PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30427570-4 2019 Application of this technique to human NADPH-cytochrome P450 reductase (CPR) demonstrated the importance of homogenously labeled samples for accurate determination of FRET efficiencies and unveiled the effect of NADP+ on the ionic-strength-dependent modulation of the conformational equilibrium of CPR. NADP 212-217 cytochrome p450 oxidoreductase Homo sapiens 39-70 30427570-4 2019 Application of this technique to human NADPH-cytochrome P450 reductase (CPR) demonstrated the importance of homogenously labeled samples for accurate determination of FRET efficiencies and unveiled the effect of NADP+ on the ionic-strength-dependent modulation of the conformational equilibrium of CPR. NADP 212-217 cytochrome p450 oxidoreductase Homo sapiens 72-75 29308883-1 2018 Conformational changes in NADPH-cytochrome P450 oxidoreductase (CYPOR) associated with electron transfer from NADPH to electron acceptors via FAD and FMN have been investigated via structural studies of the four-electron-reduced NADP+-bound enzyme and kinetic and structural studies of mutants that affect the conformation of the mobile Gly631-Asn635 loop (Asp632 loop). NADP 26-31 cytochrome p450 oxidoreductase Homo sapiens 64-69 29363234-3 2018 Light-dependent NADPH: protochlorophyllide oxidoreductase (POR) catalyzes the stereospecific trans addition of a hydride anion and a proton across the C17 -C18 double bond of protochlorophyllide. NADP 16-21 cytochrome p450 oxidoreductase Homo sapiens 23-57 29363234-3 2018 Light-dependent NADPH: protochlorophyllide oxidoreductase (POR) catalyzes the stereospecific trans addition of a hydride anion and a proton across the C17 -C18 double bond of protochlorophyllide. NADP 16-21 cytochrome p450 oxidoreductase Homo sapiens 59-62 29308883-1 2018 Conformational changes in NADPH-cytochrome P450 oxidoreductase (CYPOR) associated with electron transfer from NADPH to electron acceptors via FAD and FMN have been investigated via structural studies of the four-electron-reduced NADP+-bound enzyme and kinetic and structural studies of mutants that affect the conformation of the mobile Gly631-Asn635 loop (Asp632 loop). NADP 229-234 cytochrome p450 oxidoreductase Homo sapiens 26-62 29308883-1 2018 Conformational changes in NADPH-cytochrome P450 oxidoreductase (CYPOR) associated with electron transfer from NADPH to electron acceptors via FAD and FMN have been investigated via structural studies of the four-electron-reduced NADP+-bound enzyme and kinetic and structural studies of mutants that affect the conformation of the mobile Gly631-Asn635 loop (Asp632 loop). NADP 229-234 cytochrome p450 oxidoreductase Homo sapiens 64-69 29308883-2 2018 The structure of four-electron-reduced, NADP+-bound wild type CYPOR shows the plane of the nicotinamide ring positioned perpendicular to the FAD isoalloxazine with its carboxamide group forming H-bonds with N1 of the flavin ring and the Thr535 hydroxyl group. NADP 40-45 cytochrome p450 oxidoreductase Homo sapiens 62-67 29308883-5 2018 Structures of the mutants and reduced wild type CYPOR permit us to identify a possible pathway for NADP(H) binding to and release from CYPOR. NADP 99-106 cytochrome p450 oxidoreductase Homo sapiens 48-53 29308883-5 2018 Structures of the mutants and reduced wild type CYPOR permit us to identify a possible pathway for NADP(H) binding to and release from CYPOR. NADP 99-106 cytochrome p450 oxidoreductase Homo sapiens 135-140 29148818-1 2017 Cytochrome P450-reductase (CPR) is a versatile NADPH-dependent electron donor located in the cytoplasmic side of the endoplasmic reticulum. NADP 47-52 cytochrome p450 oxidoreductase Homo sapiens 0-25 29148818-1 2017 Cytochrome P450-reductase (CPR) is a versatile NADPH-dependent electron donor located in the cytoplasmic side of the endoplasmic reticulum. NADP 47-52 cytochrome p450 oxidoreductase Homo sapiens 27-30 29148818-7 2017 An Arrhenius analysis of diffusion constants was also carried out, demonstrating that the reduced forms of CPR and CYP2C9 interact differently with the biomimetic ER and may, in addition to protein conformational changes, contribute to the observed NADPH-dependent shift in Kd. NADP 249-254 cytochrome p450 oxidoreductase Homo sapiens 107-110 27558805-8 2016 NQO1 and CYP450OR exhibited a reciprocal preference for reducing equivalents in beta-cells: while CYP450OR preferentially utilized NADPH, NQO1 primarily utilized NADH. NADP 131-136 cytochrome p450 oxidoreductase Homo sapiens 9-17 28347139-0 2017 Single-Protein Tracking Reveals That NADPH Mediates the Insertion of Cytochrome P450 Reductase into a Biomimetic of the Endoplasmic Reticulum. NADP 37-42 cytochrome p450 oxidoreductase Homo sapiens 69-94 28347139-3 2017 Herein, we report that, contrary to this belief, CPR can exist as a peripheral membrane protein in the absence of NADPH and will transition to an integral membrane protein in the presence of stoichiometric amounts of NADPH or greater. NADP 114-119 cytochrome p450 oxidoreductase Homo sapiens 49-52 28347139-3 2017 Herein, we report that, contrary to this belief, CPR can exist as a peripheral membrane protein in the absence of NADPH and will transition to an integral membrane protein in the presence of stoichiometric amounts of NADPH or greater. NADP 217-222 cytochrome p450 oxidoreductase Homo sapiens 49-52 28347139-7 2017 These studies revealed dramatic changes in diffusion coefficient and the degree of partitioning of CPR as a function of NADPH concentration. NADP 120-125 cytochrome p450 oxidoreductase Homo sapiens 99-102 28480030-4 2017 Brain microsomes of Sprague-Dawley rats or recombinant human cytochrome P450 reductase (CPR) were incubated with NADPH and various drugs in closed vials in phosphate buffer at pH 7.4 and 37 C. After 15 minutes, the reaction was stopped by cooling in dry ice, and the headspace gas was analyzed for CO production using gas chromatography with reductive (mercuric oxide) detection. NADP 113-118 cytochrome p450 oxidoreductase Homo sapiens 88-91 27863990-11 2017 However, POR-/- abolished the signal in NADPH-stimulated assays using membrane fractions from the very same cells. NADP 40-45 cytochrome p450 oxidoreductase Homo sapiens 9-12 29163152-2 2017 CPR contains 3 distinct functional domains: a FMN-binding domain (acceptor reduction), a linker (hinge), and a connecting/FAD domain (NADPH oxidation). NADP 134-139 cytochrome p450 oxidoreductase Homo sapiens 0-3 28618157-1 2017 The haem-containing mono-oxygenase cytochrome P450 3A4 (CYP3A4) and its redox partner NADPH-dependent cytochrome P450 oxidoreductase (CPR) are among the most important enzymes in human liver for metabolizing drugs and xenobiotic compounds. NADP 86-91 cytochrome p450 oxidoreductase Homo sapiens 102-132 28188256-2 2017 POR reduces one of the double bonds of the protochlorophyllide (Pchlide) using NADPH and light. NADP 79-84 cytochrome p450 oxidoreductase Homo sapiens 0-3 28188256-4 2017 Moreover, we showed for the first time that NADH can, like NADPH, form active complexes with Pchlide and POR, however, at much higher concentrations. NADP 59-64 cytochrome p450 oxidoreductase Homo sapiens 105-108 28188256-5 2017 Additionally, monogalactosyldiacylglycerol (MGDG) was shown to be the main factor responsible for the red shift of the fluorescence emission maximum of Pchlide:POR:NADPH complexes. NADP 164-169 cytochrome p450 oxidoreductase Homo sapiens 160-163 27032764-1 2017 Cytochrome P450 aromatase (CYP19A1), in human placenta metabolizes androgens to estrogens and uses reduced nicotinamide adenine dinucleotide phosphate through cytochrome P450 oxidoreductase (POR) for the energy requirements of its metabolic activities. NADP 107-150 cytochrome p450 oxidoreductase Homo sapiens 159-189 27032764-1 2017 Cytochrome P450 aromatase (CYP19A1), in human placenta metabolizes androgens to estrogens and uses reduced nicotinamide adenine dinucleotide phosphate through cytochrome P450 oxidoreductase (POR) for the energy requirements of its metabolic activities. NADP 107-150 cytochrome p450 oxidoreductase Homo sapiens 191-194 27737328-2 2016 The POR gene encodes a flavor protein that transfers electrons from nicotinamide adenine dinucleotide phosphate (NADPH) to all microsomal cytochrome P450 type II (including 21-hydroxylase, 17alpha-hydroxylase 17,20 lyase and aromatase), which is fundamental for their enzymatic activity. NADP 68-111 cytochrome p450 oxidoreductase Homo sapiens 4-7 27737328-2 2016 The POR gene encodes a flavor protein that transfers electrons from nicotinamide adenine dinucleotide