PMID-sentid Pub_year Sent_text compound_name comp_offset prot_official_name organism prot_offset 32159324-0 2020 Covalent Modification of the Flavin in Proline Dehydrogenase by Thiazolidine-2-Carboxylate. 4,6-dinitro-o-cresol 29-35 proline dehydrogenase 1 Homo sapiens 39-60 32840348-1 2020 Prenylated FMN (prFMN) is a recently discovered modified flavin cofactor containing an additional non-aromatic ring, connected to the N5 and C6 atoms. 4,6-dinitro-o-cresol 57-63 formin 1 Homo sapiens 11-14 32459875-4 2020 Elucidation of the crystal structure of human MAO B bound to the inhibitor revealed that DPI binds deeply in the active-site cavity to establish multiple hydrophobic interactions with the surrounding side chains and the flavin. 4,6-dinitro-o-cresol 220-226 monoamine oxidase B Homo sapiens 46-51 32569467-4 2020 The metal-free flavin/NOx/TEMPO catalytic cycles are uniquely compatible, especially compared to other Nef and NOx-generating processes, and reveal selectivity over flavin-catalyzed sulfoxide formation. 4,6-dinitro-o-cresol 15-21 S100 calcium binding protein B Homo sapiens 103-106 32569467-4 2020 The metal-free flavin/NOx/TEMPO catalytic cycles are uniquely compatible, especially compared to other Nef and NOx-generating processes, and reveal selectivity over flavin-catalyzed sulfoxide formation. 4,6-dinitro-o-cresol 165-171 S100 calcium binding protein B Homo sapiens 103-106 32088324-11 2020 We also describe methods that permit correlation of the flavin content with the amount of active enzyme and thus permit simple, rapid quantitation and evaluation of purified DPD sample. 4,6-dinitro-o-cresol 56-62 dihydropyrimidine dehydrogenase Homo sapiens 174-177 32915550-3 2020 Chicken cryptochrome4 (cCRY4) has been identified as a candidate magnetoreceptive molecule due to its expression in the retina and its ability to form stable flavin neutral radicals (FADH ) upon blue light absorption. 4,6-dinitro-o-cresol 158-164 cryptochrome 4 Gallus gallus 8-21 32887801-6 2020 Importantly, we also identify a small molecule dicarboxylate that acts as an essential cofactor in this process and works in synergy with SDHAF2 to properly orient the flavin and capping domains of SDHA. 4,6-dinitro-o-cresol 168-174 succinate dehydrogenase complex assembly factor 2 Homo sapiens 138-144 32887801-6 2020 Importantly, we also identify a small molecule dicarboxylate that acts as an essential cofactor in this process and works in synergy with SDHAF2 to properly orient the flavin and capping domains of SDHA. 4,6-dinitro-o-cresol 168-174 succinate dehydrogenase complex flavoprotein subunit A Homo sapiens 138-142 32895367-8 2020 In support of this analogy, flavin-depleted proteins increasingly associated with a number of proteostasis network components, as identified by the mass spectrometry analysis of the FAD-free NQO1 aggregates. 4,6-dinitro-o-cresol 28-34 NAD(P)H quinone dehydrogenase 1 Homo sapiens 191-195 32651204-4 2020 In this study, based on the genetic manipulation and biochemical assay, we characterized XanH as an indispensable FAD-dependent halogenase (FDH) for the biosynthesis of 1 XanH was found to be a bifunctional protein capable of flavin reduction and chlorination, and exclusively used the reduced nicotinamide adenine dinucleotide (NADH). 4,6-dinitro-o-cresol 226-232 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 114-138 32651204-4 2020 In this study, based on the genetic manipulation and biochemical assay, we characterized XanH as an indispensable FAD-dependent halogenase (FDH) for the biosynthesis of 1 XanH was found to be a bifunctional protein capable of flavin reduction and chlorination, and exclusively used the reduced nicotinamide adenine dinucleotide (NADH). 4,6-dinitro-o-cresol 226-232 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 140-143 32788383-6 2020 These experiments showed that paralogs of SLC52A2 with lower riboflavin affinities could not mediate H2O2-induced cell death and that riboflavin depletion protected HAP1 cells from H2O2 toxicity through a specific process that could not be rescued by other flavin compounds. 4,6-dinitro-o-cresol 65-71 solute carrier family 52 member 2 Homo sapiens 42-49 32516403-7 2020 Retinal flavin levels were also altered in the Rtbdn-/-/Prph2R172W retina. 4,6-dinitro-o-cresol 8-14 retbindin Mus musculus 47-52 32048687-4 2020 Opto-Rac1 induction of lamellipodia formation was spatially restricted to the patterned illumination field and was efficient, requiring sparse stimulation duty ratios of ~1-2% (at the sensitivity threshold for flavin photocycling) to cause significant changes in cell morphology. 4,6-dinitro-o-cresol 210-216 Rac family small GTPase 1 Homo sapiens 5-9 30985024-1 2019 In luminous bacteria NAD(P)H:flavin-oxidoreductases LuxG and Fre, there are homologous enzymes that could provide a luciferase with reduced flavin. 4,6-dinitro-o-cresol 29-35 frizzled related protein Homo sapiens 61-64 31832774-0 2019 The Arabidopsis cryptochrome 2 I404F mutant is hypersensitive and shows flavin reduction even in the absence of light. 4,6-dinitro-o-cresol 72-78 cryptochrome 2 Arabidopsis thaliana 16-30 31075535-7 2019 Further deletion of fccA and its replacement by cctA resulted in a strain with ferric iron reduction rates similar to the wild type and a lower concentration of periplasmic flavin compared to the quadruple mutant. 4,6-dinitro-o-cresol 173-179 cytochrome c3 family protein Shewanella oneidensis MR-1 48-52 30946572-4 2019 A flavin-dependent oxidase encoded by gene ro02984 was found to oxidize either mandelic acid or phenylglyoxal. 4,6-dinitro-o-cresol 2-8 multicopper oxidase family protein Rhodococcus jostii RHA1 19-26 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 31407761-0 2019 A detailed mechanism of the oxidative half-reaction of d-amino acid oxidase: another route for flavin oxidation. 4,6-dinitro-o-cresol 95-101 D-amino acid oxidase Homo sapiens 55-75 31407761-2 2019 DAAO catalyses hydride transfer from the substrate to the flavin in the reductive half-reaction, and the flavin is reoxidized by O2 in the oxidative half-reaction. 4,6-dinitro-o-cresol 58-64 D-amino acid oxidase Homo sapiens 0-4 31407761-2 2019 DAAO catalyses hydride transfer from the substrate to the flavin in the reductive half-reaction, and the flavin is reoxidized by O2 in the oxidative half-reaction. 4,6-dinitro-o-cresol 105-111 D-amino acid oxidase Homo sapiens 0-4 31175188-2 2019 It is currently unclear how maturation of FccA and other periplasmic flavoproteins is achieved, specifically in the context of flavin cofactor loading, and the fitness cost of flavin secretion has not been quantified. 4,6-dinitro-o-cresol 127-133 flavocytochrome c Shewanella oneidensis MR-1 42-46 31033286-3 2019 Formation of the AviCys in cypemycin requires an oxidative decarboxylation of the precursor peptide C-terminal Cys, and this reaction is catalyzed by a flavin-dependent decarboxylase CypD. 4,6-dinitro-o-cresol 152-158 peptidylprolyl isomerase D Homo sapiens 183-187 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 31033286-8 2019 These results provide important mechanistic insights into CypD and other flavin-dependent Cys decarboxylases, and could facilitate future biosynthetic and bioengineering efforts in studying AviCys-containing RiPPs. 4,6-dinitro-o-cresol 73-79 peptidylprolyl isomerase D Homo sapiens 58-62 30685643-1 2019 Human dihydroorotate dehydrogenase (hDHODH) is a flavin-dependent enzyme essential to pyrimidine de novo biosynthesis, which serves as an attractive therapeutic target for the treatment of autoimmune disorders. 4,6-dinitro-o-cresol 49-55 dihydroorotate dehydrogenase (quinone) Homo sapiens 36-42 30657259-3 2019 Of note are the recent studies of cytochrome P450 reductases (CPR)-P450 (CYP) endoplasmic reticulum redox chains, showing the relationship between dynamics and electron flow through flavin and haem redox centres and the impact this has on monooxygenation chemistry. 4,6-dinitro-o-cresol 182-188 peptidylprolyl isomerase G Homo sapiens 73-76 31142738-1 2019 The UbiX-UbiD enzymes are widespread in microbes, acting in concert to decarboxylate alpha-beta unsaturated carboxylic acids using a highly modified flavin cofactor, prenylated FMN (prFMN). 4,6-dinitro-o-cresol 149-155 formin 1 Homo sapiens 177-180 31105635-4 2019 D-amino acid oxidase (DAO) is a flavin-dependent enzyme widely distributed in the central nervous system. 4,6-dinitro-o-cresol 32-38 D-amino acid oxidase Homo sapiens 0-20 31105635-4 2019 D-amino acid oxidase (DAO) is a flavin-dependent enzyme widely distributed in the central nervous system. 4,6-dinitro-o-cresol 32-38 D-amino acid oxidase Homo sapiens 22-25 30615965-0 2019 Anion-specific interaction with human NQO1 inhibits flavin binding. 4,6-dinitro-o-cresol 52-58 NAD(P)H quinone dehydrogenase 1 Homo sapiens 38-42 31027295-3 2019 Two main families of thymidylate synthases have been identified in bacteria, folate-dependent thymidylate synthase (TS) and flavin-dependent TS (FDTS). 4,6-dinitro-o-cresol 124-130 thymidylate synthetase Homo sapiens 21-41 31027295-3 2019 Two main families of thymidylate synthases have been identified in bacteria, folate-dependent thymidylate synthase (TS) and flavin-dependent TS (FDTS). 4,6-dinitro-o-cresol 124-130 thymidylate synthetase Homo sapiens 116-118 30615965-4 2019 It is known that NQO1 stability in vivo is strongly modulated by binding of its flavin cofactor. 4,6-dinitro-o-cresol 80-86 NAD(P)H quinone dehydrogenase 1 Homo sapiens 17-21 31191868-1 2019 We have previously described the synthesis and evaluation of 3,5-diamino-1,2,4-triazole analogues as inhibitors of the flavin-dependent histone demethylase LSD1. 4,6-dinitro-o-cresol 119-125 lysine demethylase 1A Homo sapiens 156-160 30243998-2 2019 We investigated here the effects of phosphorylating S82 in human NADP(H):quinone oxidoreductase 1, a representative example of disease-associated flavoprotein in which protein stability is coupled to the intracellular flavin levels. 4,6-dinitro-o-cresol 218-224 NAD(P)H quinone dehydrogenase 1 Homo sapiens 65-97 30671578-3 2019 Two mechanisms of multistep hopping of charge to/from the oxidised/reduced flavin-based moiety through residues of aromatic amino acids located in GOx and long range charge direct tunnelling from the cofactor to the organic semiconductor surface have been proposed and evaluated. 4,6-dinitro-o-cresol 75-81 hydroxyacid oxidase 1 Homo sapiens 147-150 30246917-0 2019 Steric hindrance controls pyridine nucleotide specificity of a flavin-dependent NADH:quinone oxidoreductase. 4,6-dinitro-o-cresol 63-69 crystallin zeta Homo sapiens 85-107 31072498-1 2019 Prenylated flavin mononucleotide (prFMN) is a recently discovered flavin cofactor produced by the UbiX family of FMN prenyltransferases, and is required for the activity of UbiD-like reversible decarboxylases. 4,6-dinitro-o-cresol 11-17 formin 1 Homo sapiens 36-39 31172469-3 2019 In a flavin-dependent fashion, cytochrome b558 shuttles electrons from cytoplasmic NADPH across membranes to molecular oxygen and thereby generates superoxide anion. 4,6-dinitro-o-cresol 5-11 mitochondrially encoded cytochrome b Homo sapiens 31-43 30451826-4 2018 Structural and enzymatic analyses indicate that Osm1 has a specific binding pocket for flavin molecules, including FAD, FMN, and riboflavin, catalyzing their oxidation while reducing fumarate to succinate. 4,6-dinitro-o-cresol 87-93 fumarate reductase Saccharomyces cerevisiae S288C 48-52 30358055-3 2018 Demonstrated herein is the incorporation of a natural flavin cofactor (FMN) into the specific microenvironment of a water-soluble polymer which allows the efficient reduction of the FMN by NADH in aqueous solution. 