificial "anaerobic" acceptors are connected with different redox-states of flavoprotein or with different flavine coenzymes, and that the electron transport on cytochrome P-450 and directly on oxygen takes place in interrelated redox-states of flavoprotein. Oxygen 118-124 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 292-308 198028-6 1977 On the basis of the data obtained it is suggested that the reactions of NADPH-cytochrome c reductase interaction with oxygen and artificial "anaerobic" acceptors are connected with different redox-states of flavoprotein or with different flavine coenzymes, and that the electron transport on cytochrome P-450 and directly on oxygen takes place in interrelated redox-states of flavoprotein. Oxygen 325-331 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 292-308 852592-0 1977 Sub-zero temperature studies of microsomal cytochrome P-450: interaction of Fe2+ with oxygen. Oxygen 86-92 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 43-59 19937-5 1977 The fact that the function of cytochrome P-450 is sensitive to changes in oxygen tension establishes its role as an "oxygen sensor" for cellular metabolism. Oxygen 74-80 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 30-46 19937-5 1977 The fact that the function of cytochrome P-450 is sensitive to changes in oxygen tension establishes its role as an "oxygen sensor" for cellular metabolism. Oxygen 117-123 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 30-46 824157-2 1976 Cytochrome P-450 serves as the binding site for oxygen and substrate while the reductase acts as an electron carrier shuttling electrons from NADPH to cytochrome P-450. Oxygen 48-54 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-16 824157-2 1976 Cytochrome P-450 serves as the binding site for oxygen and substrate while the reductase acts as an electron carrier shuttling electrons from NADPH to cytochrome P-450. Oxygen 48-54 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 151-167 12746-10 1976 In the mechanism of action of carbonyl cyanide m-chlorophenylhydrazone the key step may be the electrostatic interaction of its protonated form and one of the forms of activated oxygen at the catalytic centre of cytochrome P-450. Oxygen 178-184 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 212-228 1902-2 1975 In oxidation of NADP.H2 there were at least three point of molecular O2 reduction: NADP.H2-specific flavoprotein, Fe2+ participating in reactions of peroxidation of unsaturated fatty acids and cytochrome P-450. Oxygen 69-71 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 193-209 1216968-0 1975 Proceedings: The effects of adducts and the nature of activated oxygen for cytochrome P-450 catalyzed hydroxylation reactions. Oxygen 64-70 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 75-91 1902-3 1975 Efficiency of cytochrome P-450 inhibitors could not be evaluated by polarography as in the pathway several sites of molecular O2 activation were observed. Oxygen 126-128 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 14-30 33215946-9 2021 EXPERT OPINION: Overall, the CYP enzymes, depending upon the isoform, play a contributory or protective role in hyperoxic lung injury, and are, therefore, ideal candidates for developing drugs that can treat oxygen-mediated lung injury. Oxygen 208-214 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 29-32 33936006-1 2021 Cytochrome P450 enzymes, or P450s, are haem monooxygenases renowned for their ability to insert one atom from molecular oxygen into an exceptionally broad range of substrates while reducing the other atom to water. Oxygen 48-54 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-15 33592181-1 2021 Human cytochrome P450 enzymes (CYPs or P450s) are known to be reduced by their electron transfer partners in the absence of substrate and in turn to reduce other acceptor molecules such as molecular oxygen, thereby creating superoxide anions (O2- ). Oxygen 199-205 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 6-21 33592181-1 2021 Human cytochrome P450 enzymes (CYPs or P450s) are known to be reduced by their electron transfer partners in the absence of substrate and in turn to reduce other acceptor molecules such as molecular oxygen, thereby creating superoxide anions (O2- ). Oxygen 243-246 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 6-21 33461459-2 2021 BACKGROUND: Current pharmacokinetic investigations consider reactive oxygen species formed in microsomal reactions as toxic waste products, whereas our works (Manoj et al., 2016) showed that DROS are the reaction mainstay in cytochrome P450 mediated metabolism and that they play significant roles in explaining several unexplained physiologies (Parashar et al., 2018). Oxygen 69-75 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 