PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27461959-0 2016 Role of active site loop in coenzyme binding and flavin reduction in cytochrome P450 reductase. 4,6-dinitro-o-cresol 49-55 cytochrome p450 oxidoreductase Homo sapiens 69-94 31445894-1 2019 The electron configuration of flavin cofactors, FMN and FAD, is a critical factor governing the reactivity of NADPH-cytochrome P450 reductase (CPR). 4,6-dinitro-o-cresol 30-36 cytochrome p450 oxidoreductase Homo sapiens 143-146 31445894-2 2019 The current view of electron transfer by the mammalian CPR, based on equilibrium redox potentials of the flavin cofactors, is that the two electron-reduced FMN hydroquinone (FMNH2), rather than one electron-reduced FMN semiquinone, serves as electron donor to the terminal protein acceptors. 4,6-dinitro-o-cresol 105-111 cytochrome p450 oxidoreductase Homo sapiens 55-58 31445894-8 2019 Our data on yeast CPR are in line with the previous observations of others that the flavin short-lived transient semiquinone intermediates may have a role in the electron transfer by CPR at physiological conditions. 4,6-dinitro-o-cresol 84-90 cytochrome p450 oxidoreductase Homo sapiens 18-21 31445894-8 2019 Our data on yeast CPR are in line with the previous observations of others that the flavin short-lived transient semiquinone intermediates may have a role in the electron transfer by CPR at physiological conditions. 4,6-dinitro-o-cresol 84-90 cytochrome p450 oxidoreductase Homo sapiens 183-186 28970799-5 2017 Quality of POR protein was checked by cytochrome c reduction assay as well as flavin content measurements. 4,6-dinitro-o-cresol 78-84 cytochrome p450 oxidoreductase Homo sapiens 11-14 31249341-2 2019 CPR has two flavin-containing domains: one with flavin adenine dinucleotide (FAD), called FAD domain, and the other with flavin mononucleotide (FMN), called FMN domain. 4,6-dinitro-o-cresol 12-18 cytochrome p450 oxidoreductase Homo sapiens 0-3 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. 4,6-dinitro-o-cresol 217-223 cytochrome p450 oxidoreductase Homo sapiens 62-67 21265736-1 2011 CPR (NADPH-cytochrome P450 reductase) is a multidomain protein containing two flavin-containing domains joined by a connecting domain thought to control the necessary movements of the catalytic domains during electronic cycles. 4,6-dinitro-o-cresol 78-84 cytochrome p450 oxidoreductase Homo sapiens 5-36 22097960-10 2011 Moreover, analysis of analogous cytochrome P450 reductase (CPR) variants points to key differences in the driving force for flavin reduction and suggests that the conserved FAD stacking tryptophan residue in CPR also promotes interflavin electron transfer. 4,6-dinitro-o-cresol 124-130 cytochrome p450 oxidoreductase Homo sapiens 32-57 22097960-10 2011 Moreover, analysis of analogous cytochrome P450 reductase (CPR) variants points to key differences in the driving force for flavin reduction and suggests that the conserved FAD stacking tryptophan residue in CPR also promotes interflavin electron transfer. 4,6-dinitro-o-cresol 124-130 cytochrome p450 oxidoreductase Homo sapiens 59-62 22097960-10 2011 Moreover, analysis of analogous cytochrome P450 reductase (CPR) variants points to key differences in the driving force for flavin reduction and suggests that the conserved FAD stacking tryptophan residue in CPR also promotes interflavin electron transfer. 4,6-dinitro-o-cresol 124-130 cytochrome p450 oxidoreductase Homo sapiens 208-211 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. 4,6-dinitro-o-cresol 211-217 cytochrome p450 oxidoreductase Homo sapiens 278-283 25809265-2 2015 Using small-angle x-ray scattering and nuclear magnetic resonance data, we describe the conformational free-energy landscape of the NADPH-cytochrome P450 reductase (CPR), a typical bidomain redox enzyme composed of two covalently-bound flavin domains, under various experimental conditions. 