4,6-dinitro-o-cresol 54-60 formin 1 Homo sapiens 71-74 30358055-3 2018 Demonstrated herein is the incorporation of a natural flavin cofactor (FMN) into the specific microenvironment of a water-soluble polymer which allows the efficient reduction of the FMN by NADH in aqueous solution. 4,6-dinitro-o-cresol 54-60 formin 1 Homo sapiens 182-185 29948731-3 2018 Mutations in NDUFV1 (Flavin binding subunit of Respiratory complex 1) results in neurological manifestations including Leigh syndrome and leucoencephalopathy. 4,6-dinitro-o-cresol 21-27 NADH:ubiquinone oxidoreductase core subunit V1 Homo sapiens 13-19 30052294-3 2019 The co-crystal of F-Tyr and a T239A variant of human IYD have now been characterized to provide a structural basis for control of its flavin reactivity. 4,6-dinitro-o-cresol 134-140 iodotyrosine deiodinase Homo sapiens 53-56 30052294-6 2019 Even substitution of Thr with Ser decreases the midpoint potential of human IYD between its oxidized and semiquinone forms of flavin by almost 80 mV. 4,6-dinitro-o-cresol 126-132 iodotyrosine deiodinase Homo sapiens 76-79 30052295-8 2019 This shows that some of the ability of thioredoxin reductase to reduce this substrate comes from the flavin coenzyme. 4,6-dinitro-o-cresol 101-107 peroxiredoxin 2 Mus musculus 39-60 30451826-6 2018 We conclude that soluble eukaryotic fumarate reductases can maintain an oxidizing environment under anaerobic conditions, either by oxidizing cellular flavin cofactors or by a direct interaction with flavoenzymes such as Ero1. 4,6-dinitro-o-cresol 151-157 ER oxidoreductin Saccharomyces cerevisiae S288C 221-225 30157376-4 2018 The flavin radicals accumulated with logistic time-dependent kinetics when the protein concentrations were higher than 30 muM. 4,6-dinitro-o-cresol 4-10 latexin Homo sapiens 122-125 30345401-3 2018 Formation of AviCys moiety requires an oxidative decarboxylation of the C-terminal Cys of the precursor peptide CypA, and this process is catalyzed by a flavin-containing protein CypD. 4,6-dinitro-o-cresol 153-159 peptidylprolyl isomerase A Mus musculus 112-116 30345401-3 2018 Formation of AviCys moiety requires an oxidative decarboxylation of the C-terminal Cys of the precursor peptide CypA, and this process is catalyzed by a flavin-containing protein CypD. 4,6-dinitro-o-cresol 153-159 peptidylprolyl isomerase F (cyclophilin F) Mus musculus 179-183 29894198-1 2018 Nitration of tetraphenylporphyrin cage compound 1, at -40 C, leads to the regioselective formation of the chiral mononitro compound 2 (75% isolated yield) and, at -30 C, to the achiral syn-dinitro-derivative 3 and the chiral anti-dinitro derivative 4 in a diastereomeric ratio of 5:2, which were separated by chromatography (46 and 20% yields, respectively). 4,6-dinitro-o-cresol 191-198 synemin Homo sapiens 187-190 29894198-1 2018 Nitration of tetraphenylporphyrin cage compound 1, at -40 C, leads to the regioselective formation of the chiral mononitro compound 2 (75% isolated yield) and, at -30 C, to the achiral syn-dinitro-derivative 3 and the chiral anti-dinitro derivative 4 in a diastereomeric ratio of 5:2, which were separated by chromatography (46 and 20% yields, respectively). 4,6-dinitro-o-cresol 232-239 synemin Homo sapiens 187-190 29768224-1 2018 p-Hydroxyphenylacetate 3-hydroxylase component 1 (C1) is a useful enzyme for generating reduced flavin and NAD+ intermediates. 4,6-dinitro-o-cresol 96-102 heterogeneous nuclear ribonucleoprotein C Homo sapiens 50-52 29274788-6 2018 The recombinant G183R hDAAO is produced as an inactive apoprotein: the substitution alters the protein conformation that negatively affects the ability to bind the flavin cofactor in the orientation required for hydride-transfer during catalysis. 4,6-dinitro-o-cresol 164-170 D-amino acid oxidase Homo sapiens 22-27 29648801-5 2018 PRODH is a flavin-dependent enzyme that couples proline oxidation with reduction of membrane-bound quinone, while GSALDH catalyzes the NAD+-dependent oxidation of GSAL to glutamate. 4,6-dinitro-o-cresol 11-17 proline dehydrogenase 1 Homo sapiens 0-5 28579060-7 2018 Flavin supplementation might prove to be beneficial for those mutations triggering FAD loss in the hE3 component. 4,6-dinitro-o-cresol 0-6 dihydrolipoamide dehydrogenase Homo sapiens 99-102 29912243-1 2018 A bipyridine ruthenium(ii) complex (Ru-1) with a flavin moiety connected to one of the bipyridine ligands via an acetylene bond was designed and synthesized, and its photophysical properties were investigated. 4,6-dinitro-o-cresol 49-55 Scm like with four mbt domains 1 Homo sapiens 36-40 29912243-2 2018 Compared with the tris(bipyridine) Ru(ii) complex (Ru-0), which has an extinction coefficient epsilon = 1.36 x 104 M-1 cm-1 at 453 nm, the introduction of the flavin moiety endows Ru-1 with strong absorption in the visible range (epsilon = 2.34 x 104 M-1 cm-1 at 456 nm). 4,6-dinitro-o-cresol 159-165 Scm like with four mbt domains 1 Homo sapiens 180-184 29912243-4 2018 We propose that the emission of Ru-1 originates from the low lying triplet excited state of 3IL according to the time-resolved transient difference absorption spectra, the calculated T1 spin density and the T1 thermo-vibration modes localized on the flavin-decorated bipyridine ligand. 4,6-dinitro-o-cresol 250-256 Scm like with four mbt domains 1 Homo sapiens 32-36 29973922-15 2018 A flavin-based electron confurcating (FBEC) HdrABC complex is proposed for nitrate-dependent reverse methanogenesis in which the oxidation of CoM-SH/CoB-SH and Fdx2- is coupled to reduction of F420. 4,6-dinitro-o-cresol 2-8 ferredoxin 2 Homo sapiens 160-164 29669807-0 2018 PqsL uses reduced flavin to produce 2-hydroxylaminobenzoylacetate, a preferred PqsBC substrate in alkyl quinolone biosynthesis in Pseudomonas aeruginosa. 4,6-dinitro-o-cresol 18-24 monooxygenase Pseudomonas aeruginosa PAO1 0-4 29669807-4 2018 However, we found that unlike related enzymes, PqsL hydroxylates a primary aromatic amine group, and it does not use NAD(P)H as cosubstrate, but unexpectedly required reduced flavin as electron donor. 4,6-dinitro-o-cresol 175-181 monooxygenase Pseudomonas aeruginosa PAO1 47-51 29669807-8 2018 Our study completes the AQNO biosynthetic pathway in P. aeruginosa, indicating that PqsL produces the unstable product 2-hydroxylaminobenzoylacetate from 2-ABA and depends on free reduced flavin as electron donor instead of NAD(P)H. 4,6-dinitro-o-cresol 188-194 monooxygenase Pseudomonas aeruginosa PAO1 84-88 29532940-5 2018 Using ectopic expression and silencing, gene expression analysis, protein interaction and chromatin immunoprecipitation experiments, we show that PttGIs are likely to act in a complex with PttFKF1s (FLAVIN-BINDING, KELCH REPEAT, F-BOX 1) and PttCDFs (CYCLING DOF FACTOR) to control the expression of PttFT2, the key gene regulating short-day-induced growth cessation in Populus. 4,6-dinitro-o-cresol 199-205 flavin-binding, kelch repeat, f box 1 Arabidopsis thaliana 229-236 29429898-2 2018 The mechanisms of flavin reduction and hydrogen peroxide production by KMO inhibitors are unknown. 4,6-dinitro-o-cresol 18-24 kynurenine 3-monooxygenase Saccharomyces cerevisiae S288C 71-74 29429898-4 2018 Proton transfer in the hydrogen bond network triggers flavin reduction in p-hydroxybenzoate hydroxylase, but the mechanism triggering flavin reduction in KMO is different. 4,6-dinitro-o-cresol 54-60 kynurenine 3-monooxygenase Saccharomyces cerevisiae S288C 154-157 29429898-4 2018 Proton transfer in the hydrogen bond network triggers flavin reduction in p-hydroxybenzoate hydroxylase, but the mechanism triggering flavin reduction in KMO is different. 4,6-dinitro-o-cresol 134-140 kynurenine 3-monooxygenase Saccharomyces cerevisiae S288C 154-157 29581265-6 2018 Differential effects of Trp-mediated flavin photoreduction on cellular turnover of TIM and dCRY indicate that these activities are separated in time and space. 4,6-dinitro-o-cresol 37-43 timeless Drosophila melanogaster 83-86 29487133-5 2018 We found that the most potent BLVRB inhibitors contain a tricyclic hydrocarbon core structure similar to the isoalloxazine ring of flavin mononucleotide and that both xanthene- and acridine-based compounds inhibit BLVRB"s flavin and dichlorophenolindophenol (DCPIP) reductase functions. 4,6-dinitro-o-cresol 131-137 biliverdin reductase B Homo sapiens 30-35 29138259-1 2017 Spermine oxidase (SMOX) is a flavin-containing enzyme that oxidizes spermine to produce spermidine, 3-aminopropanaldehyde, and hydrogen peroxide. 4,6-dinitro-o-cresol 29-35 spermine oxidase Homo sapiens 0-16 29632820-1 2018 Dihydroorotate dehydrogenase (DHODH) is a flavin-binding enzyme essential for pyrimidine biosynthesis, which converts dihydroorotate to orotate. 4,6-dinitro-o-cresol 42-48 dihydroorotate dehydrogenase (quinone) Homo sapiens 30-35 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 29111436-4 2018 In addition, upon complex formation, we measured an increase of cytochrome b5 reductase flavin autofluorescence that was dependent upon the presence of cytochrome b5. 4,6-dinitro-o-cresol 88-94 cytochrome b5 type A Homo sapiens 64-77 29111436-4 2018 In addition, upon complex formation, we measured an increase of cytochrome b5 reductase flavin autofluorescence that was dependent upon the presence of cytochrome b5. 4,6-dinitro-o-cresol 88-94 cytochrome b5 type A Homo sapiens 152-165 29210583-4 2018 Subsequently, a 500 mus loss of beta-sheet structure ~25 A away from flavin was resolved and suggested to be part of the signal conduction to the CCT. 4,6-dinitro-o-cresol 69-75 CCT Homo sapiens 146-149 29316637-1 2018 FAD synthase (FADS, EC 2.7.7.2) is the last essential enzyme involved in the pathway of biosynthesis of Flavin cofactors starting from Riboflavin (Rf). 4,6-dinitro-o-cresol 104-110 flavin adenine dinucleotide synthetase 1 Homo sapiens 0-12 29316637-1 2018 FAD synthase (FADS, EC 2.7.7.2) is the last essential enzyme involved in the pathway of biosynthesis of Flavin cofactors starting from Riboflavin (Rf). 4,6-dinitro-o-cresol 104-110 flavin adenine dinucleotide synthetase 1 Homo sapiens 14-18 29190076-4 2017 In this study, the typical ultraviolet-visible (UV-vis) absorption spectrum of oxidized flavin was observed for the S101C enzyme in HEPES, TES, or sodium phosphate, whereas an absorption spectrum suggesting the presence of a C4a-flavin adduct with cysteine was obtained in Tris-HCl at pH 8.0. pH titrations of the UV-vis absorption spectrum of the wild-type, S101A, S101C, and H99N enzymes in the presence and absence of Tris allowed for the determination of two pKa values that define a pH range in which the C4a-S-cysteinyl flavin is stabilized. 4,6-dinitro-o-cresol 88-94 complement C4A (Rodgers blood group) Homo sapiens 225-228 29190076-4 2017 In this study, the typical ultraviolet-visible (UV-vis) absorption spectrum of oxidized flavin was observed for the S101C enzyme in HEPES, TES, or sodium phosphate, whereas an absorption spectrum suggesting the presence of a C4a-flavin adduct with cysteine was obtained in Tris-HCl at pH 8.0. pH titrations of the UV-vis absorption spectrum of the wild-type, S101A, S101C, and H99N enzymes in the presence and absence of Tris allowed for the determination of two pKa values that define a pH range in which the C4a-S-cysteinyl flavin is stabilized. 4,6-dinitro-o-cresol 88-94 complement C4A (Rodgers blood group) Homo sapiens 510-513 29326945-7 2017 hDAAO shows a very low affinity for the flavin cofactor. 