phosphate (NADPH) to all microsomal cytochrome P450 type II (including 21-hydroxylase, 17alpha-hydroxylase 17,20 lyase and aromatase), which is fundamental for their enzymatic activity. NADP 113-118 cytochrome p450 oxidoreductase Homo sapiens 4-7 27558805-8 2016 NQO1 and CYP450OR exhibited a reciprocal preference for reducing equivalents in beta-cells: while CYP450OR preferentially utilized NADPH, NQO1 primarily utilized NADH. NADP 131-136 cytochrome p450 oxidoreductase Homo sapiens 98-106 27404282-3 2016 We also studied the efficiencies of the coenzymes of these reductases, NADPH as a coenzyme of POR, and NADH as a coenzyme of CBR, to mediate BaP oxidation. NADP 71-76 cytochrome p450 oxidoreductase Homo sapiens 94-97 27461959-1 2016 Cytochrome P450 reductase (CPR) contains a loop within the active site (comprising Asp(634), Ala(635), Arg(636) and Asn(637); human CPR numbering) that relocates upon NADPH binding. NADP 167-172 cytochrome p450 oxidoreductase Homo sapiens 0-25 27461959-1 2016 Cytochrome P450 reductase (CPR) contains a loop within the active site (comprising Asp(634), Ala(635), Arg(636) and Asn(637); human CPR numbering) that relocates upon NADPH binding. NADP 167-172 cytochrome p450 oxidoreductase Homo sapiens 27-30 27461959-1 2016 Cytochrome P450 reductase (CPR) contains a loop within the active site (comprising Asp(634), Ala(635), Arg(636) and Asn(637); human CPR numbering) that relocates upon NADPH binding. NADP 167-172 cytochrome p450 oxidoreductase Homo sapiens 132-135 27404282-10 2016 They suggest that NADH-dependent CBR can replace NADPH-dependent POR in the P450 1A1-catalyzed metabolism of BaP. NADP 49-54 cytochrome p450 oxidoreductase Homo sapiens 65-68 27285815-5 2016 Here, we have used static and time-resolved spectroscopic measurements of a number of active site variants to study the role of a number of residues, which are located in the proposed NADPH/Pchlide binding site based on previous homology models, in the reaction mechanism of POR. NADP 184-189 cytochrome p450 oxidoreductase Homo sapiens 275-278 26850353-10 2016 Differences in the kinetic parameters of human and mosquito CPR in terms of NADPH binding have been demonstrated and could potentially be used to design species specific pesticides. NADP 76-81 cytochrome p450 oxidoreductase Homo sapiens 60-63 26172514-2 2015 Here we compare nanodisc formation for NADPH-dependent cytochrome P450 oxidoreductase (POR) using two different scaffold proteins, MSP1D1 and MSP1E3D1. NADP 39-44 cytochrome p450 oxidoreductase Homo sapiens 87-90 26361974-7 2015 In combination, the data reveal differences in rate-determining steps between plant CPR and their mammalian equivalent in mediating the flux of reducing equivalents from NADPH to external electron acceptors. NADP 170-175 cytochrome p450 oxidoreductase Homo sapiens 84-87 26293521-1 2015 BACKGROUND AND OBJECTIVE: The polymorphic enzyme P450 oxidoreductase (POR) transfers electrons from nicotinamide adenine dinucleotide phosphate (NADPH) to cytochrome P450 (CYP) 3A enzyme s, which metabolize atorvastatin. NADP 100-143 cytochrome p450 oxidoreductase Homo sapiens 49-68 26293521-1 2015 BACKGROUND AND OBJECTIVE: The polymorphic enzyme P450 oxidoreductase (POR) transfers electrons from nicotinamide adenine dinucleotide phosphate (NADPH) to cytochrome P450 (CYP) 3A enzyme s, which metabolize atorvastatin. NADP 100-143 cytochrome p450 oxidoreductase Homo sapiens 70-73 26293521-1 2015 BACKGROUND AND OBJECTIVE: The polymorphic enzyme P450 oxidoreductase (POR) transfers electrons from nicotinamide adenine dinucleotide phosphate (NADPH) to cytochrome P450 (CYP) 3A enzyme s, which metabolize atorvastatin. NADP 145-150 cytochrome p450 oxidoreductase Homo sapiens 49-68 26293521-1 2015 BACKGROUND AND OBJECTIVE: The polymorphic enzyme P450 oxidoreductase (POR) transfers electrons from nicotinamide adenine dinucleotide phosphate (NADPH) to cytochrome P450 (CYP) 3A enzyme s, which metabolize atorvastatin. NADP 145-150 cytochrome p450 oxidoreductase Homo sapiens 70-73 26361974-2 2015 While all three CPR forms elicit comparable rates for cytochrome c(3+) turnover, NADPH reduction of the FAD cofactor is ~50-fold faster in aaCPR and ATR2 compared to hCPR, with a kobs of ~500 s(-1) (6 C). NADP 81-86 cytochrome p450 oxidoreductase Homo sapiens 166-170 26361974-4 2015 In hCPR, transfer of a hydride ion from NADPH to FAD is tightly coupled to subsequent FAD to FMN electron transfer, indicating that the former catalytic event is slow relative to the latter. NADP 40-45 cytochrome p450 oxidoreductase Homo sapiens 3-7 25517035-1 2014 UNLABELLED: The enzymatic reactivity of a series of benzo[1,2-c]1,2,5-oxadiazole N-oxides (benzofuroxans; BFXs) towards mammalian single-electron transferring NADPH:cytochrome P-450 reductase (P-450R) and two-electron (hydride) transferring NAD(P)H: quinone oxidoreductase (NQO1) was examined in this work. NADP 159-164 cytochrome p450 oxidoreductase Homo sapiens 176-191 25728647-1 2015 Cytochrome P450 oxidoreductase (POR) is a 2-flavin protein that transfers electrons from NADPH via its FAD and FMN moieties to all microsomal cytochrome P450 enzymes, including steroidogenic and drug-metabolizing P450s. NADP 89-94 cytochrome p450 oxidoreductase Homo sapiens 11-30 25728647-1 2015 Cytochrome P450 oxidoreductase (POR) is a 2-flavin protein that transfers electrons from NADPH via its FAD and FMN moieties to all microsomal cytochrome P450 enzymes, including steroidogenic and drug-metabolizing P450s. NADP 89-94 cytochrome p450 oxidoreductase Homo sapiens 32-35 25728647-6 2015 Transient kinetic dissection of the reaction of POR with NADPH and the reduction in cytochrome c by POR using stopped-flow techniques revealed defects in individual electron transfer steps mediated by A287P. NADP 57-62 cytochrome p450 oxidoreductase Homo sapiens 48-51 26066995-6 2015 CYP3A4-substrate binding, reduction of CPR with NADPH, and interflavin and interprotein electron transfer were identified as citrate-sensitive steps. NADP 48-53 cytochrome p450 oxidoreductase Homo sapiens 39-42 25517035-3 2014 The reduction of BFXs by both P-450R and NQO1 was accompanied by O2 uptake, which was much lower than the NADPH oxidation rate; except for annelated BFXs, whose reduction was followed by the production of peroxide. NADP 106-111 cytochrome p450 oxidoreductase Homo sapiens 30-36 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). NADP 151-156 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). NADP 151-156 cytochrome p450 oxidoreductase Homo sapiens 188-191 25521355-3 2014 The polymorphic enzyme POR transfers electrons from NADPH to CYP450 enzymes including CYP3A, which metabolize atorvastatin. NADP 52-57 cytochrome p450 oxidoreductase Homo sapiens 23-26 25517035-1 2014 UNLABELLED: The enzymatic reactivity of a series of benzo[1,2-c]1,2,5-oxadiazole N-oxides (benzofuroxans; BFXs) towards mammalian single-electron transferring NADPH:cytochrome P-450 reductase (P-450R) and two-electron (hydride) transferring NAD(P)H: quinone oxidoreductase (NQO1) was examined in this work. NADP 159-164 cytochrome p450 oxidoreductase Homo sapiens 193-200 23332101-1 2013 Methionine synthase reductase (MSR) and cytochrome P450 reductase (CPR) transfer reducing equivalents from NADPH via an FAD and FMN cofactor to a redox partner protein. NADP 107-112 cytochrome p450 oxidoreductase Homo sapiens 40-65 24322786-5 2014 However, when NADPH was replaced by a direct electron donor to CYPs, cumene hydroperoxide, hereby bypassing the CYP oxidoreductase (POR), all variant enzymes were active, indicating unproductive interactions between CYP2C9.35 and POR. NADP 14-19 cytochrome p450 oxidoreductase Homo sapiens 132-135 24322786-5 2014 However, when NADPH was replaced by a direct electron donor to CYPs, cumene hydroperoxide, hereby bypassing the CYP oxidoreductase (POR), all variant enzymes were active, indicating unproductive interactions between CYP2C9.35 and POR. NADP 14-19 cytochrome p450 oxidoreductase Homo sapiens 230-233 24322786-7 2014 In conclusion, our data strongly suggest that the Arg125Leu mutation in CYP2C9.35 prevents CYP2C9-POR interactions resulting in the absence of NADPH-dependent CYP2C9-catalyzed activity in vivo, thus influencing the warfarin sensitivity in the carriers of this allele. NADP 143-148 cytochrome p450 oxidoreductase Homo sapiens 98-101 24589657-1 2014 Cytochrome P450 reductase (CPR) and methionine synthase reductase (MSR) transfer reducing equivalents from NADPH to FAD to FMN. NADP 107-112 cytochrome p450 oxidoreductase Homo sapiens 0-25 24589657-1 