PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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). Flavin-Adenine Dinucleotide 142-145 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). Flavin-Adenine Dinucleotide 142-145 cytochrome p450 oxidoreductase Homo sapiens 64-69 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. Flavin-Adenine Dinucleotide 49-52 cytochrome p450 oxidoreductase Homo sapiens 3-7 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. Flavin-Adenine Dinucleotide 86-89 cytochrome p450 oxidoreductase Homo sapiens 3-7 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. Flavin-Adenine Dinucleotide 103-106 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. Flavin-Adenine Dinucleotide 103-106 cytochrome p450 oxidoreductase Homo sapiens 32-35 23332101-7 2013 By contrast, the CPR variants (W676F and W676Y) displayed modest decreases in cytochrome c(3+) reduction, a 30- and 3.5-fold decrease in the rate of FAD reduction, accumulation of a FADH2 -NADP(+) charge-transfer complex and dramatically suppressed rates of interflavin electron transfer. Flavin-Adenine Dinucleotide 149-152 cytochrome p450 oxidoreductase Homo sapiens 17-20 25832023-2 2015 CPR is composed of a membrane anchor and a catalytic domain that contains FAD and flavin mononucleotide (FMN) as redox centers and mediates electron transfer to CYP. Flavin-Adenine Dinucleotide 74-77 cytochrome p450 oxidoreductase Homo sapiens 0-3 24589657-1 2014 Cytochrome P450 reductase (CPR) and methionine synthase reductase (MSR) transfer reducing equivalents from NADPH to FAD to FMN. Flavin-Adenine Dinucleotide 116-119 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. Flavin-Adenine Dinucleotide 116-119 cytochrome p450 oxidoreductase Homo sapiens 27-30 23332101-0 2013 Aromatic substitution of the FAD-shielding tryptophan reveals its differential role in regulating electron flux in methionine synthase reductase and cytochrome P450 reductase. Flavin-Adenine Dinucleotide 29-32 cytochrome p450 oxidoreductase Homo sapiens 149-174 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. Flavin-Adenine Dinucleotide 120-123 cytochrome p450 oxidoreductase Homo sapiens 40-65 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. Flavin-Adenine Dinucleotide 120-123 cytochrome p450 oxidoreductase Homo sapiens 67-70 23332101-9 2013 By contrast, the bulky indole ring of W676 accelerates catalysis in CPR by lowering the energy barrier for displacement of the oxidized nicotinamide ring coplanar with the FAD. Flavin-Adenine Dinucleotide 172-175 cytochrome p450 oxidoreductase Homo sapiens 68-71 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. Flavin-Adenine Dinucleotide 84-111 cytochrome p450 oxidoreductase Homo sapiens 0-5 21808038-8 2011 FAD addition to either variant prevents trypsin digestion, supporting the role of the cofactor in conferring stability to CYPOR structure. Flavin-Adenine Dinucleotide 0-3 cytochrome p450 oxidoreductase Homo sapiens 122-127 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. Flavin-Adenine Dinucleotide 156-159 cytochrome p450 oxidoreductase Homo sapiens 80-83 19931102-3 2010 CPR shuttles electrons from NADPH through the FAD and FMN-cofactors into the central heme-group of the P450s. Flavin-Adenine Dinucleotide 46-49 cytochrome p450 oxidoreductase Homo sapiens 0-3 19483672-4 2009 Available CPR structures show a closed conformation, with the two cofactors in tight proximity, which is consistent with FAD-to-FMN, but not FMN-to-P450, electron transfer. Flavin-Adenine Dinucleotide 121-124 cytochrome p450 oxidoreductase Homo sapiens 10-13 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. Flavin-Adenine Dinucleotide 113-116 cytochrome p450 oxidoreductase Homo sapiens 0-5 16391466-4 2006 CPR is a flavoprotein containing both flavine-adenine dinucleotide and flavine mononucleotide. Flavin-Adenine Dinucleotide 38-66 cytochrome p450 oxidoreductase