4,6-dinitro-o-cresol 40-46 D-amino acid oxidase Homo sapiens 0-5 29198865-1 2018 Lysine-specific demethylase 1 (LSD1) is a flavin-dependent enzyme that removes methyl groups from mono- or dimethylated lysine residues at the fourth position of histone H3. 4,6-dinitro-o-cresol 42-48 lysine demethylase 1A Homo sapiens 0-29 29198865-1 2018 Lysine-specific demethylase 1 (LSD1) is a flavin-dependent enzyme that removes methyl groups from mono- or dimethylated lysine residues at the fourth position of histone H3. 4,6-dinitro-o-cresol 42-48 lysine demethylase 1A Homo sapiens 31-35 29721980-0 2018 Retbindin Is Capable of Protecting Photoreceptors from Flavin-Sensitized Light-Mediated Cell Death In Vitro. 4,6-dinitro-o-cresol 55-61 retbindin Homo sapiens 0-9 29721980-3 2018 Here we confirm that Rtbdn is capable of flavin binding and that this characteristic can protect photoreceptors from flavin-sensitized light damage. 4,6-dinitro-o-cresol 41-47 retbindin Homo sapiens 21-26 29721980-3 2018 Here we confirm that Rtbdn is capable of flavin binding and that this characteristic can protect photoreceptors from flavin-sensitized light damage. 4,6-dinitro-o-cresol 117-123 retbindin Homo sapiens 21-26 29138259-1 2017 Spermine oxidase (SMOX) is a flavin-containing enzyme that oxidizes spermine to produce spermidine, 3-aminopropanaldehyde, and hydrogen peroxide. 4,6-dinitro-o-cresol 29-35 spermine oxidase Homo sapiens 18-22 28774660-1 2017 Iodotyrosine deiodinase (IYD) is unusual for its reliance on flavin to promote reductive dehalogenation under aerobic conditions. 4,6-dinitro-o-cresol 61-67 iodotyrosine deiodinase Homo sapiens 0-23 28847921-13 2017 In recent years, novel bacterial lactate-oxidizing enzymes have been continually reported, including the unique NAD-independent d-lactate dehydrogenase that contains an Fe-S oxidoreductase domain besides the typical flavin-containing domain (Fe-S d-iLDH). 4,6-dinitro-o-cresol 216-222 FAD-binding oxidoreductase Pseudomonas putida KT2440 128-151 28821425-0 2017 Flavin-dependent thymidylate synthase: N5 of flavin as a Methylene carrier. 4,6-dinitro-o-cresol 0-6 thymidylate synthetase Homo sapiens 17-37 28821425-0 2017 Flavin-dependent thymidylate synthase: N5 of flavin as a Methylene carrier. 4,6-dinitro-o-cresol 45-51 thymidylate synthetase Homo sapiens 17-37 28821425-5 2017 The flavin-dependent catalytic mechanism is different than thymidylate synthase because it requires flavin as a reducing agent and methylene transporter. 4,6-dinitro-o-cresol 4-10 thymidylate synthetase Homo sapiens 59-79 28577910-3 2017 Over the past decade, a variety of biochemical, spectroscopic, structural and mechanistic studies of IDI-2 have provided mounting evidence that the flavin coenzyme of IDI-2 acts in a most unusual manner - as an acid/base catalyst to mediate a 1,3-proton addition/elimination reaction. 4,6-dinitro-o-cresol 148-154 isopentenyl-diphosphate delta isomerase 2 Homo sapiens 101-106 28577910-3 2017 Over the past decade, a variety of biochemical, spectroscopic, structural and mechanistic studies of IDI-2 have provided mounting evidence that the flavin coenzyme of IDI-2 acts in a most unusual manner - as an acid/base catalyst to mediate a 1,3-proton addition/elimination reaction. 4,6-dinitro-o-cresol 148-154 isopentenyl-diphosphate delta isomerase 2 Homo sapiens 167-172 28577910-4 2017 While not entirely without precedent, IDI-2 is by far the most extensively studied flavoenzyme that employs flavin-mediated acid/base catalysis. 4,6-dinitro-o-cresol 108-114 isopentenyl-diphosphate delta isomerase 2 Homo sapiens 38-43 28821425-5 2017 The flavin-dependent catalytic mechanism is different than thymidylate synthase because it requires flavin as a reducing agent and methylene transporter. 4,6-dinitro-o-cresol 100-106 thymidylate synthetase Homo sapiens 59-79 28774660-1 2017 Iodotyrosine deiodinase (IYD) is unusual for its reliance on flavin to promote reductive dehalogenation under aerobic conditions. 4,6-dinitro-o-cresol 61-67 iodotyrosine deiodinase Homo sapiens 25-28 28821425-6 2017 This catalytic mechanism is not well-understood, but since it is known to be very different from thymidylate synthase, there is potential for mechanism-based inhibitors that can selectively inhibit the flavin-dependent enzyme to target many human pathogens with low host toxicity. 4,6-dinitro-o-cresol 202-208 thymidylate synthetase Homo sapiens 97-117 28577910-5 2017 Thus, IDI-2 serves as an important mechanistic model for understanding this often overlooked, but potentially widespread reactivity of flavin coenzymes. 4,6-dinitro-o-cresol 135-141 isopentenyl-diphosphate delta isomerase 2 Homo sapiens 6-11 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 28808132-3 2017 Etfs are flavin-containing heterodimers best known for donating electrons derived from fatty acid and amino acid oxidation to an electron transfer respiratory chain via Etf-quinone oxidoreductase. 4,6-dinitro-o-cresol 9-15 crystallin zeta Homo sapiens 173-195 28783258-3 2017 Here, we define further mechanistic details of the NAD(P)H FAD hydride-transfer step of the reaction based on spectroscopic studies and high-resolution (~ 1.5 A) crystallographic views of the nicotinamide-flavin interaction in crystals of corn root FNR Tyr316Ser and Tyr316Ala variants soaked with either nicotinamide, NADP+ , or NADPH. 4,6-dinitro-o-cresol 207-213 Ferredoxin--NADP reductase, embryo isozyme, chloroplastic-like Zea mays 251-254 28890968-0 2017 Ultrafast flavin photoreduction in an oxidized animal (6-4) photolyase through an unconventional tryptophan tetrad. 4,6-dinitro-o-cresol 10-16 6-4 photolyase Xenopus laevis 55-70 28970799-8 2017 The mutation Q153R initially identified in a patient with disordered steroidogenesis showed remarkably increased activities of both CYP19A1 and CYP3A4 without any significant change in flavin content, indicating improved protein-protein interactions between POR Q153R and some P450 proteins. 4,6-dinitro-o-cresol 185-191 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 144-150 28643772-4 2017 Here we report the in vitro reconstitution of an unusual flavin-dependent bacterial indoloterpenoid cyclase, XiaF, together with a designated flavoenzyme-reductase (XiaP) that mediates a key step in xiamycin biosynthesis. 4,6-dinitro-o-cresol 57-63 X-linked inhibitor of apoptosis Homo sapiens 165-169 28458234-6 2017 Electrochemically induced FTIR difference spectra revealed that the flavin cofactor in AdR also changes due to the interaction with [2Fe2S] cluster in the Adx/AdR electron transfer complex. 4,6-dinitro-o-cresol 68-74 ferredoxin reductase Homo sapiens 87-90 28458234-6 2017 Electrochemically induced FTIR difference spectra revealed that the flavin cofactor in AdR also changes due to the interaction with [2Fe2S] cluster in the Adx/AdR electron transfer complex. 4,6-dinitro-o-cresol 68-74 ferredoxin 1 Homo sapiens 155-158 28458234-6 2017 Electrochemically induced FTIR difference spectra revealed that the flavin cofactor in AdR also changes due to the interaction with [2Fe2S] cluster in the Adx/AdR electron transfer complex. 4,6-dinitro-o-cresol 68-74 ferredoxin reductase Homo sapiens 159-162 29088714-2 2017 LSD1 is a flavin-containing AO that specifically catalyzes the demethylation of mono- and di-methylated histone H3 lysine 4 through an FAD-dependent oxidative reaction. 4,6-dinitro-o-cresol 10-16 lysine demethylase 1A Homo sapiens 0-4 29348830-3 2017 As a kind of iron flavin dependent enzyme, dihydroorotate dehydrogenase (DHODH, EC 1.3.3.1) is the fourth and a key enzyme in the de novo biosynthesis of pyrimidines. 4,6-dinitro-o-cresol 18-24 dihydroorotate dehydrogenase (quinone) Homo sapiens 43-71 29348830-3 2017 As a kind of iron flavin dependent enzyme, dihydroorotate dehydrogenase (DHODH, EC 1.3.3.1) is the fourth and a key enzyme in the de novo biosynthesis of pyrimidines. 4,6-dinitro-o-cresol 18-24 dihydroorotate dehydrogenase (quinone) Homo sapiens 73-78 28512131-2 2017 The first step in this pathway is catalyzed by a flavoprotein, sulfide quinone oxidoreductase (SQR), which converts H2S to a persulfide and transfers electrons to coenzyme Q via a flavin cofactor. 4,6-dinitro-o-cresol 180-186 crystallin zeta Homo sapiens 71-93 28146103-3 2017 In this study, we hypothesized that human quinone reductase 2 (hQR2), known to act as a flavin redox switch upon binding to the broadly used antimalarial chloroquine, could be involved in the activity of the redox-active indolone derivatives. 4,6-dinitro-o-cresol 88-94 N-ribosyldihydronicotinamide:quinone reductase 2 Homo sapiens 42-61 28566714-8 2017 The results obtained suggest that the functioning of mitochondrial flavin-binding enzymes, Nde1p for instance, is required for the hyperpolarization of inner mitochondrial membrane and ROS production in respiring S. cerevisiae cells under heat-shock conditions. 4,6-dinitro-o-cresol 67-73 NADH-ubiquinone reductase (H(+)-translocating) NDE1 Saccharomyces cerevisiae S288C 91-96 28103421-4 2017 Here, we report the 2.3 A structure of Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) and find that the position of the two flavin cofactors differs from that of other known CPR structures. 4,6-dinitro-o-cresol 139-145 P450 reductase 2 Arabidopsis thaliana 95-99 28134365-1 2017 Ndi1 is a special type-II complex I nicotinamide-adenine-dinucleotide (NADH):ubiquinone (UQ) oxidoreductase in the yeast respiratory chain, with two bound UQs (UQI and UQII) mediating electron transfer from flavin cofactors to ubiquinone, in the absence of Fe-S chains. 4,6-dinitro-o-cresol 207-213 NADH-ubiquinone reductase (H(+)-translocating) NDI1 Saccharomyces cerevisiae S288C 0-4 27851982-2 2017 Interdomain electron transfer between the flavin and cytochrome domain in CDH, preceding the electron flow to lytic polysaccharide monooxygenase, is known to be pH dependent, but the exact mechanism of this regulation has not been experimentally proven so far. 4,6-dinitro-o-cresol 42-48 choline dehydrogenase Homo sapiens 74-77 28146103-3 2017 In this study, we hypothesized that human quinone reductase 2 (hQR2), known to act as a flavin redox switch upon binding to the broadly used antimalarial chloroquine, could be involved in the activity of the redox-active indolone derivatives. 4,6-dinitro-o-cresol 88-94 N-ribosyldihydronicotinamide:quinone reductase 2 Homo sapiens 63-67 27470128-2 2016 Using a flavin-dependent oxidative mechanism, LSD1 demethylates the N-terminal tail of histone H3 in the context of a variety of developmental processes. 4,6-dinitro-o-cresol 8-14 lysine demethylase 1A Homo sapiens 46-50 28098177-2 2017 X-ray diffraction structures of oxidoreductase flavoenzymes have revealed recurrent features which facilitate catalysis, such as a hydrogen bond between a main chain nitrogen atom and the flavin redox center (N5). 4,6-dinitro-o-cresol 188-194 thioredoxin reductase 1 Homo sapiens 32-46 28755362-4 2017 The Cytb 558 is the membrane catalytic core of the NADPH oxidase complex, through which the reducing equivalent provided by NADPH is transferred via the associated prosthetic groups (one flavin and two hemes) to reduce dioxygen into superoxide anion. 4,6-dinitro-o-cresol 187-193 mitochondrially encoded cytochrome b Homo sapiens 4-8 27734680-3 2016 In this work, we present atomistic empirical valence bond simulations of the rate-limiting step of the MAO-A-catalyzed NA (norepinephrine) degradation, involving hydride transfer from the substrate alpha-methylene group to the flavin moiety of the flavin adenine dinucleotide prosthetic group, employing the full dimensionality and thermal fluctuations of the hydrated enzyme, with extensive configurational sampling. 