2014 Cytochrome P450 reductase (CPR) and methionine synthase reductase (MSR) transfer reducing equivalents from NADPH to FAD to FMN. NADP 107-112 cytochrome p450 oxidoreductase Homo sapiens 27-30 24196959-0 2013 Zinc finger nuclease knock-out of NADPH:cytochrome P450 oxidoreductase (POR) in human tumor cell lines demonstrates that hypoxia-activated prodrugs differ in POR dependence. NADP 34-39 cytochrome p450 oxidoreductase Homo sapiens 51-70 24196959-0 2013 Zinc finger nuclease knock-out of NADPH:cytochrome P450 oxidoreductase (POR) in human tumor cell lines demonstrates that hypoxia-activated prodrugs differ in POR dependence. NADP 34-39 cytochrome p450 oxidoreductase Homo sapiens 72-75 24196959-0 2013 Zinc finger nuclease knock-out of NADPH:cytochrome P450 oxidoreductase (POR) in human tumor cell lines demonstrates that hypoxia-activated prodrugs differ in POR dependence. NADP 34-39 cytochrome p450 oxidoreductase Homo sapiens 158-161 24430948-2 2014 The polymorphic enzyme P450 oxidoreductase (POR) transfers electrons from nicotinamide adenine dinucleotide phosphate (NADPH) to cytochrome P450 (CYP) 3A enzymes, which metabolize atorvastatin and simvastatin. NADP 74-117 cytochrome p450 oxidoreductase Homo sapiens 23-42 24430948-2 2014 The polymorphic enzyme P450 oxidoreductase (POR) transfers electrons from nicotinamide adenine dinucleotide phosphate (NADPH) to cytochrome P450 (CYP) 3A enzymes, which metabolize atorvastatin and simvastatin. NADP 74-117 cytochrome p450 oxidoreductase Homo sapiens 44-47 24430948-2 2014 The polymorphic enzyme P450 oxidoreductase (POR) transfers electrons from nicotinamide adenine dinucleotide phosphate (NADPH) to cytochrome P450 (CYP) 3A enzymes, which metabolize atorvastatin and simvastatin. NADP 119-124 cytochrome p450 oxidoreductase Homo sapiens 23-42 24430948-2 2014 The polymorphic enzyme P450 oxidoreductase (POR) transfers electrons from nicotinamide adenine dinucleotide phosphate (NADPH) to cytochrome P450 (CYP) 3A enzymes, which metabolize atorvastatin and simvastatin. NADP 119-124 cytochrome p450 oxidoreductase Homo sapiens 44-47 24299267-4 2013 CPR from A. annua shows a 3.5-fold increase in uncoupled NADPH oxidation compared to human CPR and a strong preference (85 100-fold) for NADPH over NADH. NADP 57-62 cytochrome p450 oxidoreductase Homo sapiens 0-3 24299267-4 2013 CPR from A. annua shows a 3.5-fold increase in uncoupled NADPH oxidation compared to human CPR and a strong preference (85 100-fold) for NADPH over NADH. NADP 137-142 cytochrome p450 oxidoreductase Homo sapiens 0-3 23332101-1 2013 Methionine synthase reductase (MSR) and cytochrome P450 reductase (CPR) transfer reducing equivalents from NADPH via an FAD and FMN cofactor to a redox partner protein. NADP 107-112 cytochrome p450 oxidoreductase Homo sapiens 67-70 23475681-1 2013 P450 oxidoreductase (POR) is the flavoprotein that transfers electrons from NADPH to microsomal cytochrome P450 enzymes and to some other proteins. NADP 76-81 cytochrome p450 oxidoreductase Homo sapiens 0-19 22809523-3 2013 CYP reactions in vivo require the cofactor NADPH as the source of electrons and an additional enzyme, cytochrome P450 reductase (CPR), as the electron transfer partner; consequently, any laboratory or industrial use of CYPs is limited by the need to supply NADPH and CPR. NADP 257-262 cytochrome p450 oxidoreductase Homo sapiens 102-127 22809523-3 2013 CYP reactions in vivo require the cofactor NADPH as the source of electrons and an additional enzyme, cytochrome P450 reductase (CPR), as the electron transfer partner; consequently, any laboratory or industrial use of CYPs is limited by the need to supply NADPH and CPR. NADP 257-262 cytochrome p450 oxidoreductase Homo sapiens 129-132 23475681-1 2013 P450 oxidoreductase (POR) is the flavoprotein that transfers electrons from NADPH to microsomal cytochrome P450 enzymes and to some other proteins. NADP 76-81 cytochrome p450 oxidoreductase Homo sapiens 21-24 22120726-6 2012 The CPR activity was quantified using NADPH fluorescence at lambda(Ex) = 340 nm and lambda(Em) = 450 nm. NADP 38-43 cytochrome p450 oxidoreductase Homo sapiens 4-7 24362093-9 2013 Human CYP1A1 expressed with NADPH:CYP reductase (POR) in Supersomes oxidized BaP to the same metabolites as microsomes, but BaP-4,5-dihydrodiol has not been detected. NADP 28-33 cytochrome p450 oxidoreductase Homo sapiens 49-52 22543241-1 2012 The NADPH cytochrome P450 reductase (CPR), a diflavin enzyme, catalyzes the electron transfer (ET) from NADPH to the substrate P450. NADP 4-9 cytochrome p450 oxidoreductase Homo sapiens 37-40 22205152-2 2012 It was found that at a high NADPH concentration (500 mumol/l), the anthracenedione agent ametantrone, with an unmodified quinone structure, was susceptible to CPR-dependent reductive activation. NADP 28-33 cytochrome p450 oxidoreductase Homo sapiens 159-162 22205878-6 2011 Open and closed states of CPR were correlated with key steps in the catalytic cycle which demonstrated how redox chemistry and NADPH binding drive successive opening and closing of the enzyme. NADP 127-132 cytochrome p450 oxidoreductase Homo sapiens 26-29 22123124-1 2012 Cytochrome P450 oxidoreductase (POR) transfers electrons from NADPH to several oxygenase enzymes including cytochrome P450 (CYP). NADP 62-67 cytochrome p450 oxidoreductase Homo sapiens 0-30 22123124-1 2012 Cytochrome P450 oxidoreductase (POR) transfers electrons from NADPH to several oxygenase enzymes including cytochrome P450 (CYP). NADP 62-67 cytochrome p450 oxidoreductase Homo sapiens 32-35 22205878-10 2011 Motions critical to the broader biological functions of CPR are tightly coupled to enzyme chemistry in the human NADPH-CPR-CYP redox chain. NADP 113-118 cytochrome p450 oxidoreductase Homo sapiens 56-59 22205878-10 2011 Motions critical to the broader biological functions of CPR are tightly coupled to enzyme chemistry in the human NADPH-CPR-CYP redox chain. NADP 113-118 cytochrome p450 oxidoreductase Homo sapiens 119-122 21659470-6 2011 Presteady-state measurements of the rate of electron transfer from NADPH-dependent cytochrome P450 reductase (CPR) to CYP2B6.8 using stopped-flow spectrophotometry revealed that CYP2B6.8 is incapable of accepting electrons from CPR. NADP 67-72 cytochrome p450 oxidoreductase Homo sapiens 83-108 21323388-3 2011 P450-catalyzed monooxygenations are dependent on electron donation typically from NADPH catalyzed by NADPH-cytochrome P450 oxidoreductase (CPR). NADP 82-87 cytochrome p450 oxidoreductase Homo sapiens 101-137 21323388-3 2011 P450-catalyzed monooxygenations are dependent on electron donation typically from NADPH catalyzed by NADPH-cytochrome P450 oxidoreductase (CPR). NADP 82-87 cytochrome p450 oxidoreductase Homo sapiens 139-142 21659470-6 2011 Presteady-state measurements of the rate of electron transfer from NADPH-dependent cytochrome P450 reductase (CPR) to CYP2B6.8 using stopped-flow spectrophotometry revealed that CYP2B6.8 is incapable of accepting electrons from CPR. NADP 67-72 cytochrome p450 oxidoreductase Homo sapiens 110-113 21659470-6 2011 Presteady-state measurements of the rate of electron transfer from NADPH-dependent cytochrome P450 reductase (CPR) to CYP2B6.8 using stopped-flow spectrophotometry revealed that CYP2B6.8 is incapable of accepting electrons from CPR. NADP 67-72 cytochrome p450 oxidoreductase Homo sapiens 228-231 21345800-1 2011 The crystal structure of NADPH-cytochrome P450 reductase (CYPOR) implies that a large domain movement is essential for electron transfer from NADPH via FAD and FMN to its redox partners. NADP 25-30 cytochrome p450 oxidoreductase Homo sapiens 58-63 21345800-9 2011 Furthermore, comparison of these mutant and wild type structures strongly suggests that the Gly(631)-Asn(635) loop movement controls NADPH binding and NADP(+) release; this loop movement in turn facilitates the flavin domain movement, allowing electron transfer from FMN to the CYPOR redox partners. NADP 133-138 cytochrome p450 oxidoreductase Homo sapiens 278-283 21345800-9 2011 Furthermore, comparison of these mutant and wild type structures strongly suggests that the Gly(631)-Asn(635) loop movement controls NADPH binding and NADP(+) release; this loop movement in turn facilitates the flavin domain movement, allowing electron transfer from FMN to the CYPOR redox partners. NADP 133-137 cytochrome p450 oxidoreductase Homo sapiens 278-283 21084761-1 2011 Cytochrome P450 oxidoreductase (POR) transfers electrons from NADPH to all microsomal cytochrome P450 (CYP) enzymes and is necessary for microsomal CYP activities. NADP 62-67 