4,6-dinitro-o-cresol 236-242 cytochrome p450 oxidoreductase Homo sapiens 132-163 25809265-2 2015 Using small-angle x-ray scattering and nuclear magnetic resonance data, we describe the conformational free-energy landscape of the NADPH-cytochrome P450 reductase (CPR), a typical bidomain redox enzyme composed of two covalently-bound flavin domains, under various experimental conditions. 4,6-dinitro-o-cresol 236-242 cytochrome p450 oxidoreductase Homo sapiens 165-168 22982532-4 2012 Recent structural and biophysical studies of CYPOR have shown that the two flavin domains undergo large domain movements during catalysis. 4,6-dinitro-o-cresol 75-81 cytochrome p450 oxidoreductase Homo sapiens 45-50 22205878-7 2011 Specifically, we provide evidence that reduction of the flavin moieties in CPR induces CPR opening, whereas ligand binding induces CPR closing. 4,6-dinitro-o-cresol 56-62 cytochrome p450 oxidoreductase Homo sapiens 75-78 22205878-7 2011 Specifically, we provide evidence that reduction of the flavin moieties in CPR induces CPR opening, whereas ligand binding induces CPR closing. 4,6-dinitro-o-cresol 56-62 cytochrome p450 oxidoreductase Homo sapiens 87-90 22205878-7 2011 Specifically, we provide evidence that reduction of the flavin moieties in CPR induces CPR opening, whereas ligand binding induces CPR closing. 4,6-dinitro-o-cresol 56-62 cytochrome p450 oxidoreductase Homo sapiens 87-90 22205878-8 2011 A dynamic reaction cycle was created in which CPR optimizes internal electron transfer between flavin cofactors by adopting closed states and signals "ready and waiting" conformations to partner CYP enzymes by adopting more open states. 4,6-dinitro-o-cresol 95-101 cytochrome p450 oxidoreductase Homo sapiens 46-49 18681889-0 2008 Inter-flavin electron transfer in cytochrome P450 reductase - effects of solvent and pH identify hidden complexity in mechanism. 4,6-dinitro-o-cresol 6-12 cytochrome p450 oxidoreductase Homo sapiens 34-59 19908820-2 2009 We show that the lipid bilayer has a role in defining the redox potential of the CPR flavin domains. 4,6-dinitro-o-cresol 85-91 cytochrome p450 oxidoreductase Homo sapiens 81-84 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. 4,6-dinitro-o-cresol 32-38 cytochrome p450 oxidoreductase Homo sapiens 94-125 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. 4,6-dinitro-o-cresol 32-38 cytochrome p450 oxidoreductase Homo sapiens 127-133 7724541-3 1995 Similarities in amino acid sequence and in functional domain arrangement with other key flavoproteins, including nitric oxide synthase, make CPR an excellent prototype for studies of interactions between two flavin cofactors. 4,6-dinitro-o-cresol 208-214 cytochrome p450 oxidoreductase Homo sapiens 141-144 7840627-0 1995 Flavin-binding and protein structural integrity studies on NADPH-cytochrome P450 reductase are consistent with the presence of distinct domains. 4,6-dinitro-o-cresol 0-6 cytochrome p450 oxidoreductase Homo sapiens 59-90 6272650-0 1981 Influence of flavin addition and removal on the formation of superoxide by NADPH-Cytochrome P-450 reductase: a spin-trap study. 4,6-dinitro-o-cresol 13-19 cytochrome p450 oxidoreductase Homo sapiens 75-107 16249336-7 2005 The modulation of CYPOR by the addition of the NOS C termini is also supported by flavin reoxidation and fluorescence-quenching studies and antibody recognition of the C-terminal extension. 4,6-dinitro-o-cresol 82-88 cytochrome p450 oxidoreductase Homo sapiens 18-23 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. 4,6-dinitro-o-cresol 137-143 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. 4,6-dinitro-o-cresol 137-143 cytochrome p450 oxidoreductase Homo sapiens 112-115 12631275-8 2003 Despite overall structural resemblance of NR1 and CPR, our studies reveal thermodynamic similarities but major kinetic differences in the electron transfer reactions catalysed by the flavin-binding domains. 4,6-dinitro-o-cresol 183-189 cytochrome p450 oxidoreductase Homo sapiens 50-53 8954538-1 1996 NADPH cytochrome P450 reductase binds two flavin cofactors, FMN and FAD, per molecule of reductase. 4,6-dinitro-o-cresol 42-48 cytochrome p450 oxidoreductase Homo sapiens 0-31