4,6-dinitro-o-cresol 227-233 monoamine oxidase A Homo sapiens 103-108 27806563-6 2016 The Y118A SsuE FMN cofactor was reduced with approximately 1 equiv of NADPH in anaerobic titration experiments, and the flavin remained bound following reduction. 4,6-dinitro-o-cresol 120-126 formin 1 Homo sapiens 15-18 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 27613870-5 2016 We found that S1179D substitution in CaM-free eNOS had multiple effects; it increased the rate of flavin reduction, altered the conformational equilibrium of the reductase domain, and increased the rate of its conformational transitions. 4,6-dinitro-o-cresol 98-104 nitric oxide synthase 3 Homo sapiens 46-50 27295021-1 2016 Spermine oxidase (SMOX) is a flavin-containing enzyme that specifically oxidizes spermine to produce spermidine, 3-aminopropanaldehyde and hydrogen peroxide. 4,6-dinitro-o-cresol 29-35 spermine oxidase Homo sapiens 0-16 27295021-1 2016 Spermine oxidase (SMOX) is a flavin-containing enzyme that specifically oxidizes spermine to produce spermidine, 3-aminopropanaldehyde and hydrogen peroxide. 4,6-dinitro-o-cresol 29-35 spermine oxidase Homo sapiens 18-22 27590343-4 2016 It transferred electrons from F420H2 to thioredoxin via protein-bound flavin; Km values for thioredoxin and F420H2 were 6.3 and 28.6 mum, respectively. 4,6-dinitro-o-cresol 70-76 thioredoxin Homo sapiens 40-51 27590343-4 2016 It transferred electrons from F420H2 to thioredoxin via protein-bound flavin; Km values for thioredoxin and F420H2 were 6.3 and 28.6 mum, respectively. 4,6-dinitro-o-cresol 70-76 thioredoxin Homo sapiens 92-103 27423124-2 2016 Photon absorption by Arabidopsis cryptochromes cry1 and cry2 initiates electron transfer to the oxidized flavin cofactor (FADox) and formation of the presumed biological signaling state FADH . 4,6-dinitro-o-cresol 105-111 cryptochrome 1 Arabidopsis thaliana 47-51 27423124-2 2016 Photon absorption by Arabidopsis cryptochromes cry1 and cry2 initiates electron transfer to the oxidized flavin cofactor (FADox) and formation of the presumed biological signaling state FADH . 4,6-dinitro-o-cresol 105-111 cryptochrome 2 Arabidopsis thaliana 56-60 27461959-4 2016 The D634A and D634N variants elicited a modest increase in coenzyme binding affinity coupled with a 36- and 10-fold reduction in cytochrome c(3+) turnover and a 17- and 3-fold decrease in the pre-steady state rate of flavin reduction. 4,6-dinitro-o-cresol 217-223 cytochrome c, somatic Homo sapiens 129-141 27207795-4 2016 BLVRB(S111L) encompassed within the substrate/cofactor [alpha/beta dinucleotide NAD(P)H] binding fold is a functionally defective redox coupler using flavin and biliverdin (BV) IXbeta tetrapyrrole(s) and results in exaggerated reactive oxygen species accumulation as a putative metabolic signal leading to differential hematopoietic lineage commitment and enhanced thrombopoiesis. 4,6-dinitro-o-cresol 150-156 biliverdin reductase B Homo sapiens 0-5 27551082-2 2016 Photoreduction of the Drosophila CRY (dCRY) flavin cofactor to the anionic semiquinone (ASQ) restructures a C-terminal tail helix (CTT) that otherwise inhibits interactions with targets that include the clock protein Timeless (TIM). 4,6-dinitro-o-cresol 44-50 timeless Drosophila melanogaster 217-225 27551082-2 2016 Photoreduction of the Drosophila CRY (dCRY) flavin cofactor to the anionic semiquinone (ASQ) restructures a C-terminal tail helix (CTT) that otherwise inhibits interactions with targets that include the clock protein Timeless (TIM). 4,6-dinitro-o-cresol 44-50 timeless Drosophila melanogaster 227-230 27189945-5 2016 The DeltaGly-141 and DeltaG141/E142N mutants were inactive with cytochrome P450 but fully active in reducing cytochrome c In the DeltaGly-141 mutants, the backbone amide of Glu/Asn-142 forms an H-bond to the N5 of the oxidized flavin, which leads to formation of an unstable red anionic semiquinone with a more negative potential than the hydroquinone. 4,6-dinitro-o-cresol 227-233 cytochrome c, somatic Homo sapiens 109-121 27528074-2 2016 Here we tested the phototoxic effects of the flavin-containing phototoxic protein miniSOG targeted to the cytoplasmic surfaces of late endosomes and lysosomes by fusion with Rab7. 4,6-dinitro-o-cresol 45-51 RAB7B, member RAS oncogene family Homo sapiens 174-178 27040799-6 2016 Proline dehydrogenase/proline oxidase (PRODH/POX) is flavin-dependent enzyme associated with the inner mitochondrial membrane. 4,6-dinitro-o-cresol 53-59 proline dehydrogenase 1 Homo sapiens 39-48 27446119-2 2016 Arabidopsis cryptochromes (cry1 and cry2) absorb light through an oxidized flavin (FADox) cofactor which undergoes reduction to both FADH and FADH(-) redox states. 4,6-dinitro-o-cresol 75-81 cryptochrome 1 Arabidopsis thaliana 27-31 27273875-6 2016 This loss in activity may be rationalized in terms of one model for the mechanism of action of artemisinins, namely the cofactor model, wherein the presence of a leaving group at C10 assists in driving hydride transfer from reduced flavin cofactors to the peroxide during perturbation of intracellular redox homeostasis by artemisinins. 4,6-dinitro-o-cresol 232-238 homeobox C10 Homo sapiens 179-182 27271694-6 2016 In the frame of the hypothesis that FADS, acting as a "FAD chaperone", could play a crucial role in the biogenesis of mitochondrial flavo-proteome, several basic functional aspects of flavin cofactor delivery to cognate apo-flavoenzyme are also briefly dealt with. 4,6-dinitro-o-cresol 184-190 flavin adenine dinucleotide synthetase 1 Homo sapiens 36-40 27446119-2 2016 Arabidopsis cryptochromes (cry1 and cry2) absorb light through an oxidized flavin (FADox) cofactor which undergoes reduction to both FADH and FADH(-) redox states. 4,6-dinitro-o-cresol 75-81 cryptochrome 2 Arabidopsis thaliana 36-40 27446119-5 2016 Our model fits the experimental data for flavin photoconversion in vitro for both cry1 and cry2, providing calculated quantum yields which are significantly lower in cry1 than for cry2. 4,6-dinitro-o-cresol 41-47 cryptochrome 1 Arabidopsis thaliana 82-86 27446119-5 2016 Our model fits the experimental data for flavin photoconversion in vitro for both cry1 and cry2, providing calculated quantum yields which are significantly lower in cry1 than for cry2. 4,6-dinitro-o-cresol 41-47 cryptochrome 2 Arabidopsis thaliana 91-95 27446119-5 2016 Our model fits the experimental data for flavin photoconversion in vitro for both cry1 and cry2, providing calculated quantum yields which are significantly lower in cry1 than for cry2. 4,6-dinitro-o-cresol 41-47 cryptochrome 1 Arabidopsis thaliana 166-170 27446119-5 2016 Our model fits the experimental data for flavin photoconversion in vitro for both cry1 and cry2, providing calculated quantum yields which are significantly lower in cry1 than for cry2. 4,6-dinitro-o-cresol 41-47 cryptochrome 2 Arabidopsis thaliana 180-184 27446119-7 2016 The fit to the in vivo data provided quantum yields for cry1 and cry2 flavin reduction similar to those obtained in vitro, with decreased cry1 quantum yield as compared to cry2. 4,6-dinitro-o-cresol 70-76 cryptochrome 2 Arabidopsis thaliana 65-69 27337104-2 2016 Lysine demethylation, as catalysed by two families of lysine demethylases (the flavin-dependent KDM1 enzymes and the 2-oxoglutarate- and oxygen-dependent JmjC KDMs, respectively), proceeds via oxidation of the N-methyl group, resulting in the release of formaldehyde. 4,6-dinitro-o-cresol 79-85 lysine demethylase 1A Homo sapiens 96-100 27243969-2 2016 The studied flavin compounds were disubstituted with polar substituents at the N1 and N3 positions (alloxazine) or at the N3 and N10 positions (isoalloxazines). 4,6-dinitro-o-cresol 12-18 nuclear receptor subfamily 4 group A member 1 Homo sapiens 129-132 27020113-8 2016 For Arabidopsis thaliana cryptochrome 1 (AtCry1) we find that spin relaxation implies optimal radical pair lifetimes of the order of microseconds, and that flavin-Z pairs are less affected by relaxation than flavin-tryptophan pairs. 4,6-dinitro-o-cresol 156-162 cryptochrome 1 Arabidopsis thaliana 41-47 27213223-2 2016 In this study, we investigated the ET reaction of the flavin-dependent enzyme fructose dehydrogenase (FDH) with the redox protein cytochrome c (cyt c). 4,6-dinitro-o-cresol 54-60 alcohol dehydrogenase 5 (class III), chi polypeptide Homo sapiens 102-105 27213223-2 2016 In this study, we investigated the ET reaction of the flavin-dependent enzyme fructose dehydrogenase (FDH) with the redox protein cytochrome c (cyt c). 4,6-dinitro-o-cresol 54-60 cytochrome c, somatic Homo sapiens 130-142 27213223-2 2016 In this study, we investigated the ET reaction of the flavin-dependent enzyme fructose dehydrogenase (FDH) with the redox protein cytochrome c (cyt c). 4,6-dinitro-o-cresol 54-60 cytochrome c, somatic Homo sapiens 144-149 27214228-1 2016 Many microorganisms use flavin-dependent thymidylate synthase (FDTS) to synthesize the essential nucleotide 2"-deoxythymidine 5"-monophosphate (dTMP) from 2"-deoxyuridine 5"-monophosphate (dUMP), 5,10-methylenetetrahydrofolate (CH2THF), and NADPH. 4,6-dinitro-o-cresol 24-30 thymidylate synthetase Homo sapiens 41-61 26427470-4 2016 Here we present a brief overview of flavins in the retina and initial findings that suggest retbindin may be located in the photoreceptor layer where flavin acquisition from the RPE would occur. 4,6-dinitro-o-cresol 36-42 retbindin Homo sapiens 92-101 27003727-4 2016 For IDI-2 from the pathogenic bacterium Streptococcus pneumoniae, the flavin can be treated kinetically as a dissociable cosubstrate in incubations with IPP and excess NADH. 4,6-dinitro-o-cresol 70-76 isopentenyl-diphosphate delta isomerase 2 Homo sapiens 4-9 27003727-10 2016 Dithionite reduction of FMN in the IDI-2 FMN and IPP mixture was biphasic with k(red)(IDI-2 FMN IPP (fast)) = 326 s(-1) and k(red)(IDI-2 FMN IPP (slow)) = 6.9 s(-1) The pseudo-first-order rate constant for the slow component was similar to those for NADH reduction of the flavin in the IDI-2 FMN and IPP mixture and may reflect a rate-limiting conformational change in the enzyme. 4,6-dinitro-o-cresol 272-278 isopentenyl-diphosphate delta isomerase 2 Homo sapiens 35-40 26923072-5 2016 The electron flow from NADPH to Flavin, and finally to the heme of the paired nNOS subunit within a dimer, is facilitated upon calmodulin (CaM) binding. 4,6-dinitro-o-cresol 32-38 nitric oxide synthase 1 Homo sapiens 78-82 26840722-0 2016 Spin Densities in Flavin Analogs within a Flavoprotein. 4,6-dinitro-o-cresol 18-24 spindlin 1 Homo sapiens 0-4 27010708-3 2016 Recently, we demonstrated that the rate-limiting step of MAO B catalyzed conversion of amines into imines represents the hydride anion transfer from the substrate alpha-CH2 group to the N5 atom of the flavin cofactor moiety. 4,6-dinitro-o-cresol 201-207 monoamine oxidase B Homo sapiens 57-62 26385068-1 2015 In the photosynthetic electron transfer (ET) chain, two electrons transfer from photosystem I to the flavin-dependent ferredoxin-NADP(+) reductase (FNR) via two sequential independent ferredoxin (Fd) electron carriers. 4,6-dinitro-o-cresol 101-107 Ferredoxin--NADP reductase, embryo isozyme, chloroplastic-like Zea mays 118-146 26726739-10 2016 We identified a selective, cell-compatible photo-oxygenation catalyst of Abeta, a flavin catalyst attached to an Abeta-binding peptide, which markedly decreased the aggregation potency and neurotoxicity of Abeta. 