cytochrome p450 oxidoreductase Homo sapiens 0-30 21103538-5 2011 Here, we investigate the vibrational frequencies of the POR-bound and unbound substrate, and product, and thus provide a detailed assignment of the spectral changes in the 1800-1250 cm(-1) region associated with the catalytic conversion of PChlide:NADPH:TyrOH into Chlide:NADP(+):TyrO(-). NADP 248-253 cytochrome p450 oxidoreductase Homo sapiens 56-59 21103538-5 2011 Here, we investigate the vibrational frequencies of the POR-bound and unbound substrate, and product, and thus provide a detailed assignment of the spectral changes in the 1800-1250 cm(-1) region associated with the catalytic conversion of PChlide:NADPH:TyrOH into Chlide:NADP(+):TyrO(-). NADP 248-252 cytochrome p450 oxidoreductase Homo sapiens 56-59 21103538-9 2011 Rapid-scan FTIR measurements on the Pchlide:POR:NADPH complex at 4 cm(-1) spectral resolution reveal a new band in the 1670 cm(-1) region. NADP 48-53 cytochrome p450 oxidoreductase Homo sapiens 44-47 21171640-1 2011 In plants, the oxidoreductase enzyme POR reduces protochlorophyllide (Pchlide) into chlorophyllide (Chlide), using NADPH as a cofactor. NADP 115-120 cytochrome p450 oxidoreductase Homo sapiens 37-40 21070833-1 2011 P450 oxidoreductase (POR) transports electrons from NADPH to all microsomal cytochrome P450 enzymes, including steroidogenic P450c17, P450c21 and P450aro. NADP 52-57 cytochrome p450 oxidoreductase Homo sapiens 0-19 21070833-1 2011 P450 oxidoreductase (POR) transports electrons from NADPH to all microsomal cytochrome P450 enzymes, including steroidogenic P450c17, P450c21 and P450aro. NADP 52-57 cytochrome p450 oxidoreductase Homo sapiens 21-24 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. NADP 28-33 cytochrome p450 oxidoreductase Homo sapiens 0-3 21084761-1 2011 Cytochrome P450 oxidoreductase (POR) transfers electrons from NADPH to all microsomal cytochrome P450 (CYP) enzymes and is necessary for microsomal CYP activities. NADP 62-67 cytochrome p450 oxidoreductase Homo sapiens 32-35 18282462-6 2008 The epoxygenase and hydroxylase reactions were NADPH-dependent, required the functional expression of the CPR-encoding emb-8 gene, and were inhibited by 17-ODYA and PPOH, two compounds known to inactivate mammalian AA-metabolizing CYP isoforms. NADP 47-52 cytochrome p450 oxidoreductase Homo sapiens 106-109 20732302-1 2010 Human heme oxygenase-1 (HO-1) carries out heme catabolism supported by electrons supplied from the NADPH through NADPH P450 reductase (POR, CPR). NADP 99-104 cytochrome p450 oxidoreductase Homo sapiens 135-138 20732302-1 2010 Human heme oxygenase-1 (HO-1) carries out heme catabolism supported by electrons supplied from the NADPH through NADPH P450 reductase (POR, CPR). NADP 99-104 cytochrome p450 oxidoreductase Homo sapiens 140-143 20572660-2 2010 Here we unite electron-electron double resonance (ELDOR) studies of the diradical (disemiquinoid) form of human cytochrome P450 reductase (CPR), a nicotinamide adenine phosphate dinucleotide (NADPH)-linked diflavin oxidoreductase required for P450 enzyme reduction, with functional studies of internal ET to gain new insight into the extent and properties of the energy landscape for conformationally controlled ET. NADP 192-197 cytochrome p450 oxidoreductase Homo sapiens 112-137 20572660-2 2010 Here we unite electron-electron double resonance (ELDOR) studies of the diradical (disemiquinoid) form of human cytochrome P450 reductase (CPR), a nicotinamide adenine phosphate dinucleotide (NADPH)-linked diflavin oxidoreductase required for P450 enzyme reduction, with functional studies of internal ET to gain new insight into the extent and properties of the energy landscape for conformationally controlled ET. NADP 192-197 cytochrome p450 oxidoreductase Homo sapiens 139-142 19908820-1 2009 Cytochrome P450 reductase (CPR) is a tethered membrane protein which transfers electrons from NADPH to microsomal P450s. NADP 94-99 cytochrome p450 oxidoreductase Homo sapiens 0-25 19908820-1 2009 Cytochrome P450 reductase (CPR) is a tethered membrane protein which transfers electrons from NADPH to microsomal P450s. NADP 94-99 cytochrome p450 oxidoreductase Homo sapiens 27-30 19837910-6 2009 POR activity was measured by four assays: reduction of cytochrome c, oxidation of reduced nicotinamide adenine dinucleotide phosphate, and support of the 17alpha-hydroxylase and 17,20 lyase activities of P450c17. NADP 90-133 cytochrome p450 oxidoreductase Homo sapiens 0-3 19937842-0 2009 RNA-interference approach to study functions of NADPH : cytochrome P450 oxidoreductase in human hepatocytes. NADP 48-53 cytochrome p450 oxidoreductase Homo sapiens 67-86 18941714-1 2009 Mammalian NADPH-cytochrome P450 reductase (CPR) transfers electrons from NADPH to cytochrome P450 enzymes and other several microsomal enzymes. NADP 10-15 cytochrome p450 oxidoreductase Homo sapiens 43-46 18941714-4 2009 The electrons released from NADPH by CPR were transferred to CTC in the reaction medium, and CTC reduction activity could be assessed spectrophotometrically and spectrofluorometrically. NADP 28-33 cytochrome p450 oxidoreductase Homo sapiens 37-40 18397975-3 2008 Mutations in P450 oxidoreductase (POR), the protein that transfers electrons from reduced nicotinamide adenine dinucleotide phosphate to all microsomal P450s, can ameliorate the 21OHD phenotype and, therefore, could be a modifier gene. NADP 90-133 cytochrome p450 oxidoreductase Homo sapiens 13-32 18397975-3 2008 Mutations in P450 oxidoreductase (POR), the protein that transfers electrons from reduced nicotinamide adenine dinucleotide phosphate to all microsomal P450s, can ameliorate the 21OHD phenotype and, therefore, could be a modifier gene. NADP 90-133 cytochrome p450 oxidoreductase Homo sapiens 34-37 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. NADP 249-254 cytochrome p450 oxidoreductase Homo sapiens 68-93 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. NADP 249-254 cytochrome p450 oxidoreductase Homo sapiens 95-98 20849814-1 2010 Cytochrome P450 3A4 (CYP3A4), the major P450 present in human liver metabolizes approximately half the drugs in clinical use and requires electrons supplied from NADPH through NADPH-P450 reductase (POR, CPR). NADP 162-167 cytochrome p450 oxidoreductase Homo sapiens 198-201 20849814-1 2010 Cytochrome P450 3A4 (CYP3A4), the major P450 present in human liver metabolizes approximately half the drugs in clinical use and requires electrons supplied from NADPH through NADPH-P450 reductase (POR, CPR). NADP 162-167 cytochrome p450 oxidoreductase Homo sapiens 203-206 20599740-3 2010 Stable and fully functional complexes with different CPR:CYP3A4 stoichiometric ratios are formed within several minutes after addition of the full-length CPR to the solution of CYP3A4 preassembled into POPC Nanodiscs at 37 degrees C. We find that the steady state rates of NADPH oxidation and testosterone hydroxylation strongly depend on CPR:CYP3A4 ratio and reach maximum at tenfold molar access of CPR. NADP 273-278 cytochrome p450 oxidoreductase Homo sapiens 154-157 20599740-3 2010 Stable and fully functional complexes with different CPR:CYP3A4 stoichiometric ratios are formed within several minutes after addition of the full-length CPR to the solution of CYP3A4 preassembled into POPC Nanodiscs at 37 degrees C. We find that the steady state rates of NADPH oxidation and testosterone hydroxylation strongly depend on CPR:CYP3A4 ratio and reach maximum at tenfold molar access of CPR. NADP 273-278 cytochrome p450 oxidoreductase Homo sapiens 154-157 20599740-3 2010 Stable and fully functional complexes with different CPR:CYP3A4 stoichiometric ratios are formed within several minutes after addition of the full-length CPR to the solution of CYP3A4 preassembled into POPC Nanodiscs at 37 degrees C. We find that the steady state rates of NADPH oxidation and testosterone hydroxylation strongly depend on CPR:CYP3A4 ratio and reach maximum at tenfold molar access of CPR. NADP 273-278 cytochrome p450 oxidoreductase Homo sapiens 154-157 20188793-1 2010 Cytochrome P450 oxidoreductase (POR) supplies electrons from NADPH to steroid and drug metabolizing reactions catalyzed by the cytochrome P450s located in endoplasmic reticulum. NADP 61-66 cytochrome p450 oxidoreductase Homo sapiens 32-35 20188793-5 2010 Computational molecular docking experiments with a FMN free structural model of POR revealed that an external FMN could be docked in close proximity to the FAD moiety and receive electrons donated by NADPH. NADP 200-205 cytochrome p450 oxidoreductase Homo sapiens 80-83 