225-240 30633519-2 2019 CYP450 is a nanomachine that uses dioxygen and two reducing and two proton equivalents to oxidize a plethora of molecules (so-called substrates) as a means of supplying bio-organisms with essential molecules (e.g., brain neurotransmitters, sex hormones, etc.) Oxygen 34-42 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-6 25793416-1 2015 Cytochrome P450 enzymes are renowned for their ability to insert oxygen into an enormous variety of compounds with a high degree of chemo- and regio-selectivity under mild conditions. Oxygen 65-71 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-15 29266939-1 2018 Cytochrome P450 (CYP) monooxygenases catalyze the oxidation of chemically inert carbon-hydrogen bonds in diverse endogenous and exogenous organic compounds by atmospheric oxygen. Oxygen 26-32 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-15 29266939-1 2018 Cytochrome P450 (CYP) monooxygenases catalyze the oxidation of chemically inert carbon-hydrogen bonds in diverse endogenous and exogenous organic compounds by atmospheric oxygen. Oxygen 26-32 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 17-20 27727524-1 2016 Cytochrome P450 enzymes are heme-containing mono-oxygenases that mainly react through oxygen-atom transfer. Oxygen 49-55 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-15 26233903-4 2015 CYP enzymes catalyze the oxygenation of an organic substrate and the simultaneous reduction of molecular oxygen. Oxygen 25-31 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-3 29560240-1 2015 Cytochrome P450 enzymes are heme based monoxygenases that catalyse a range of oxygen atom transfer reactions with various substrates, including aliphatic and aromatic hydroxylation as well as epoxidation reactions. Oxygen 42-48 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-15 26002730-2 2015 CYP enzymes catalyze monooxygenation reactions by inserting one oxygen atom from O2 into an enormous number and variety of substrates. Oxygen 25-31 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-3 26002730-2 2015 CYP enzymes catalyze monooxygenation reactions by inserting one oxygen atom from O2 into an enormous number and variety of substrates. Oxygen 81-83 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-3 26002730-5 2015 CYP-mediated hydroxylations occur via a consensus H atom abstraction/oxygen rebound mechanism involving an initial abstraction by CpdI of a H atom from the substrate, generating a highly-reactive protonated Compound II (CpdII) intermediate (FeIV-OH) and a carbon-centered alkyl radical that rebounds onto the ferryl hydroxyl moiety to yield the hydroxylated substrate. Oxygen 69-75 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-3 26002730-6 2015 CYP enzymes utilize hydroperoxides, peracids, perborate, percarbonate, periodate, chlorite, iodosobenzene and N-oxides as surrogate oxygen atom donors to oxygenate substrates via the shunt pathway in the absence of NAD(P)H/O2 and reduction-oxidation (redox) auxiliary proteins. Oxygen 132-138 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-3 26002730-6 2015 CYP enzymes utilize hydroperoxides, peracids, perborate, percarbonate, periodate, chlorite, iodosobenzene and N-oxides as surrogate oxygen atom donors to oxygenate substrates via the shunt pathway in the absence of NAD(P)H/O2 and reduction-oxidation (redox) auxiliary proteins. Oxygen 223-225 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-3 24233717-1 2013 Cytochrome P450 enzymes activate oxygen at heme iron centers to oxidize relatively inert substrate carbon-hydrogen bonds. Oxygen 33-39 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-15 24117377-4 2013 CYP on polycrystalline ITO film enhanced the electron transfer rate of oxygen reduction about fifteen times more than with amorphous film. Oxygen 71-77 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-3 24117377-6 2013 The oxygen reduction current at the polycrystalline ITO film electrodes had increased 3- to 4-fold, specifically coupled with the oxidation of drugs (testosterone and quinidine) by the monooxygenase activity of CYP. Oxygen 4-10 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 211-214 24117377-7 2013 In contrast, the oxygen reduction current completely disappeared in the presence of the CYP inhibitor (ketoconazole). Oxygen 17-23 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 88-91 22929863-4 2012 In this study, we show that the electrocatalytic oxidation of hydrogen peroxide on a platinum electrode generates reactive oxygen species, presumably surface-bound platinum-oxo species, which are capable of oxygen insertion reactions in analogy to oxo-ferryl radical cations in the active site of Cytochrome P450. Oxygen 123-129 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 297-312