4,6-dinitro-o-cresol 82-88 amyloid beta precursor protein Homo sapiens 73-78 27527619-1 2016 Riboflavin, or vitamin B2, plays an important role in the cell as biological precursor of FAD and FMN, two important flavin cofactors which are essential for the structure and function of flavoproteins. 4,6-dinitro-o-cresol 4-10 formin 1 Homo sapiens 98-101 26634408-2 2015 The SsuE enzyme is an NADPH-dependent FMN reductase that provides reduced flavin to the SsuD monooxygenase enzyme. 4,6-dinitro-o-cresol 74-80 formin 1 Homo sapiens 38-41 26385068-1 2015 In the photosynthetic electron transfer (ET) chain, two electrons transfer from photosystem I to the flavin-dependent ferredoxin-NADP(+) reductase (FNR) via two sequential independent ferredoxin (Fd) electron carriers. 4,6-dinitro-o-cresol 101-107 Ferredoxin--NADP reductase, embryo isozyme, chloroplastic-like Zea mays 148-151 25755053-7 2015 Spectral changes during inactivation of MAO A included bleaching at 456 nm and an increased absorbance at 400 nm, consistent with flavin modification. 4,6-dinitro-o-cresol 130-136 monoamine oxidase A Homo sapiens 40-45 26649273-5 2015 This in vitro study extends earlier investigations of the oxidation of Arabidopsis cryptochrome1 by molecular oxygen and demonstrates that, under some conditions, a more complex model for oxidation of the flavin than was previously proposed is required to accommodate the spectral evidence (see P. Muller and M. Ahmad (2011) J. Biol. 4,6-dinitro-o-cresol 205-211 cryptochrome 1 Arabidopsis thaliana 83-96 26496755-4 2015 Moreover, sgRNA targeting flavin containing monooxygenases3 (Fmo3) gene and the corresponding single strand oligonucleotides (ssODN) donor template with point mutation were co-injected into the male pronucleus of one-cell mouse embryos stimulated HR-mediated repair mechanism. 4,6-dinitro-o-cresol 26-32 flavin containing dimethylaniline monoxygenase 3 Homo sapiens 61-65 26237213-3 2015 Upon reduction by NADH, hAIF dimerizes and produces very stable flavin/nicotinamide charge transfer complexes (CTC), by stacking of the oxidized nicotinamide moiety of the NAD(+) coenzyme against the re-face of the reduced flavin ring of its FAD cofactor. 4,6-dinitro-o-cresol 64-70 apoptosis inducing factor mitochondria associated 1 Homo sapiens 24-28 26237213-3 2015 Upon reduction by NADH, hAIF dimerizes and produces very stable flavin/nicotinamide charge transfer complexes (CTC), by stacking of the oxidized nicotinamide moiety of the NAD(+) coenzyme against the re-face of the reduced flavin ring of its FAD cofactor. 4,6-dinitro-o-cresol 223-229 apoptosis inducing factor mitochondria associated 1 Homo sapiens 24-28 26237213-7 2015 Characterization of P173G hAIF indicates that the stacking of P173 against the isoalloxazine ring is relevant to determine the flavin environment and to modulate the enzyme affinity for NADH. 4,6-dinitro-o-cresol 127-133 apoptosis inducing factor mitochondria associated 1 Homo sapiens 26-30 26237213-7 2015 Characterization of P173G hAIF indicates that the stacking of P173 against the isoalloxazine ring is relevant to determine the flavin environment and to modulate the enzyme affinity for NADH. 4,6-dinitro-o-cresol 127-133 NADH:ubiquinone oxidoreductase subunit B11 Homo sapiens 20-24 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 26151430-4 2015 Time-dependent quenching of flavin fluorescence was used to monitor halotyrosine association to IYD. 4,6-dinitro-o-cresol 28-34 iodotyrosine deiodinase Homo sapiens 96-99 25820384-6 2015 After internalization and lysosomal release, Cbl binds to the cytosolic chaperon MMACHC that is responsible for (i) flavin-dependent decyanation of [CN-Co(3+) Cbl to [Co(2+)]Cbl; (ii) glutathione-dependent dealkylation of MeCbl and AdoCbl to [Co(2+/1+)]Cbl; and (iii) glutathione-dependent decyanation of CNCbl or reduction of HOCbl under anaerobic conditions. 4,6-dinitro-o-cresol 116-122 Cbl proto-oncogene Homo sapiens 45-48 25820384-6 2015 After internalization and lysosomal release, Cbl binds to the cytosolic chaperon MMACHC that is responsible for (i) flavin-dependent decyanation of [CN-Co(3+) Cbl to [Co(2+)]Cbl; (ii) glutathione-dependent dealkylation of MeCbl and AdoCbl to [Co(2+/1+)]Cbl; and (iii) glutathione-dependent decyanation of CNCbl or reduction of HOCbl under anaerobic conditions. 4,6-dinitro-o-cresol 116-122 metabolism of cobalamin associated C Homo sapiens 81-87 25820384-6 2015 After internalization and lysosomal release, Cbl binds to the cytosolic chaperon MMACHC that is responsible for (i) flavin-dependent decyanation of [CN-Co(3+) Cbl to [Co(2+)]Cbl; (ii) glutathione-dependent dealkylation of MeCbl and AdoCbl to [Co(2+/1+)]Cbl; and (iii) glutathione-dependent decyanation of CNCbl or reduction of HOCbl under anaerobic conditions. 4,6-dinitro-o-cresol 116-122 Cbl proto-oncogene Homo sapiens 159-162 25820384-6 2015 After internalization and lysosomal release, Cbl binds to the cytosolic chaperon MMACHC that is responsible for (i) flavin-dependent decyanation of [CN-Co(3+) Cbl to [Co(2+)]Cbl; (ii) glutathione-dependent dealkylation of MeCbl and AdoCbl to [Co(2+/1+)]Cbl; and (iii) glutathione-dependent decyanation of CNCbl or reduction of HOCbl under anaerobic conditions. 4,6-dinitro-o-cresol 116-122 Cbl proto-oncogene Homo sapiens 159-162 25820384-6 2015 After internalization and lysosomal release, Cbl binds to the cytosolic chaperon MMACHC that is responsible for (i) flavin-dependent decyanation of [CN-Co(3+) Cbl to [Co(2+)]Cbl; (ii) glutathione-dependent dealkylation of MeCbl and AdoCbl to [Co(2+/1+)]Cbl; and (iii) glutathione-dependent decyanation of CNCbl or reduction of HOCbl under anaerobic conditions. 4,6-dinitro-o-cresol 116-122 Cbl proto-oncogene Homo sapiens 159-162 25822458-7 2015 Moreover, such CaM-free iNOS has similar flavin content and reductase activity as iNOS co-expressed with CaM, suggesting that CaM may not be as much required for the functional assembly of the iNOS reductase domain as its oxygenase domain. 4,6-dinitro-o-cresol 41-47 calmodulin 2 Mus musculus 15-18 25822458-7 2015 Moreover, such CaM-free iNOS has similar flavin content and reductase activity as iNOS co-expressed with CaM, suggesting that CaM may not be as much required for the functional assembly of the iNOS reductase domain as its oxygenase domain. 4,6-dinitro-o-cresol 41-47 nitric oxide synthase 2, inducible Mus musculus 24-28 26083754-3 2015 Here we show that Fdc1 is solely responsible for the reversible decarboxylase activity, and that it requires a new type of cofactor: a prenylated flavin synthesized by the associated UbiX/Pad1. 4,6-dinitro-o-cresol 146-152 peptidyl arginine deiminase 1 Homo sapiens 188-192 25728647-5 2015 Externally added flavin partially restored the cytochrome c reductase activity of A287P, suggesting that flavin therapy may be useful for this frequent form of PORD. 4,6-dinitro-o-cresol 17-23 cytochrome c, somatic Homo sapiens 47-59 25728647-5 2015 Externally added flavin partially restored the cytochrome c reductase activity of A287P, suggesting that flavin therapy may be useful for this frequent form of PORD. 4,6-dinitro-o-cresol 105-111 cytochrome c, somatic Homo sapiens 47-59 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 26039487-4 2015 Proteins of the flavin-binding KELCH repeat F-box 1 / LOV KELCH protein 2 / ZEITLUPE family are positive regulators of hypocotyl elongation under red light in Arabidopsis. 4,6-dinitro-o-cresol 16-22 LOV KELCH protein 2 Arabidopsis thaliana 54-73 25531177-17 2015 The pure preparations of these molecules induce rapid reduction of the renalase flavin cofactor (230 s(-1) for 6-dihydroNAD, 850 s(-1) for 2-dihydroNAD) but bind only a few fold more tightly than beta-NADH. 4,6-dinitro-o-cresol 80-86 renalase, FAD dependent amine oxidase Homo sapiens 71-79 25470783-0 2015 LED-illuminated NMR studies of flavin-catalyzed photooxidations reveal solvent control of the electron-transfer mechanism. 4,6-dinitro-o-cresol 31-37 small integral membrane protein 10 like 2A Homo sapiens 0-3 26313597-2 2015 In plants, cryptochrome (cry1, cry2) biological activity has been linked to flavin photoreduction via an electron transport chain to the protein surface comprising 3 evolutionarily conserved tryptophan residues known as the "Trp triad." 4,6-dinitro-o-cresol 76-82 cryptochrome 1 Arabidopsis thaliana 25-29 26313597-2 2015 In plants, cryptochrome (cry1, cry2) biological activity has been linked to flavin photoreduction via an electron transport chain to the protein surface comprising 3 evolutionarily conserved tryptophan residues known as the "Trp triad." 4,6-dinitro-o-cresol 76-82 cryptochrome 2 Arabidopsis thaliana 31-35 26313597-4 2015 However, photoreduction of the flavin in Arabidopsis cry2 proteins occurs in vivo even with mutations in the Trp triad, indicating the existence of alternative electron transfer pathways to the flavin. 4,6-dinitro-o-cresol 31-37 cryptochrome 2 Arabidopsis thaliana 53-57 26039487-4 2015 Proteins of the flavin-binding KELCH repeat F-box 1 / LOV KELCH protein 2 / ZEITLUPE family are positive regulators of hypocotyl elongation under red light in Arabidopsis. 4,6-dinitro-o-cresol 16-22 Galactose oxidase/kelch repeat superfamily protein Arabidopsis thaliana 76-84 26313597-4 2015 However, photoreduction of the flavin in Arabidopsis cry2 proteins occurs in vivo even with mutations in the Trp triad, indicating the existence of alternative electron transfer pathways to the flavin. 4,6-dinitro-o-cresol 194-200 cryptochrome 2 Arabidopsis thaliana 53-57 25220264-2 2014 In this work, we present a comprehensive study of the rate-limiting step of dopamine degradation by MAO B, which consists in the hydride transfer from the methylene group of the substrate to the flavin moiety of the FAD prosthetic group. 4,6-dinitro-o-cresol 195-201 monoamine oxidase B Homo sapiens 100-105 24859458-2 2014 In humans, N(epsilon)-methyllysine residue demethylation is catalysed by two distinct subfamilies of demethylases (KDMs), the flavin-dependent KDM1 subfamily and the 2-oxoglutarate- (2OG) dependent JmjC subfamily, which both employ oxidative mechanisms. 4,6-dinitro-o-cresol 126-132 lysine demethylase 1A Homo sapiens 143-147 25220264-4 2014 We show that MAO B is specifically tuned to catalyze the hydride transfer step from the substrate to the flavin moiety of the FAD prosthetic group and that it lowers the activation barrier by 12.3 kcal mol-1 compared to the same reaction in aqueous solution, a rate enhancement of more than nine orders of magnitude. 4,6-dinitro-o-cresol 105-111 monoamine oxidase B Homo sapiens 13-18 25283388-3 2014 Photoinduced electron transfer (ET) in 2-H2 occurred from the singlet excited state of the porphyrin moiety (H2 Por) to the flavin (Fl) moiety to produce the singlet charge-separated (CS) state (1) (H2 Por(.+) -Fl(.-) ), which decayed through back ET (BET) to form (3) [H2 Por]*-Fl with rate constants of 1.2x10(10) and 1.2x10(9) s(-1) , respectively. 4,6-dinitro-o-cresol 124-130 delta/notch like EGF repeat containing Homo sapiens 252-255 25428980-2 2014 Plant cryptochrome (cry1 and cry2) biological activity has been linked to flavin photoreduction via an electron transport chain comprising three evolutionarily conserved tryptophan residues known as the Trp triad. 4,6-dinitro-o-cresol 74-80 cryptochrome 1 Arabidopsis thaliana 20-24 25173759-0 2014 Role of Mg2+ ions in flavin recognition by RNA aptamer. 