20205376-2 2010 Complexed with NADPH to the enzyme protochlorophyllide oxidoreductase (POR), it is reduced to chlorophyllide, a process that occurs via a set of spectroscopically distinct intermediate states and is initiated from the excited state of PChlide. NADP 15-20 cytochrome p450 oxidoreductase Homo sapiens 71-74 19931102-3 2010 CPR shuttles electrons from NADPH through the FAD and FMN-cofactors into the central heme-group of the P450s. NADP 28-33 cytochrome p450 oxidoreductase Homo sapiens 0-3 18191533-7 2008 P450R overexpression appears therefore to be detrimental to MDA 231 cells, depleting NADPH and increasing ROS levels; the increased oxidative stress observed in MDA R4 cells might explain the enhanced sensitivity to 5-fluorouracil. NADP 85-90 cytochrome p450 oxidoreductase Homo sapiens 0-5 17635179-3 2007 POR is a flavoprotein that contains both flavin mononucleotide and flavin adenine dinucleotide as cofactors and uses NADPH as the source of electrons. NADP 117-122 cytochrome p450 oxidoreductase Homo sapiens 0-3 17595315-7 2007 Mutations C569Y and V608F in the NADPH binding domain of POR had 49 and 28% of activity of CYP19A1 compared with normal reductase and were more sensitive to the amount of NADPH available for supporting CYP19A1 activity. NADP 33-38 cytochrome p450 oxidoreductase Homo sapiens 57-60 17595315-7 2007 Mutations C569Y and V608F in the NADPH binding domain of POR had 49 and 28% of activity of CYP19A1 compared with normal reductase and were more sensitive to the amount of NADPH available for supporting CYP19A1 activity. NADP 171-176 cytochrome p450 oxidoreductase Homo sapiens 57-60 17595315-8 2007 Substitution of NADH for NADPH had a higher impact on C569Y and V608F mutants of POR. NADP 25-30 cytochrome p450 oxidoreductase Homo sapiens 81-84 18630181-4 2008 CYPOR is a four domain-containing monomeric flavoprotein that contains two flavins, flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), a binding site for NADPH, and the N-terminal sequence of 25 amino acids which determines the microsomal localization of the protein. NADP 170-175 cytochrome p450 oxidoreductase Homo sapiens 0-5 16574318-3 2007 Our assays showed that the reduction of MX by exogenously added CPR in the presence of low NADPH concentration had no effect in increasing its ability to inhibit the growth of sensitive and MDR tumour cells. NADP 91-96 cytochrome p450 oxidoreductase Homo sapiens 64-67 17505056-1 2007 P450 oxidoreductase (POR) has a pivotal role in facilitating electron transfer from nicotinamide adenine dinucleotide phosphate to microsomal cytochrome P450 (CYP) enzymes, including the steroidogenic enzymes CYP17A1 and CYP21A2. NADP 84-127 cytochrome p450 oxidoreductase Homo sapiens 0-19 17505056-1 2007 P450 oxidoreductase (POR) has a pivotal role in facilitating electron transfer from nicotinamide adenine dinucleotide phosphate to microsomal cytochrome P450 (CYP) enzymes, including the steroidogenic enzymes CYP17A1 and CYP21A2. NADP 84-127 cytochrome p450 oxidoreductase Homo sapiens 21-24 16574318-4 2007 In contrast, an important increase in antiproliferative activity of MX after its reductive activation by CPR at high NADPH concentration was observed against HL60/VINC as well as HL60/DOX cells. NADP 117-122 cytochrome p450 oxidoreductase Homo sapiens 105-108 16867988-8 2006 A catalytic mechanism of POR is suggested in which Pchlide absorbs a photon, creating a transient charge separation across the C-17-C-18 double bond, which promotes ultrafast hydride transfer from the pro-S face of NADPH to the C-17 of Pchlide. NADP 215-220 cytochrome p450 oxidoreductase Homo sapiens 25-28 16391466-13 2006 CONCLUSION: alpha-Lipoic acid decreased NADPH-CPR activity in the lung and heart. NADP 40-45 cytochrome p450 oxidoreductase Homo sapiens 46-49 16769893-5 2006 We report that a Fe(III)(Schiff-base), in the place of the active-site heme prosthetic group of HO, can be reduced by NADPH/CPR. NADP 118-123 cytochrome p450 oxidoreductase Homo sapiens 124-127 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. NADP 30-35 cytochrome p450 oxidoreductase Homo sapiens 36-39 16467261-1 2005 Microsomal P450 enzymes, which metabolize drugs and catalyze steroid biosynthesis require electron donation from NADPH via P450 oxidoreductase (POR). NADP 113-118 cytochrome p450 oxidoreductase Homo sapiens 123-142 16467261-1 2005 Microsomal P450 enzymes, which metabolize drugs and catalyze steroid biosynthesis require electron donation from NADPH via P450 oxidoreductase (POR). NADP 113-118 cytochrome p450 oxidoreductase Homo sapiens 144-147 15479629-1 2004 NADPH-cytochrome P450 reductase (CPR) transfers electrons from NADPH to cytochrome P450, and catalyzes the one-electron reduction of many drugs and foreign compounds. NADP 0-5 cytochrome p450 oxidoreductase Homo sapiens 33-36 15774560-6 2005 Type II P450 enzymes, found in the endoplasmic reticulum, receive electrons from NADPH via P450 oxidoreductase (POR), which contains two flavin moieties. NADP 81-86 cytochrome p450 oxidoreductase Homo sapiens 91-110 15774560-6 2005 Type II P450 enzymes, found in the endoplasmic reticulum, receive electrons from NADPH via P450 oxidoreductase (POR), which contains two flavin moieties. NADP 81-86 cytochrome p450 oxidoreductase Homo sapiens 112-115 15516695-2 2005 In this study, we investigated the effect of NADP(H) on the interaction of HO-1 with CPR by surface plasmon resonance. NADP 45-52 cytochrome p450 oxidoreductase Homo sapiens 85-88 15516695-3 2005 We found that HO-1 associated with CPR more tightly in the presence of NADP(+) (K(D) = 0.5 microm) than in its absence (K(D) = 2.4 microm). NADP 71-78 cytochrome p450 oxidoreductase Homo sapiens 35-38 15516695-5 2005 R185A showed a 100-fold decreased affinity for CPR compared with wild type, even in the presence of NADP(+) (K(D) = 36.3 microm). NADP 100-107 cytochrome p450 oxidoreductase Homo sapiens 47-50 15516695-8 2005 Computer modeling of the HO-1/CPR complex showed that the guanidino group of Arg(185) is located within the hydrogen bonding distance of 2"-phosphate of NADPH, suggesting that Arg(185) contributes to the binding to CPR through an electrostatic interaction with the phosphate group. NADP 153-158 cytochrome p450 oxidoreductase Homo sapiens 30-33 15943915-1 2005 NADPH-cytochrome P450 reductase (CPR) transfers electrons from NADPH to cytochrome P450 and also catalyzes the one-electron reduction of many drugs and foreign compounds. NADP 0-5 cytochrome p450 oxidoreductase Homo sapiens 33-36 15943915-5 2005 The electrons released from NADPH by CPR were transferred to MTT. NADP 28-33 cytochrome p450 oxidoreductase Homo sapiens 37-40 15793702-1 2005 P450 oxidoreductase (POR) is the obligatory flavoprotein intermediate that transfers electrons from reduced nicotinamide adenine dinucleotide phosphate (NADPH) to all microsomal cytochrome P450 enzymes. NADP 108-151 cytochrome p450 oxidoreductase Homo sapiens 0-19 15793702-1 2005 P450 oxidoreductase (POR) is the obligatory flavoprotein intermediate that transfers electrons from reduced nicotinamide adenine dinucleotide phosphate (NADPH) to all microsomal cytochrome P450 enzymes. NADP 108-151 cytochrome p450 oxidoreductase Homo sapiens 21-24 15793702-1 2005 P450 oxidoreductase (POR) is the obligatory flavoprotein intermediate that transfers electrons from reduced nicotinamide adenine dinucleotide phosphate (NADPH) to all microsomal cytochrome P450 enzymes. NADP 153-158 cytochrome p450 oxidoreductase Homo sapiens 0-19 15793702-1 2005 P450 oxidoreductase (POR) is the obligatory flavoprotein intermediate that transfers electrons from reduced nicotinamide adenine dinucleotide phosphate (NADPH) to all microsomal cytochrome P450 enzymes. NADP 153-158 cytochrome p450 oxidoreductase Homo sapiens 21-24 15763633-3 2005 Zn2+ inhibited the CO-binding spectra of CYP3A4 reduced by NADPH-cytochrome P450 reductase (CPR) and NADPH only in the presence of b5. NADP 59-64 cytochrome p450 oxidoreductase Homo sapiens 92-95 15479629-5 2004 Thus, electrons released from NADPH by CPR were transferred to DPPH, and DPPH reduction was then followed spectrophotometrically by measuring A(520) reduction. NADP 30-35 cytochrome p450 oxidoreductase Homo sapiens 39-42 12787027-4 2003 Biochemistry (2002) 41, 4626-4637] have shown that the observed rate, 1/tau, of interflavin electron transfer (FADsq - FMNsq-->FADox - FMNhq) in CPR reduced at the two-electron level with NADPH is 55 +/- 2 s-1, whereas with dithionite-reduced enzyme the observed rate is 11 +/- 0.5 s-1, suggesting that NADPH (or NADP+) binding has