Homo sapiens 0-3 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. Flavin-Adenine Dinucleotide 67-94 cytochrome p450 oxidoreductase Homo sapiens 0-3 17505056-4 2007 We compared the impact of missense mutations encoding for single amino acid changes in three distinct regions of the POR molecule: 1), Y181D and H628P close to the central electron transfer area, 2) S244C located within the hinge close to the flavin adenine dinucleotide and flavin mononucleotide domains of POR, and 3) A287P that is clearly distant from the two other regions. Flavin-Adenine Dinucleotide 243-270 cytochrome p450 oxidoreductase Homo sapiens 117-120 16998238-11 2006 Based on these findings, decreased FAD-binding affinity is proposed as the basis of the observed loss of CYPOR function in the Y459H and V492E POR mutations in ABS. Flavin-Adenine Dinucleotide 35-38 cytochrome p450 oxidoreductase Homo sapiens 105-110 16998238-11 2006 Based on these findings, decreased FAD-binding affinity is proposed as the basis of the observed loss of CYPOR function in the Y459H and V492E POR mutations in ABS. Flavin-Adenine Dinucleotide 35-38 cytochrome p450 oxidoreductase Homo sapiens 107-110 9237990-0 1997 Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes. Flavin-Adenine Dinucleotide 87-90 cytochrome p450 oxidoreductase Homo sapiens 31-62 12779335-4 2003 In an attempt to unambiguously characterize the redox properties of the physiologically relevant FMNH(2) form of the reductase, the T491V mutant of NADPH-cytochrome P450 reductase has been reconstituted with 5"-deazaFAD which binds to the FAD-binding site of the reductase with a K(d) of 94 nM. Flavin-Adenine Dinucleotide 216-219 cytochrome p450 oxidoreductase Homo sapiens 148-179 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. Flavin-Adenine Dinucleotide 249-276 cytochrome p450 oxidoreductase Homo sapiens 134-165 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. Flavin-Adenine Dinucleotide 249-276 cytochrome p450 oxidoreductase Homo sapiens 167-170 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. Flavin-Adenine Dinucleotide 278-281 cytochrome p450 oxidoreductase Homo sapiens 134-165 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. Flavin-Adenine Dinucleotide 278-281 cytochrome p450 oxidoreductase Homo sapiens 167-170 9237990-1 1997 Microsomal NADPH-cytochrome P450 reductase (CPR) is one of only two mammalian enzymes known to contain both FAD and FMN, the other being nitric-oxide synthase. Flavin-Adenine Dinucleotide 108-111 cytochrome p450 oxidoreductase Homo sapiens 11-42 9237990-1 1997 Microsomal NADPH-cytochrome P450 reductase (CPR) is one of only two mammalian enzymes known to contain both FAD and FMN, the other being nitric-oxide synthase. Flavin-Adenine Dinucleotide 108-111 cytochrome p450 oxidoreductase Homo sapiens 44-47 7724541-2 1995 CPR is unique in that it is one of only two mammalian enzymes known to contain both flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), the other being the various isoforms of nitric oxide synthase. Flavin-Adenine Dinucleotide 84-111 cytochrome p450 oxidoreductase Homo sapiens 0-3 7724541-2 1995 CPR is unique in that it is one of only two mammalian enzymes known to contain both flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), the other being the various isoforms of nitric oxide synthase. Flavin-Adenine Dinucleotide 113-116 cytochrome p450 oxidoreductase Homo sapiens 0-3 7513993-1 1994 To create a semi-artificial monomolecular oxygenase system, FAD or FMN were covalently bound to cytochrome P450 2B4 as electron donor centers and bleomycin to NADPH-cytochrome P450 reductase as a generator of active oxygen species. Flavin-Adenine Dinucleotide 60-63 cytochrome p450 oxidoreductase Homo sapiens 159-190 3099832-1 1986 Microsomal NADPH-cytochrome P-450 reductase is the only mammalian flavoprotein known to contain both FAD and FMN as prosthetic