4,6-dinitro-o-cresol 21-27 mucin 7, secreted Homo sapiens 8-11 25428980-2 2014 Plant cryptochrome (cry1 and cry2) biological activity has been linked to flavin photoreduction via an electron transport chain comprising three evolutionarily conserved tryptophan residues known as the Trp triad. 4,6-dinitro-o-cresol 74-80 cryptochrome 2 Arabidopsis thaliana 29-33 25045844-3 2014 Knockdown of RFT2 in ESCC cells resulted in decreases of intracellular flavin status, mitochondrial membrane potential and cellular ATP levels, and inhibitions of cell proliferation, colony formation and anchorage-independent growth. 4,6-dinitro-o-cresol 71-77 solute carrier family 52 member 3 Homo sapiens 13-17 25194416-2 2014 Both FAD and FMN flavin groups mediate the transfer of NADPH derived electrons to NOS. 4,6-dinitro-o-cresol 17-23 formin 1 Homo sapiens 13-16 25101006-1 2014 BACKGROUND AND AIMS: AIF (apoptosis inducing factor) is a flavin and NADH containing protein located within mitochondria required for optimal function of the respiratory chain. 4,6-dinitro-o-cresol 58-64 apoptosis-inducing factor, mitochondrion-associated 1 Mus musculus 21-24 25361953-7 2014 Among these promoters, that of FLAVIN BINDING KELCH REPEAT F-BOX1 was analyzed in detail and shown to harbor a CRM functionally related to GI CRM2. 4,6-dinitro-o-cresol 31-37 flavin-binding, kelch repeat, f box 1 Arabidopsis thaliana 59-65 25361953-7 2014 Among these promoters, that of FLAVIN BINDING KELCH REPEAT F-BOX1 was analyzed in detail and shown to harbor a CRM functionally related to GI CRM2. 4,6-dinitro-o-cresol 31-37 double-stranded RNA binding protein-related / DsRBD protein-like protein Arabidopsis thaliana 142-146 24944315-2 2014 Flavin and colleagues report that SPINK1 is neither prognostic nor absolutely mutually exclusive with ERG, raising important questions about prostate cancer molecular subtyping and prognostic biomarker evaluation. 4,6-dinitro-o-cresol 0-6 serine peptidase inhibitor Kazal type 1 Homo sapiens 34-40 25201173-8 2014 By contrast, the expression of FT and photoperiod genes in leaves and the expression of FD and AP1 in the shoot apex were no longer enhanced when the RfBP gene was silenced, RfBP protein production canceled, and flavin concentrations were elevated to the steady-state levels inside plant leaves. 4,6-dinitro-o-cresol 212-218 K-box region and MADS-box transcription factor family protein Arabidopsis thaliana 95-98 24676540-3 2014 It is postulated that GO layers decrease the distance between the flavin cofactor (FAD/FADH2) of the glucose oxidase enzyme (GOx) and the electrode surface, though experimental evidence concerning the distance dependence of the rate constant for heterogeneous electron-transfer (k(het)) has not yet been observed. 4,6-dinitro-o-cresol 66-72 hydroxyacid oxidase 1 Homo sapiens 101-123 24676540-3 2014 It is postulated that GO layers decrease the distance between the flavin cofactor (FAD/FADH2) of the glucose oxidase enzyme (GOx) and the electrode surface, though experimental evidence concerning the distance dependence of the rate constant for heterogeneous electron-transfer (k(het)) has not yet been observed. 4,6-dinitro-o-cresol 66-72 hydroxyacid oxidase 1 Homo sapiens 125-128 24582598-8 2014 These data show the robustness of the ALR protein fold towards the multiple mutations required to insert the SECIS element and provide the first example of a selenolate to flavin charge-transfer complex. 4,6-dinitro-o-cresol 172-178 growth factor, augmenter of liver regeneration Homo sapiens 38-41 24858690-2 2014 DMGDH is a flavin containing enzyme which catalyzes the oxidative demethylation of dimethylglycine in vitro with the formation of sarcosine (N-methylglycine), hydrogen peroxide and formaldehyde. 4,6-dinitro-o-cresol 11-17 dimethylglycine dehydrogenase Rattus norvegicus 0-5 24715612-2 2014 The first histone demethylase to be discovered was a lysine-specific demethylase 1, LSD1, a flavin containing enzyme which carries out the demethylation of di- and monomethyllysine 4 in histone H3. 4,6-dinitro-o-cresol 92-98 lysine demethylase 1A Homo sapiens 84-88 24742678-3 2014 Human CblC exhibits glutathione (GSH)-dependent alkyltransferase activity and flavin-dependent reductive decyanation activity with cyanocobalamin (CNCbl). 4,6-dinitro-o-cresol 78-84 Cbl proto-oncogene C Homo sapiens 6-10 23907989-1 2013 Sulfide:quinone oxidoreductase (SQR) is a flavin-dependent enzyme that plays a physiological role in two important processes. 4,6-dinitro-o-cresol 42-48 crystallin zeta Homo sapiens 8-30 24339209-5 2014 Photooxygenation of Abeta can be performed even in the presence of cells, by using a selective flavin catalyst attached to an Abeta-binding peptide; the Abeta cytotoxicity was attenuated in this case as well. 4,6-dinitro-o-cresol 95-101 amyloid beta precursor protein Homo sapiens 20-25 24339209-5 2014 Photooxygenation of Abeta can be performed even in the presence of cells, by using a selective flavin catalyst attached to an Abeta-binding peptide; the Abeta cytotoxicity was attenuated in this case as well. 4,6-dinitro-o-cresol 95-101 amyloid beta precursor protein Homo sapiens 126-131 24339209-5 2014 Photooxygenation of Abeta can be performed even in the presence of cells, by using a selective flavin catalyst attached to an Abeta-binding peptide; the Abeta cytotoxicity was attenuated in this case as well. 4,6-dinitro-o-cresol 95-101 amyloid beta precursor protein Homo sapiens 126-131 23999537-4 2014 Enzyme activity measurements and hydrogen peroxide production studies by Amplex Red fluorescence, and luminol luminescence in combination with oxygraphy revealed flavin as the most likely source of electron leak in SDH under in vivo conditions, while we propose coenzyme Q as the site of ROS production in the case of mGPDH. 4,6-dinitro-o-cresol 162-168 succinate dehydrogenase complex iron sulfur subunit B Homo sapiens 215-218 23999537-4 2014 Enzyme activity measurements and hydrogen peroxide production studies by Amplex Red fluorescence, and luminol luminescence in combination with oxygraphy revealed flavin as the most likely source of electron leak in SDH under in vivo conditions, while we propose coenzyme Q as the site of ROS production in the case of mGPDH. 4,6-dinitro-o-cresol 162-168 glycerol phosphate dehydrogenase 2, mitochondrial Mus musculus 318-323 24764101-5 2014 At the end of this guide, we present data taken on non-photobiological flavoproteins, glutathione reductase and lipoamide dehydrogenase, that suggest that Stark spectroscopy is a unique way to elucidate the electrostatic environment that the flavin cofactor experiences bound inside the protein. 4,6-dinitro-o-cresol 242-248 glutathione-disulfide reductase Homo sapiens 86-107 24764101-5 2014 At the end of this guide, we present data taken on non-photobiological flavoproteins, glutathione reductase and lipoamide dehydrogenase, that suggest that Stark spectroscopy is a unique way to elucidate the electrostatic environment that the flavin cofactor experiences bound inside the protein. 4,6-dinitro-o-cresol 242-248 dihydrolipoamide dehydrogenase Homo sapiens 112-135 24473192-4 2014 The electrons liberated in this process are delivered to an oxidoreductase by simple flavin redox mediators. 4,6-dinitro-o-cresol 85-91 thioredoxin reductase 1 Homo sapiens 60-74 24297896-7 2013 The oscillator protein Timeless (TIM) contains a sequence similar to the CTT; the corresponding peptide binds dCRY in light and protects the flavin from oxidation. 4,6-dinitro-o-cresol 141-147 timeless Drosophila melanogaster 23-31 24297896-7 2013 The oscillator protein Timeless (TIM) contains a sequence similar to the CTT; the corresponding peptide binds dCRY in light and protects the flavin from oxidation. 4,6-dinitro-o-cresol 141-147 timeless Drosophila melanogaster 33-36 24100037-7 2013 Using a novel imaging modality for monitoring mitochondrial flavin fluorescence in mouse islets, we show that slow oscillations in mitochondrial redox potential stimulated by 10 mm glucose are in phase with glycolytic efflux through PKM2, measured simultaneously from neighboring islet beta-cells expressing PKAR. 4,6-dinitro-o-cresol 60-66 pyruvate kinase, muscle Mus musculus 233-237 24681944-4 2014 Spin-radical pair products are modulated by the 7 MHz RF magnetic fields that presumably decouple flavin hyperfine interactions during spin coherence. 4,6-dinitro-o-cresol 98-104 spindlin 1 Rattus norvegicus 0-4 24681944-4 2014 Spin-radical pair products are modulated by the 7 MHz RF magnetic fields that presumably decouple flavin hyperfine interactions during spin coherence. 4,6-dinitro-o-cresol 98-104 spindlin 1 Rattus norvegicus 135-139 23754593-1 2014 Flavocytochrome P450BM-3 is a soluble bacterial reductase composed of two flavin (FAD/FMN) and one HEME domains. 4,6-dinitro-o-cresol 74-80 formin 1 Homo sapiens 86-89 24368083-2 2014 Here, the reaction of reduced flavin and dioxygen catalyzed by pyranose 2-oxidase (P2O), a flavoenzyme oxidase that is unique in its formation of C4a-hydroperoxyflavin, was investigated by density functional calculations, transient kinetics, and site-directed mutagenesis. 4,6-dinitro-o-cresol 30-36 complement C4A (Rodgers blood group) Homo sapiens 146-149 24368083-3 2014 Based on work from the 1970s-1980s, the current understanding of the dioxygen activation process in flavoenzymes is believed to involve electron transfer from flavin to dioxygen and subsequent proton transfer to form C4a-hydroperoxyflavin. 4,6-dinitro-o-cresol 159-165 complement C4A (Rodgers blood group) Homo sapiens 217-220 24368083-7 2014 Furthermore, the C4a-hydroperoxyflavin is stabilized by the side chains of Thr169, His548, and Asn593 in a "face-on" configuration where it can undergo a unimolecular reaction to generate H2O2 and oxidized flavin. 4,6-dinitro-o-cresol 32-38 complement C4A (Rodgers blood group) Homo sapiens 17-20 23964689-5 2013 We have identified the catalytic activity of renalase as an alpha-NAD(P)H oxidase/anomerase, whereby low equilibrium concentrations of the alpha-anomer of NADPH and NADH initiate rapid reduction of the renalase flavin cofactor. 4,6-dinitro-o-cresol 211-217 renalase, FAD dependent amine oxidase Homo sapiens 45-53 23964689-5 2013 We have identified the catalytic activity of renalase as an alpha-NAD(P)H oxidase/anomerase, whereby low equilibrium concentrations of the alpha-anomer of NADPH and NADH initiate rapid reduction of the renalase flavin cofactor. 4,6-dinitro-o-cresol 211-217 renalase, FAD dependent amine oxidase Homo sapiens 60-91 23964689-5 2013 We have identified the catalytic activity of renalase as an alpha-NAD(P)H oxidase/anomerase, whereby low equilibrium concentrations of the alpha-anomer of NADPH and NADH initiate rapid reduction of the renalase flavin cofactor. 4,6-dinitro-o-cresol 211-217 renalase, FAD dependent amine oxidase Homo sapiens 202-210 23733181-0 2013 The crystal structure of six-transmembrane epithelial antigen of the prostate 4 (Steap4), a ferri/cuprireductase, suggests a novel interdomain flavin-binding site. 4,6-dinitro-o-cresol 143-149 STEAP4 metalloreductase Homo sapiens 81-87 23728815-0 2013 Fusion of a flavin-based fluorescent protein to hydroxynitrile lyase from Arabidopsis thaliana improves enzyme stability. 4,6-dinitro-o-cresol 12-18 methyl esterase 5 Arabidopsis thaliana 48-68 23927065-9 2013 The separate monooxygenase domain of MICAL-2 has the classic regulatory behavior of flavin-dependent aromatic hydroxylases (Class A monooxygenases): slow reduction of the flavin when the substrate to be oxygenated is absent. 