an important role in controlling the rate of internal electron transfer. NADP 191-196 cytochrome p450 oxidoreductase Homo sapiens 148-151 15209523-1 2004 The chlorophyll biosynthetic enzyme protochlorophyllide reductase (POR) catalyzes the reduction of protochlorophyllide (Pchlide) into chlorophyllide (Chlide) with reduced nicotinamide adenine dinucleotide phosphate (NADPH) as a cofactor. NADP 171-214 cytochrome p450 oxidoreductase Homo sapiens 67-70 15209523-1 2004 The chlorophyll biosynthetic enzyme protochlorophyllide reductase (POR) catalyzes the reduction of protochlorophyllide (Pchlide) into chlorophyllide (Chlide) with reduced nicotinamide adenine dinucleotide phosphate (NADPH) as a cofactor. NADP 216-221 cytochrome p450 oxidoreductase Homo sapiens 67-70 14583491-4 2003 cDNA-expressed human CYPRED catalyzed doxorubicin reduction, measured as the rate of doxorubicin-stimulated NADPH consumption. NADP 108-113 cytochrome p450 oxidoreductase Homo sapiens 21-27 12787027-4 2003 Biochemistry (2002) 41, 4626-4637] have shown that the observed rate, 1/tau, of interflavin electron transfer (FADsq - FMNsq-->FADox - FMNhq) in CPR reduced at the two-electron level with NADPH is 55 +/- 2 s-1, whereas with dithionite-reduced enzyme the observed rate is 11 +/- 0.5 s-1, suggesting that NADPH (or NADP+) binding has an important role in controlling the rate of internal electron transfer. NADP 306-311 cytochrome p450 oxidoreductase Homo sapiens 148-151 12787027-4 2003 Biochemistry (2002) 41, 4626-4637] have shown that the observed rate, 1/tau, of interflavin electron transfer (FADsq - FMNsq-->FADox - FMNhq) in CPR reduced at the two-electron level with NADPH is 55 +/- 2 s-1, whereas with dithionite-reduced enzyme the observed rate is 11 +/- 0.5 s-1, suggesting that NADPH (or NADP+) binding has an important role in controlling the rate of internal electron transfer. NADP 316-321 cytochrome p450 oxidoreductase Homo sapiens 148-151 12787027-5 2003 In relaxation experiments performed with CPR reduced at the two-electron level with NADH, the observed rate of internal electron transfer (1/tau = 18 +/- 0.7 s-1) is intermediate in value between those seen with dithionite-reduced and NADPH-reduced enzyme, indicating that the presence of the 2"-phosphate is important for enhancing internal electron transfer. NADP 235-240 cytochrome p450 oxidoreductase Homo sapiens 41-44 12787027-8 2003 Reduction of CPR at the two-electron level by NADPH, NADH or dithionite generates the same spectral species, consistent with an electron distribution that is equivalent regardless of reductant at the initiation of the temperature jump. NADP 46-51 cytochrome p450 oxidoreductase Homo sapiens 13-16 12787027-9 2003 Spectroelectrochemical experiments establish that the redox potentials of the flavins of CPR are unchanged on binding 2",5"-ADP, supporting the view that enhanced rates of interdomain electron transfer have their origin in a conformational change produced by binding NADPH or its fragments. NADP 267-272 cytochrome p450 oxidoreductase Homo sapiens 89-92 12177453-1 2002 The chlorophyll biosynthesis enzyme protochlorophyllide reductase (POR) catalyzes the light-dependent reduction of protochlorophyllide (Pchlide) into chlorophyllide in the presence of NADPH. NADP 184-189 cytochrome p450 oxidoreductase Homo sapiens 36-65 12725870-1 2003 Microsomal P450-mediated monooxygenase activity supported by NADPH requires an interaction between flavoprotein NADPH-cytochrome P450 reductase and cytochrome P450. NADP 61-66 cytochrome p450 oxidoreductase Homo sapiens 112-143 12631275-3 2003 The midpoint reduction potentials of the oxidized/semiquinone (-315 +/- 5 mV) and semiquinone/dihydroquinone (-365 +/- 15 mV) couples of the FAD/NADPH domain are similar to those for the FAD/NADPH domain of human CPR, but the rate of hydride transfer from NADPH to the FAD/NADPH domain of NR1 is approximately 200-fold slower. NADP 145-150 cytochrome p450 oxidoreductase Homo sapiens 213-216 12401791-4 2003 The assembly of this novel light-harvesting POR-Pchlide complex (LHPP) requires both the proper interaction of the PORA and PORB with their cognate substrates as well as the oligomerization of the resulting POR-pigment-NADPH ternary complexes into the native, lipid-containing structure of the etioplast. NADP 219-224 cytochrome p450 oxidoreductase Homo sapiens 44-47 12401791-4 2003 The assembly of this novel light-harvesting POR-Pchlide complex (LHPP) requires both the proper interaction of the PORA and PORB with their cognate substrates as well as the oligomerization of the resulting POR-pigment-NADPH ternary complexes into the native, lipid-containing structure of the etioplast. NADP 219-224 cytochrome p450 oxidoreductase Homo sapiens 115-118 12177453-1 2002 The chlorophyll biosynthesis enzyme protochlorophyllide reductase (POR) catalyzes the light-dependent reduction of protochlorophyllide (Pchlide) into chlorophyllide in the presence of NADPH. NADP 184-189 cytochrome p450 oxidoreductase Homo sapiens 67-70 11673874-1 2001 Based on the similarity in both structure and function of the reductase domain of neuronal nitric oxide synthase (nNOSred) to that of NADPH-cytochrome P450 reductase (CPR), we determined whether the characteristics of hydride transfer from NADPH to flavin adenine dinucleotide (FAD) were similar for both proteins. NADP 134-139 cytochrome p450 oxidoreductase Homo sapiens 167-170 9237990-2 1997 CPR is a membrane-bound protein and catalyzes electron transfer from NADPH to all known microsomal cytochromes P450. NADP 69-74 cytochrome p450 oxidoreductase Homo sapiens 0-3 9685732-6 1998 The rates of substrate-triggered aerobic NADPH consumption in systems containing CYP2B4(Delta2-27) and P450R were 16 to 56% those obtained with the unchanged hemoprotein. NADP 41-46 cytochrome p450 oxidoreductase Homo sapiens 103-108 10594372-1 1999 The neuronal NO synthase (nNOS) flavin domain, which has similar redox properties to those of NADPH-cytochrome P450 reductase (P450R), contains binding sites for calmodulin, FAD, FMN, and NADPH. NADP 94-99 cytochrome p450 oxidoreductase Homo sapiens 127-133 9109653-4 1997 When the reaction is carried out with nicotinamide adenine dinucleotide phosphate (reduced) (NADPH) and recombinant human NADPH-cytochrome P450 reductase, a second product, identified as 1-methyl-4-(4"-hydroxyphenyl)-1,2,3,6-tetrahydropyridine, is formed in addition to 4-phenyl-1,2,3,6-tetrahydropyridine. NADP 38-81 cytochrome p450 oxidoreductase Homo sapiens 122-153 9109653-4 1997 When the reaction is carried out with nicotinamide adenine dinucleotide phosphate (reduced) (NADPH) and recombinant human NADPH-cytochrome P450 reductase, a second product, identified as 1-methyl-4-(4"-hydroxyphenyl)-1,2,3,6-tetrahydropyridine, is formed in addition to 4-phenyl-1,2,3,6-tetrahydropyridine. NADP 93-98 cytochrome p450 oxidoreductase Homo sapiens 122-153 8185310-6 1994 Study of the NADPH-dependent reduction of cytochrome P4501A2 in the reconstituted system showed that the rate constant and reduction level of cytochrome P4501A2 were always higher when the reaction was initiated by NADPH than when it was initiated by NADPH-cytochrome P450 reductase. NADP 13-18 cytochrome p450 oxidoreductase Homo sapiens 251-282 8185310-6 1994 Study of the NADPH-dependent reduction of cytochrome P4501A2 in the reconstituted system showed that the rate constant and reduction level of cytochrome P4501A2 were always higher when the reaction was initiated by NADPH than when it was initiated by NADPH-cytochrome P450 reductase. NADP 215-220 cytochrome p450 oxidoreductase Homo sapiens 251-282 8199313-1 1994 The oxidation rate of NADPH is markedly stimulated during the mechanism-based inactivation of cytochrome P450 2B1 by N-methylcarbazole (NMC) in a reconstituted system consisting of NADPH-cytochrome P450 reductase, cytochrome P450 and phospholipid. NADP 22-27 cytochrome p450 oxidoreductase Homo sapiens 181-212 8199313-3 1994 The 1-OH-NMC is further metabolized in an NADPH-dependent manner by the reconstituted system or by purified NADPH-cytochrome P450 reductase to give a more polar metabolite which has been isolated by HPLC. NADP 42-47 cytochrome p450 oxidoreductase Homo sapiens 108-139 8218222-5 1993 P-450R (R597M) has a Km for NADPH that is 150 times that of P-450R (WT) and a Ki for NADP+ that is 240 times that of P-450R (WT). NADP 85-90 cytochrome p450 oxidoreductase Homo sapiens 0-6 8218221-7 1993 The NADP+ pKi profile shows a pKa of 5.95 for the 2"-phosphate of NADP+, which is bound to P-450R as the dianion, and a pKa of 9.53 for