groups. Flavin-Adenine Dinucleotide 101-104 cytochrome p450 oxidoreductase Homo sapiens 11-43 1390631-1 1992 Fluorescence quenching and energy-transfer studies have been carried out to determine the position of FAD and FMN groups of NADPH-cytochrome P450 reductase and of the heme and substrate groups of cytochrome P450 with respect to the lipid/water interphase. Flavin-Adenine Dinucleotide 102-105 cytochrome p450 oxidoreductase Homo sapiens 124-155 32303637-2 2020 BM3 is a natural fusion enzyme comprising two major domains: a cytochrome P450 (heme-binding) catalytic domain and a NADPH-cytochrome P450 reductase (CPR) domain containing FAD and FMN cofactors in distinct domains of the CPR. Flavin-Adenine Dinucleotide 173-176 cytochrome p450 oxidoreductase Homo sapiens 117-148 32303637-2 2020 BM3 is a natural fusion enzyme comprising two major domains: a cytochrome P450 (heme-binding) catalytic domain and a NADPH-cytochrome P450 reductase (CPR) domain containing FAD and FMN cofactors in distinct domains of the CPR. Flavin-Adenine Dinucleotide 173-176 cytochrome p450 oxidoreductase Homo sapiens 150-153 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. Flavin-Adenine Dinucleotide 146-173 cytochrome p450 oxidoreductase Homo sapiens 73-76 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. Flavin-Adenine Dinucleotide 175-178 cytochrome p450 oxidoreductase Homo sapiens 73-76 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. Flavin-Adenine Dinucleotide 48-75 cytochrome p450 oxidoreductase Homo sapiens 0-3 31749697-3 2019 Electron transfer in POR occurs from NADH to FAD to FMN, and the flexible hinge region in POR is essential for domain movements to bring the FAD and FMN close together for electron transfer. Flavin-Adenine Dinucleotide 45-48 cytochrome p450 oxidoreductase Homo sapiens 21-24 31749697-3 2019 Electron transfer in POR occurs from NADH to FAD to FMN, and the flexible hinge region in POR is essential for domain movements to bring the FAD and FMN close together for electron transfer. Flavin-Adenine Dinucleotide 45-48 cytochrome p450 oxidoreductase Homo sapiens 90-93 31749697-3 2019 Electron transfer in POR occurs from NADH to FAD to FMN, and the flexible hinge region in POR is essential for domain movements to bring the FAD and FMN close together for electron transfer. Flavin-Adenine Dinucleotide 141-144 cytochrome p450 oxidoreductase Homo sapiens 21-24 31749697-3 2019 Electron transfer in POR occurs from NADH to FAD to FMN, and the flexible hinge region in POR is essential for domain movements to bring the FAD and FMN close together for electron transfer. Flavin-Adenine Dinucleotide 141-144 cytochrome p450 oxidoreductase Homo sapiens 90-93 31749697-11 2019 The negative impact of P284T mutation in the hinge region of POR seems to be due to disruption of FAD to FMN electron transfer. Flavin-Adenine Dinucleotide 98-101 cytochrome p450 oxidoreductase Homo sapiens 61-64 31445894-5 2019 In this work, we have investigated spectroscopic properties of the CPR-bound FAD and FMN reduced at 77 K by radiolytically-generated thermalized electrons. Flavin-Adenine Dinucleotide 77-80 cytochrome p450 oxidoreductase Homo sapiens 67-70 31445894-6 2019 Using UV-vis spectroscopy, we demonstrated that upon cryo-reduction of oxidized yeast CPR (yCPR) containing an equimolar ratio of both FAD and FMN, or FAD alone, neutral semiquinones were trapped at 77 K. During annealing at the elevated temperatures, unstable short-lived neutral semiquinones relaxed to spectroscopically distinct air-stable neutral semiquinones. Flavin-Adenine Dinucleotide 135-138 cytochrome p450 oxidoreductase Homo sapiens 86-89 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. Flavin-Adenine Dinucleotide 77-80 cytochrome p450 oxidoreductase Homo sapiens 0-3 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. Flavin-Adenine Dinucleotide 90-93 cytochrome p450 oxidoreductase Homo sapiens 0-3