4,6-dinitro-o-cresol 84-90 microtubule associated monooxygenase, calponin and LIM domain containing 2 Homo sapiens 37-44 23733181-7 2013 Structure-function work also suggested Steap4 utilizes an interdomain flavin-binding site to shuttle electrons between the oxidoreductase and transmembrane domains, and it showed that the disordered N-terminal residues do not contribute to enzymatic activity. 4,6-dinitro-o-cresol 70-76 STEAP4 metalloreductase Homo sapiens 39-45 23754812-8 2013 Purified AtTAH18 bound one flavin per molecule and was able to accept electrons from NAD(P)H. 4,6-dinitro-o-cresol 27-33 Flavodoxin family protein Arabidopsis thaliana 9-16 23485585-4 2013 Site-directed variants of TrxR1 demonstrate that the selenocysteine (Sec) of the enzyme is not required, whereas the C59 residue and the flavin have important roles. 4,6-dinitro-o-cresol 137-143 thioredoxin reductase 1 Homo sapiens 26-31 23485585-5 2013 Although TrxR1 and GR have analogous C59/flavin motifs, TrxR is considerably faster than GR. 4,6-dinitro-o-cresol 41-47 glutathione-disulfide reductase Homo sapiens 19-21 22833674-1 2012 NADPH-dependent thioredoxin reductases (NTRs) contain a flavin cofactor and a disulfide as redox-active groups. 4,6-dinitro-o-cresol 56-62 thioredoxin Homo sapiens 16-27 23507581-2 2013 NOSs are flavo-hemo proteins, with two flavin molecules (FAD and FMN) and one heme per monomer, which require the binding of calcium/calmodulin (Ca(2+)/CaM) to produce NO. 4,6-dinitro-o-cresol 39-45 calmodulin 1 Homo sapiens 133-143 23507581-2 2013 NOSs are flavo-hemo proteins, with two flavin molecules (FAD and FMN) and one heme per monomer, which require the binding of calcium/calmodulin (Ca(2+)/CaM) to produce NO. 4,6-dinitro-o-cresol 39-45 calmodulin 1 Homo sapiens 152-155 23246553-1 2013 Apoptosis-inducing factor (AIF) is a flavin-binding mitochondrial intermembrane space protein that is implicated in diverse but intertwined processes that include maintenance of electron transport chain function, reactive oxygen species regulation, cell death, and neurodegeneration. 4,6-dinitro-o-cresol 37-43 apoptosis-inducing factor, mitochondrion-associated 1 Mus musculus 0-25 23246553-1 2013 Apoptosis-inducing factor (AIF) is a flavin-binding mitochondrial intermembrane space protein that is implicated in diverse but intertwined processes that include maintenance of electron transport chain function, reactive oxygen species regulation, cell death, and neurodegeneration. 4,6-dinitro-o-cresol 37-43 apoptosis-inducing factor, mitochondrion-associated 1 Mus musculus 27-30 23312283-3 2013 We demonstrate that two flavin mono-oxygenase family members, FMO1 and FMO3, oxidize trimethylamine (TMA), derived from gut flora metabolism of choline, to TMAO. 4,6-dinitro-o-cresol 24-30 flavin containing monooxygenase 1 Mus musculus 62-66 23312283-3 2013 We demonstrate that two flavin mono-oxygenase family members, FMO1 and FMO3, oxidize trimethylamine (TMA), derived from gut flora metabolism of choline, to TMAO. 4,6-dinitro-o-cresol 24-30 flavin containing monooxygenase 3 Mus musculus 71-75 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 22483692-9 2012 SIGNIFICANCE: ET-1 increases O(2)(-) production especially in human arteries and less so in veins from patients with coronary artery disease via a receptor-dependent pathway involving a flavin dependent enzyme which is likely to be NADPH oxidase. 4,6-dinitro-o-cresol 186-192 endothelin 1 Homo sapiens 14-18 23155486-2 2012 Representatives of the alternative flavin-dependent thymidylate synthase family, ThyX, are found in a large number of microbial genomes, but are absent in humans. 4,6-dinitro-o-cresol 35-41 thymidylate synthetase Homo sapiens 52-72 23621882-5 2013 The amino group of the dTDP-aminosugar that is oxidized is located 4.9 A from C4a of the flavin ring. 4,6-dinitro-o-cresol 89-95 TAR DNA-binding protein-43 homolog Drosophila melanogaster 23-27 23471972-0 2013 Chloroquine binding reveals flavin redox switch function of quinone reductase 2. 4,6-dinitro-o-cresol 28-34 N-ribosyldihydronicotinamide:quinone reductase 2 Homo sapiens 60-79 23471972-6 2013 This first structure of a reduced quinone reductase shows that reduction of the FAD cofactor and binding of a specific inhibitor lead to global changes in NQO2 structure and is consistent with a functional role for NQO2 as a flavin redox switch. 4,6-dinitro-o-cresol 225-231 N-ribosyldihydronicotinamide:quinone reductase 2 Homo sapiens 155-159 23471972-6 2013 This first structure of a reduced quinone reductase shows that reduction of the FAD cofactor and binding of a specific inhibitor lead to global changes in NQO2 structure and is consistent with a functional role for NQO2 as a flavin redox switch. 4,6-dinitro-o-cresol 225-231 N-ribosyldihydronicotinamide:quinone reductase 2 Homo sapiens 215-219 23116399-3 2013 In the current review, we discuss the merits in targeting the enzyme dihydroorotate dehydrogenase (DHODH), a flavin-dependent enzyme that catalyzes the fourth and only redox step in pyrimidine de novo biosynthesis, as a strategy for the development of efficient therapeutic strategies for trypanosomatid-related diseases.We also describe the advances and perspectives from the structural biology point of view in order to unravel the structure-function relationship of trypanosomatid DHODHs, and to identify and validate target sites for drug development. 4,6-dinitro-o-cresol 109-115 dihydroorotate dehydrogenase (quinone) Homo sapiens 69-97 23116399-3 2013 In the current review, we discuss the merits in targeting the enzyme dihydroorotate dehydrogenase (DHODH), a flavin-dependent enzyme that catalyzes the fourth and only redox step in pyrimidine de novo biosynthesis, as a strategy for the development of efficient therapeutic strategies for trypanosomatid-related diseases.We also describe the advances and perspectives from the structural biology point of view in order to unravel the structure-function relationship of trypanosomatid DHODHs, and to identify and validate target sites for drug development. 4,6-dinitro-o-cresol 109-115 dihydroorotate dehydrogenase (quinone) Homo sapiens 99-104 23116400-6 2013 Upon reduction of the flavin cofactor by NADH, conformational changes leading to AIF dimerization are proposed as a key early event in the mitochondrial sensing/signaling functions of AIF. 4,6-dinitro-o-cresol 22-28 apoptosis inducing factor mitochondria associated 1 Homo sapiens 81-84 23116400-6 2013 Upon reduction of the flavin cofactor by NADH, conformational changes leading to AIF dimerization are proposed as a key early event in the mitochondrial sensing/signaling functions of AIF. 4,6-dinitro-o-cresol 22-28 apoptosis inducing factor mitochondria associated 1 Homo sapiens 184-187 22642831-8 2012 The pH profiles for the rate constant for flavin reduction for all the mutant enzymes similarly show the same pK(a) as wild-type Fms1, about ~7.4; this pK(a) is assigned to the substrate N4. 4,6-dinitro-o-cresol 42-48 polyamine oxidase Saccharomyces cerevisiae S288C 129-133 22580358-0 2012 Mutations at the flavin binding site of ETF:QO yield a MADD-like severe phenotype in Drosophila. 4,6-dinitro-o-cresol 17-23 Electron transfer flavoprotein-ubiquinone oxidoreductase Drosophila melanogaster 40-46 23019356-0 2012 Folate binding site of flavin-dependent thymidylate synthase. 4,6-dinitro-o-cresol 23-29 thymidylate synthetase Homo sapiens 40-60 22802674-4 2012 NS1 became fluorescent once bound to NOS with an excellent signal-to-noise ratio because of two-photon excitation avoiding interference from the flavin-autofluorescence and because free NS1 was not fluorescent in aqueous solutions. 4,6-dinitro-o-cresol 145-151 influenza virus NS1A binding protein Homo sapiens 0-3 22573324-3 2012 A membrane-extrinsic catalytic domain composed of the Sdh1p and Sdh2p subunits harbors the flavin and iron-sulfur cluster cofactors. 4,6-dinitro-o-cresol 91-97 succinate dehydrogenase flavoprotein subunit SDH1 Saccharomyces cerevisiae S288C 54-59 22573324-3 2012 A membrane-extrinsic catalytic domain composed of the Sdh1p and Sdh2p subunits harbors the flavin and iron-sulfur cluster cofactors. 4,6-dinitro-o-cresol 91-97 succinate dehydrogenase iron-sulfur protein subunit SDH2 Saccharomyces cerevisiae S288C 64-69 22257001-4 2012 Although redox titrations of Cyc2p flavin (E(m) = -290 mV) indicate that reduction of a disulphide at the CXXCH site of apocytochrome c (E(m) = -265 mV) is a thermodynamically favourable reaction, Cyc2p does not act as an apocytochrome c or c(1) CXXCH disulphide reductase in vitro. 4,6-dinitro-o-cresol 35-41 oxidoreductase Saccharomyces cerevisiae S288C 29-34 22415204-4 2012 The interaction of GOx with the chemical denaturant resulted in a disturbance of the structure of the flavin prosthetic group (FAD moiety) that induced the moiety to become less exposed to solvent than that in the native protein molecule. 4,6-dinitro-o-cresol 102-108 hydroxyacid oxidase 1 Homo sapiens 19-22 22505691-0 2012 An Arabidopsis FAD pyrophosphohydrolase, AtNUDX23, is involved in flavin homeostasis. 4,6-dinitro-o-cresol 66-72 nudix hydrolase homolog 23 Arabidopsis thaliana 41-49 22505691-4 2012 The transcript levels of AtNUDX23 as well as genes involved in flavin metabolism (AtFADS, AtRibF1, AtRibF2, AtFMN/FHy, LS and AtRibA) significantly increased under continuous light. 4,6-dinitro-o-cresol 63-69 nudix hydrolase homolog 23 Arabidopsis thaliana 25-33 22505691-9 2012 These results suggest that negative feedback regulation of the metabolism of flavins through the hydrolysis of FAD by AtNUDX23 in plastids is involved in flavin homeostasis in plant cells. 4,6-dinitro-o-cresol 77-83 nudix hydrolase homolog 23 Arabidopsis thaliana 118-126 22803945-1 2012 To determine the nature and characteristic parameters of the myoglobin-mitochondrion interaction during oxymyoglobin (MbO(2)) deoxygenation in the cell, we studied the quenching of the intrinsic mitochondrial flavin and tryptophan fluorescence by different liganded myoglobins in the pH range of 6-8, as well as the quenching of the fluorescence of the membrane probes 1,8-ANS and merocyanine 540 (M 540) embedded into the mitochondrial membrane. 4,6-dinitro-o-cresol 209-215 myoglobin Homo sapiens 61-70 22257001-4 2012 Although redox titrations of Cyc2p flavin (E(m) = -290 mV) indicate that reduction of a disulphide at the CXXCH site of apocytochrome c (E(m) = -265 mV) is a thermodynamically favourable reaction, Cyc2p does not act as an apocytochrome c or c(1) CXXCH disulphide reductase in vitro. 4,6-dinitro-o-cresol 35-41 oxidoreductase Saccharomyces cerevisiae S288C 197-202 22031853-10 2012 Basal and insulin-stimulated surface expression of TRPC6 were reduced by pretreatment with diphenylene iodonium, an inhibitor of NADPH oxidases and other flavin-dependent enzymes, by siRNA knockdown of NOX4, and by manganese (III) tetrakis (4-benzoic acid) porphyrin chloride, a membrane-permeable mimetic of superoxide dismutase and catalase. 4,6-dinitro-o-cresol 154-160 insulin Homo sapiens 10-17 22031853-10 2012 Basal and insulin-stimulated surface expression of TRPC6 were reduced by pretreatment with diphenylene iodonium, an inhibitor of NADPH oxidases and other flavin-dependent enzymes, by siRNA knockdown of NOX4, and by manganese (III) tetrakis (4-benzoic acid) porphyrin chloride, a membrane-permeable mimetic of superoxide dismutase and catalase. 4,6-dinitro-o-cresol 154-160 transient receptor potential cation channel subfamily C member 6 Homo sapiens 51-56 22081402-10 2012 It is proposed that reduced riboflavin synthesis impairs the activity of the flavin-containing cytokinin oxidase, increases cytokinin contents and de-represses synthesis of 5-aminolevulinic acid of tetrapyrrole metabolism in darkness. 