an enzyme group that must be protonated in order to bind NADP+. NADP 4-8 cytochrome p450 oxidoreductase Homo sapiens 91-97 8218221-7 1993 The NADP+ pKi profile shows a pKa of 5.95 for the 2"-phosphate of NADP+, which is bound to P-450R as the dianion, and a pKa of 9.53 for an enzyme group that must be protonated in order to bind NADP+. NADP 4-9 cytochrome p450 oxidoreductase Homo sapiens 91-97 8218221-7 1993 The NADP+ pKi profile shows a pKa of 5.95 for the 2"-phosphate of NADP+, which is bound to P-450R as the dianion, and a pKa of 9.53 for an enzyme group that must be protonated in order to bind NADP+. NADP 66-71 cytochrome p450 oxidoreductase Homo sapiens 91-97 8218222-1 1993 Site-directed mutagenesis has been used in conjunction with pH and alternate substrate/inhibitor studies to characterize the interactions between NADPH-cytochrome P-450 oxidoreductase (P-450R) and the 2"-phosphate of NADP(H) that provide P-450R with its strong nicotinamide nucleotide specificity. NADP 146-150 cytochrome p450 oxidoreductase Homo sapiens 185-192 8218222-1 1993 Site-directed mutagenesis has been used in conjunction with pH and alternate substrate/inhibitor studies to characterize the interactions between NADPH-cytochrome P-450 oxidoreductase (P-450R) and the 2"-phosphate of NADP(H) that provide P-450R with its strong nicotinamide nucleotide specificity. NADP 146-150 cytochrome p450 oxidoreductase Homo sapiens 185-191 8218222-2 1993 It is known that the 2"-phosphate of NADP(H) is bound to P-450R as the dianion and that interactions between it and residues on P-450R provide 5 kcal/mol of essentially uniform binding energy (preceding paper in this issue). NADP 37-41 cytochrome p450 oxidoreductase Homo sapiens 57-63 8218222-2 1993 It is known that the 2"-phosphate of NADP(H) is bound to P-450R as the dianion and that interactions between it and residues on P-450R provide 5 kcal/mol of essentially uniform binding energy (preceding paper in this issue). NADP 37-41 cytochrome p450 oxidoreductase Homo sapiens 128-134 8218222-5 1993 P-450R (R597M) has a Km for NADPH that is 150 times that of P-450R (WT) and a Ki for NADP+ that is 240 times that of P-450R (WT). NADP 28-33 cytochrome p450 oxidoreductase Homo sapiens 0-6 8218222-8 1993 The NADP+ pKi profile for P-450R (R597M) shows a pKa of 5.78 for the 2"-phosphate of NADP+, which is bound to P-450R (R597M) as the dianion, but the pKa of 9.5 for the preferentially protonated enzymic group observed in the P-450R (WT) profile is no longer present. NADP 4-8 cytochrome p450 oxidoreductase Homo sapiens 26-32 8218222-8 1993 The NADP+ pKi profile for P-450R (R597M) shows a pKa of 5.78 for the 2"-phosphate of NADP+, which is bound to P-450R (R597M) as the dianion, but the pKa of 9.5 for the preferentially protonated enzymic group observed in the P-450R (WT) profile is no longer present. NADP 4-8 cytochrome p450 oxidoreductase Homo sapiens 110-116 8218222-8 1993 The NADP+ pKi profile for P-450R (R597M) shows a pKa of 5.78 for the 2"-phosphate of NADP+, which is bound to P-450R (R597M) as the dianion, but the pKa of 9.5 for the preferentially protonated enzymic group observed in the P-450R (WT) profile is no longer present. NADP 4-8 cytochrome p450 oxidoreductase Homo sapiens 110-116 8218222-8 1993 The NADP+ pKi profile for P-450R (R597M) shows a pKa of 5.78 for the 2"-phosphate of NADP+, which is bound to P-450R (R597M) as the dianion, but the pKa of 9.5 for the preferentially protonated enzymic group observed in the P-450R (WT) profile is no longer present. NADP 4-9 cytochrome p450 oxidoreductase Homo sapiens 26-32 8218222-8 1993 The NADP+ pKi profile for P-450R (R597M) shows a pKa of 5.78 for the 2"-phosphate of NADP+, which is bound to P-450R (R597M) as the dianion, but the pKa of 9.5 for the preferentially protonated enzymic group observed in the P-450R (WT) profile is no longer present. NADP 4-9 cytochrome p450 oxidoreductase Homo sapiens 110-116 8218222-8 1993 The NADP+ pKi profile for P-450R (R597M) shows a pKa of 5.78 for the 2"-phosphate of NADP+, which is bound to P-450R (R597M) as the dianion, but the pKa of 9.5 for the preferentially protonated enzymic group observed in the P-450R (WT) profile is no longer present. NADP 4-9 cytochrome p450 oxidoreductase Homo sapiens 110-116 8394056-10 1993 The similar effects of tar on NADPH oxidation catalyzed either by microsomes or by purified NADPH-cytochrome P450 reductase suggest that cytochrome P450 reductase is an important locus of electron transfer from microsomes to components of cigarette tar extracts. NADP 30-35 cytochrome p450 oxidoreductase Homo sapiens 92-123 3499150-2 1987 The ability of paraquat, MPP+, and analogs to be reduced by chemical reductants and by NADPH, as catalyzed by liver microsomes or purified NADPH cytochrome P-450 reductase, is reported. NADP 87-92 cytochrome p450 oxidoreductase Homo sapiens 139-171 1727652-1 1992 NADPH-supported lipid peroxidation monitored by malondialdehyde (MDA) production in the presence of ferric pyrophosphate in liver microsomes was inactivated by heat treatment or by trypsin and the activity was not restored by the addition of purified NADPH-cytochrome P450 reductase (FPT). NADP 0-5 cytochrome p450 oxidoreductase Homo sapiens 251-282 3121608-6 1988 To explain the effect of NADPH concentration on the initial rate of LM2 reduction, the effect of NADPH on the reduction of NADPH-cytochrome P-450 reductase was examined. NADP 97-102 cytochrome p450 oxidoreductase Homo sapiens 123-155 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. NADP 64-69 cytochrome p450 oxidoreductase Homo sapiens 137-169 2105240-0 1990 The cosubstrate NADP(H) protects lysine 601 in the porcine NADPH-cytochrome P-450 reductase against pyridoxylation. NADP 16-23 cytochrome p450 oxidoreductase Homo sapiens 59-91 35171619-1 2022 Cytochrome P450 reductase (CPR) is a NADPH-dependent membrane-bound oxidoreductase found in the endoplasmic reticulum (ER) and is the main redox partner for most cytochrome P450 enzymes. NADP 37-42 cytochrome p450 oxidoreductase Homo sapiens 0-25 35171619-1 2022 Cytochrome P450 reductase (CPR) is a NADPH-dependent membrane-bound oxidoreductase found in the endoplasmic reticulum (ER) and is the main redox partner for most cytochrome P450 enzymes. NADP 37-42 cytochrome p450 oxidoreductase Homo sapiens 27-30 6814537-5 1982 The coincidence of the values of the rate constants and activation energy (56 +/- 5 kJ/mol) for the fast phase of NADPH-dependent reduction of cytochrome P-450 with values of catalytic constants and activation energy for demethylation of tertiary amines suggests that the first electron transfer process from NADPH-cytochrome P-450 reductase to cytochrome P-450 may be the rate-limiting step. NADP 114-119 cytochrome p450 oxidoreductase Homo sapiens 309-341 2435285-4 1987 Since both NADP and dicoumarol inhibited the naphthazarin-stimulated non-stoichiometric consumption of NADPH and oxygen then naphthazarin redox cycling probably involves both DT-diaphorase and NADPH cytochrome P-450 reductase. NADP 11-15 cytochrome p450 oxidoreductase Homo sapiens 193-225 6084519-1 1984 In the presence of NADPH and O2, NADPH-cytochrome P-450 reductase was found to activate Fe(III)-bleomycin A2 for DNA strand scission. NADP 19-24 cytochrome p450 oxidoreductase Homo sapiens 33-65 33043019-5 2020 In particular, the production of reactive oxygen species (ROS) that depends on the activity of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases (NOXs) and the mitochondrial respiratory chain promotes lipid peroxidation by lipoxygenase (ALOX) or cytochrome P450 reductase (POR). NADP 95-138 cytochrome p450 oxidoreductase Homo sapiens 284-287 6777326-9 1980 The number of NADPH binding sites in the NADPH-cytochrome P450 reductase is determined to one site/mol reductase by titration of the enzyme with NADP+ monitored by CD-spectroscopy. NADP 14-19 cytochrome p450 oxidoreductase Homo sapiens 41-72 6777326-9 1980 The number of NADPH binding sites in the NADPH-cytochrome P450 reductase is determined to one site/mol reductase by titration of the enzyme with NADP+ monitored by CD-spectroscopy. NADP 145-150 cytochrome p450 oxidoreductase Homo sapiens 41-72 42250-3 1979 Phosphatidylcholine is required in the reconstituted enzyme system for rapid electron transfer from NADPH to P-450 LM, catalyzed by NADPH-cytochrome P-450 reductase, as well as for maximal hydroxylation activity with either molecular oxygen or a peroxy compound serving as oxygen donor to the substrate. NADP 100-105 cytochrome p450 oxidoreductase Homo sapiens 132-164 42251-1 1979 Stopped flow studies were undertaken to examine the kinetics of reduction of 5,6-benzoflavone-inducible P-450 LM4 by NADPH in the presence of NADPH-cytochrome P-450 reductase and phospholipid under anaerobic CO at 25 degrees C. The reaction exhibited biphasic kinetics irrespective of NADPH concentration or of the molar ratio of reductase to P-450 LM4. NADP 117-122 cytochrome p450 oxidoreductase Homo sapiens 142-174 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. NADP 87-92 cytochrome p450 oxidoreductase Homo sapiens 101-133 33420418-7 2021 In the complexes, the interactions of the CPR FMN domain with the proximal side of CYP 1A1 are supplemented by more transient interactions of the CPR NADP domain with the distal side of CYP 1A1. NADP 150-154 cytochrome p450 oxidoreductase Homo sapiens 42-45 33420418-7 2021 In the complexes, the interactions of the CPR FMN domain with the proximal side of CYP 1A1 are supplemented by more transient interactions of the CPR NADP domain with the distal side of CYP 1A1. NADP 150-154 cytochrome p450 oxidoreductase Homo sapiens 146-149 32994263-6 2020 POR facilitates electron transfer from Nicotinamide adenine dinucleotide phosphate (NADPH) to key enzymes involved in steroid and sterol synthesis and metabolism. NADP 39-82 cytochrome p450 oxidoreductase Homo sapiens 0-3 32994263-6 2020 POR facilitates electron transfer from Nicotinamide adenine dinucleotide phosphate (NADPH) to key enzymes involved in steroid and sterol synthesis and metabolism. NADP 84-89 cytochrome p450 oxidoreductase Homo sapiens 0-3 32994263-12 2020 In 2004, it was mentioned by Fluck and his colleagues that this new CAH disease was attributable to the POR gene mutation.POR facilitates electron transfer from NADPH to key enzymes involved in steroid and sterol synthesis and metabolism.POR deficiency causes partial and combined impairment of the key enzymes involved in steroidogenesis: P450c17 (17alpha- hydroxylase/17,20 lyase), P450c21 (21-hydroxylase) and P450aro (aromatase).Clinically, Mutant POR manifests with disordered sex development, adrenal insufficiency and skeletal malformations.However, each enzyme may be differently compromised in the same patient. NADP 161-166 cytochrome p450 oxidoreductase Homo sapiens 104-107 32994263-12 2020 In 2004, it was mentioned by Fluck and his colleagues that this new CAH disease was attributable to the POR gene mutation.POR facilitates electron transfer from NADPH to key enzymes involved in steroid and sterol synthesis and metabolism.POR deficiency causes partial and combined impairment of the key enzymes involved in steroidogenesis: P450c17 (17alpha- hydroxylase/17,20 lyase), P450c21 (21-hydroxylase) and P450aro (aromatase).Clinically, Mutant POR manifests with disordered sex development, adrenal insufficiency and skeletal malformations.However, each enzyme may be differently compromised in the same patient. NADP 161-166 cytochrome p450 oxidoreductase Homo sapiens 122-125 32994263-12 2020 In 2004, it was mentioned by Fluck and his colleagues that this new CAH disease was attributable to the POR gene mutation.POR facilitates electron transfer from NADPH to key enzymes involved in steroid and sterol synthesis and metabolism.POR deficiency causes partial and combined impairment of the key enzymes involved in steroidogenesis: P450c17 (17alpha- hydroxylase/17,20 lyase), P450c21 (21-hydroxylase) and P450aro (aromatase).Clinically, Mutant POR manifests with disordered sex development, adrenal insufficiency and skeletal malformations.However, each enzyme may be differently compromised in the same patient. NADP 161-166 cytochrome p450 oxidoreductase Homo sapiens 122-125 33011882-6 2021 The activity of CYB5R and CYPOR was assessed with lucigenin-enhanced chemiluminescence stimulated by NADH and NADPH, respectively. NADP 110-115 cytochrome p450 oxidoreductase Homo sapiens 26-31 32866986-3 2021 Prolamellar bodies are highly organised, paracrystalline structures comprising aggregated oligomeric structures of POR-Pchlide-NADPH complexes. NADP 127-132 cytochrome p450 oxidoreductase Homo sapiens 115-118 33043019-5 2020 In particular, the production of reactive oxygen species (ROS) that depends on the activity of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases (NOXs) and the mitochondrial respiratory chain promotes lipid peroxidation by lipoxygenase (ALOX) or cytochrome P450 reductase (POR). NADP 140-145 cytochrome p450 oxidoreductase Homo sapiens 284-287 32708163-1 2020 Cytochrome P450 reductase (CPR) abstracts electrons from Nicotinamide adenine dinucleotide phosphate H (NADPH), transferring them to an active Cytochrome P450 (CYP) site to provide a functional CYP. NADP 104-109 cytochrome p450 oxidoreductase Homo sapiens 27-30 31669572-2 2020 CYP19A1 is a member of cytochrome P450 family of heme-thiolate monooxygenases located in the endoplasmic reticulum and depends on reducing equivalents from the reduced nicotinamide adenine dinucleotide phosphate via the cytochrome P450 oxidoreductase coded by POR. NADP 168-211 cytochrome p450 oxidoreductase Homo sapiens 260-263 31276316-2 2019 CPR shows a stringent preference for NADPH over the less expensive cofactor, NADH, economically limiting its use as a biocatalyst. NADP 37-42 cytochrome p450 oxidoreductase Homo sapiens 0-3 31276316-4 2019 Here, we report a rational evolution approach to enhance the activity of CPR with NADH, in which mutations were introduced into the NADPH-binding flavin adenine dinucleotide (FAD) domain. NADP 132-137 cytochrome p450 oxidoreductase Homo sapiens 73-76 31276316-7 2019 Unexpectedly, several mutants showed significantly improved activity towards CYP2C9 (mutant 1-014) and/or CYP2A6 (mutants 1-014, 1-015, 1-053 and 1-077) using NADPH, even though the mutations were introduced at locations remote from the putative CPR-P450 interaction face. NADP 159-164 cytochrome p450 oxidoreductase Homo sapiens 246-249 31749697-1 2019 Cytochromes P450 located in the endoplasmic reticulum require NADPH cytochrome P450 oxidoreductase (POR) for their catalytic activities. NADP 62-67 cytochrome p450 oxidoreductase Homo sapiens 100-103 30883732-0 2019 Crystal structure of a NADPH-cytochrome P450 oxidoreductase (CYPOR) and heme oxygenase 1 fusion protein implies a conformational change in CYPOR upon NADPH/NADP+ binding. NADP 156-161 cytochrome p450 oxidoreductase Homo sapiens 23-59 31249341-1 2019 Cytochrome P450 reductase (CPR) is the key protein that regulates the electron transfer from NADPH to various heme-containing monooxygenases. NADP 93-98 cytochrome p450 oxidoreductase Homo sapiens 0-25 31249341-1 2019 Cytochrome P450 reductase (CPR) is the key protein that regulates the electron transfer from NADPH to various heme-containing monooxygenases. NADP 93-98 cytochrome p450 oxidoreductase Homo sapiens 27-30 30883732-0 2019 Crystal structure of a NADPH-cytochrome P450 oxidoreductase (CYPOR) and heme oxygenase 1 fusion protein implies a conformational change in CYPOR upon NADPH/NADP+ binding. NADP 156-161 cytochrome p450 oxidoreductase Homo sapiens 61-66 30883732-0 2019 Crystal structure of a NADPH-cytochrome P450 oxidoreductase (CYPOR) and heme oxygenase 1 fusion protein implies a conformational change in CYPOR upon NADPH/NADP+ binding. NADP 156-161 cytochrome p450 oxidoreductase Homo sapiens 139-144 30883732-2 2019 Recently, we determined the complex structure of NADP+ -bound open-conformation stabilized CYPOR and heme-HMOX1, but the resolution was limited to 4.3 A. NADP 49-54 cytochrome p450 oxidoreductase Homo sapiens 91-96 30883732-5 2019 Structural comparison of the NADP+ -bound complex and the NADP+ -free fusion protein suggests that NADP+ binding regulates the conformational change in the FAD-binding domain of CYPOR. NADP 29-34 cytochrome p450 oxidoreductase Homo sapiens 178-183 30883732-5 2019 Structural comparison of the NADP+ -bound complex and the NADP+ -free fusion protein suggests that NADP+ binding regulates the conformational change in the FAD-binding domain of CYPOR. NADP 58-63 cytochrome p450 oxidoreductase Homo sapiens 178-183 30883732-5 2019 Structural comparison of the NADP+ -bound complex and the NADP+ -free fusion protein suggests that NADP+ binding regulates the conformational change in the FAD-binding domain of CYPOR. NADP 58-63 cytochrome p450 oxidoreductase Homo sapiens 178-183 30883732-6 2019 As a result of this change, the FMN-binding domain of CYPOR approaches heme-bound HMOX1 upon NADP+ binding to enhance the electron-transfer efficiency from FMN to heme. NADP 93-98 cytochrome p450 oxidoreductase Homo sapiens 54-59