4,6-dinitro-o-cresol 32-38 cytokinin oxidase 3 Arabidopsis thaliana 95-112 22145797-5 2012 In XDH (without NAD(+)), however, the redox potential of the electron donor FeS-II is 180 mV higher than that for the acceptor flavin, yielding an energetically uphill ET. 4,6-dinitro-o-cresol 127-133 xanthine dehydrogenase Homo sapiens 3-6 22145797-6 2012 On the basis of new 1.65, 2.3, 1.9, and 2.2 A resolution crystal structures for XDH, XO, the NAD(+)- and NADH-complexed XDH, E(sq/hq) were calculated to better understand how the enzyme activates an ET from FeS-II to flavin. 4,6-dinitro-o-cresol 217-223 xanthine dehydrogenase Homo sapiens 80-83 22145797-6 2012 On the basis of new 1.65, 2.3, 1.9, and 2.2 A resolution crystal structures for XDH, XO, the NAD(+)- and NADH-complexed XDH, E(sq/hq) were calculated to better understand how the enzyme activates an ET from FeS-II to flavin. 4,6-dinitro-o-cresol 217-223 xanthine dehydrogenase Homo sapiens 120-123 22145797-7 2012 The majority of the E(sq/hq) difference between XDH and XO originates from a conformational change in the loop at positions 423-433 near the flavin binding site, causing the differences in stability of the semiquinone state. 4,6-dinitro-o-cresol 141-147 xanthine dehydrogenase Homo sapiens 48-51 21538059-5 2012 In particular, the side chain of the C-terminal Y303 in Anabaena FNR appears key to providing the optimum geometry by reducing the stacking probability between the isoalloxazine and nicotinamide rings, thus providing the required co-linearity and distance among the N5 of the flavin cofactor, the C4 of the coenzyme nicotinamide and the hydride that has to be transferred between them. 4,6-dinitro-o-cresol 276-282 ferredoxin reductase Homo sapiens 65-68 22201895-9 2012 They are flavin dependent NADH preferred azoreductase, flavin dependent NADPH preferred azoreductase, and flavin free NADPH preferred azoreductase. 4,6-dinitro-o-cresol 9-15 NAD(P)H quinone dehydrogenase 1 Homo sapiens 41-53 22145797-9 2012 Instead, the positive charge of the NAD(+) ring, deprotonation of Asp429, and capping of the bulk surface of the flavin by the NAD(+) molecule all contribute to altering E(sq/hq) upon NAD(+) binding to XDH. 4,6-dinitro-o-cresol 113-119 xanthine dehydrogenase Homo sapiens 202-205 21925481-6 2012 Purification and kinetic analysis of the human KDMs JMJD2A and JMJD2D using these methods yielded activities substantially higher than those previously reported for these enzymes, which are comparable to that of the flavin-dependent KDM LSD1. 4,6-dinitro-o-cresol 216-222 lysine demethylase 4A Homo sapiens 52-58 21925481-6 2012 Purification and kinetic analysis of the human KDMs JMJD2A and JMJD2D using these methods yielded activities substantially higher than those previously reported for these enzymes, which are comparable to that of the flavin-dependent KDM LSD1. 4,6-dinitro-o-cresol 216-222 lysine demethylase 4D Homo sapiens 63-69 21925481-6 2012 Purification and kinetic analysis of the human KDMs JMJD2A and JMJD2D using these methods yielded activities substantially higher than those previously reported for these enzymes, which are comparable to that of the flavin-dependent KDM LSD1. 4,6-dinitro-o-cresol 216-222 lysine demethylase 1A Homo sapiens 237-241 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 22052907-9 2011 Notably, the activity of TTHA0420-DeltaC5 was about 10 times higher than that of the wild-type enzyme at 20-40 C. Our findings suggest that the C-terminal region of TTHA0420 may regulate the alternative binding of NADH and substrate flavin to the enzyme. 4,6-dinitro-o-cresol 234-240 flavin reductase family protein Thermus thermophilus HB8 25-33 22052907-9 2011 Notably, the activity of TTHA0420-DeltaC5 was about 10 times higher than that of the wild-type enzyme at 20-40 C. Our findings suggest that the C-terminal region of TTHA0420 may regulate the alternative binding of NADH and substrate flavin to the enzyme. 4,6-dinitro-o-cresol 234-240 flavin reductase family protein Thermus thermophilus HB8 166-174 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 22158896-3 2011 Both the crystal structures of IDI-2 binding the flavin-inhibitor adduct and the UV-visible spectra of the adducts indicate that the covalent bond is formed at C4a of flavin rather than at N5, which had been proposed previously. 4,6-dinitro-o-cresol 49-55 isopentenyl-diphosphate delta isomerase 2 Homo sapiens 31-36 22158896-3 2011 Both the crystal structures of IDI-2 binding the flavin-inhibitor adduct and the UV-visible spectra of the adducts indicate that the covalent bond is formed at C4a of flavin rather than at N5, which had been proposed previously. 4,6-dinitro-o-cresol 167-173 isopentenyl-diphosphate delta isomerase 2 Homo sapiens 31-36 22158896-4 2011 In addition, the high-resolution crystal structures of IDI-2-substrate complexes and the kinetic studies of new mutants confirmed that only the flavin cofactor can catalyze protonation of the substrates and suggest that N5 of flavin is most likely to be involved in proton transfer. 4,6-dinitro-o-cresol 144-150 isopentenyl-diphosphate delta isomerase 2 Homo sapiens 55-60 22158896-4 2011 In addition, the high-resolution crystal structures of IDI-2-substrate complexes and the kinetic studies of new mutants confirmed that only the flavin cofactor can catalyze protonation of the substrates and suggest that N5 of flavin is most likely to be involved in proton transfer. 4,6-dinitro-o-cresol 226-232 isopentenyl-diphosphate delta isomerase 2 Homo sapiens 55-60 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 21861807-1 2011 Dihydroorotate dehydrogenase (DHODH) is a flavin-dependent mitochondrial enzyme that catalyzes fourth reaction of pyrimidine de-novo synthesis. 4,6-dinitro-o-cresol 42-48 dihydroorotate dehydrogenase (quinone) Homo sapiens 0-28 21861807-1 2011 Dihydroorotate dehydrogenase (DHODH) is a flavin-dependent mitochondrial enzyme that catalyzes fourth reaction of pyrimidine de-novo synthesis. 4,6-dinitro-o-cresol 42-48 dihydroorotate dehydrogenase (quinone) Homo sapiens 30-35 21082301-0 2011 Flavin-containing monooxygenase mRNA levels are up-regulated in als brain areas in SOD1-mutant mice. 4,6-dinitro-o-cresol 0-6 superoxide dismutase 1, soluble Mus musculus 83-87 21803041-6 2011 The kinetics and NOS flavin fluorescence results together indicate that the docked FMN/heme state is populated transiently. 4,6-dinitro-o-cresol 21-27 formin 1 Homo sapiens 83-86 21680741-11 2011 The double mutant S171A/H396V reacted with oxygen to directly form the oxidized flavin without stabilizing the C4a-hydroperoxy-FMN intermediate, which confirmed the findings based on the single mutation that His-396 was important for formation and Ser-171 for stabilization of the C4a-hydroperoxy-FMN intermediate in C(2). 4,6-dinitro-o-cresol 80-86 complement C4A (Rodgers blood group) Homo sapiens 281-284 21680741-11 2011 The double mutant S171A/H396V reacted with oxygen to directly form the oxidized flavin without stabilizing the C4a-hydroperoxy-FMN intermediate, which confirmed the findings based on the single mutation that His-396 was important for formation and Ser-171 for stabilization of the C4a-hydroperoxy-FMN intermediate in C(2). 4,6-dinitro-o-cresol 80-86 formin 1 Homo sapiens 297-300 21467031-4 2011 Here, we give evidence of a mechanism for the reverse reaction, namely dark reoxidation of protein-bound flavin in Arabidopsis thaliana cryptochrome (AtCRY1) by molecular oxygen that involves formation of a spin-correlated FADH( )-superoxide radical pair. 4,6-dinitro-o-cresol 105-111 cryptochrome 1 Arabidopsis thaliana 150-156 21757996-1 2011 Proline dehydrogenase (ProDH) catalyzes the flavin-dependent oxidation of Pro into Delta1-pyrroline-5-carboxylate (P5C). 4,6-dinitro-o-cresol 44-50 Methylenetetrahydrofolate reductase family protein Arabidopsis thaliana 0-21 21757996-1 2011 Proline dehydrogenase (ProDH) catalyzes the flavin-dependent oxidation of Pro into Delta1-pyrroline-5-carboxylate (P5C). 4,6-dinitro-o-cresol 44-50 Methylenetetrahydrofolate reductase family protein Arabidopsis thaliana 23-28 21476070-12 2011 The results are contrary to the previous kinetic experiments and the computational study on the effect of p-substituents in the flavin reduction of MAO A by p-substituted benzylamine analogs. 4,6-dinitro-o-cresol 128-134 monoamine oxidase A Homo sapiens 148-153 21568312-1 2011 A single basic residue above the si-face of the flavin ring is the site of oxygen activation in glucose oxidase (GOX) (His516) and monomeric sarcosine oxidase (MSOX) (Lys265). 4,6-dinitro-o-cresol 48-54 hydroxyacid oxidase 1 Homo sapiens 96-111 21568312-1 2011 A single basic residue above the si-face of the flavin ring is the site of oxygen activation in glucose oxidase (GOX) (His516) and monomeric sarcosine oxidase (MSOX) (Lys265). 4,6-dinitro-o-cresol 48-54 hydroxyacid oxidase 1 Homo sapiens 113-116 21464294-5 2011 The ATP-induced iNOS interacted with p65 subunit of NF-kappaB in the cytosol through flavin-binding domain, which was indispensable for the locally generated NO-mediated S-nitrosylation of p65 at Cys38. 4,6-dinitro-o-cresol 85-91 nitric oxide synthase 2 Rattus norvegicus 16-20 21591753-6 2011 Of the three flavin-based compounds, RTA shows the most promise as a sensitizer in sunlight-based disinfection systems because it absorbs both visible and UV light, is an efficient 1O2 sensitizer, is a strong oxidant in its triplet state, and exhibits greater photostability. 4,6-dinitro-o-cresol 13-19 MAS related GPR family member F Homo sapiens 37-40 21510664-3 2011 The first enzyme to show such activity was LSD1, a flavin-containing enzyme that removes the methyl groups from lysines 4 and 9 of histone 3 with the generation of formaldehyde from the methyl group. 4,6-dinitro-o-cresol 51-57 lysine demethylase 1A Homo sapiens 43-47 21506232-5 2011 These indolequinones represent the first mechanism-based inhibitors of NQO2, and their novel mode of action involving alkylation of the flavin cofactor, provides significant advantages over existing competitive inhibitors in terms of potency and irreversibility, and will open new opportunities to define the role of NQO2 in disease. 4,6-dinitro-o-cresol 136-142 N-ribosyldihydronicotinamide:quinone reductase 2 Homo sapiens 71-75 21506232-5 2011 These indolequinones represent the first mechanism-based inhibitors of NQO2, and their novel mode of action involving alkylation of the flavin cofactor, provides significant advantages over existing competitive inhibitors in terms of potency and irreversibility, and will open new opportunities to define the role of NQO2 in disease. 4,6-dinitro-o-cresol 136-142 N-ribosyldihydronicotinamide:quinone reductase 2 Homo sapiens 317-321 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 21464294-5 2011 The ATP-induced iNOS interacted with p65 subunit of NF-kappaB in the cytosol through flavin-binding domain, which was indispensable for the locally generated NO-mediated S-nitrosylation of p65 at Cys38. 4,6-dinitro-o-cresol 85-91 synaptotagmin 1 Rattus norvegicus 189-192 21464294-5 2011 The ATP-induced iNOS interacted with p65 subunit of NF-kappaB in the cytosol through flavin-binding domain, which was indispensable for the locally generated NO-mediated S-nitrosylation of p65 at Cys38. 4,6-dinitro-o-cresol 85-91 synaptotagmin 1 Rattus norvegicus 37-40 21383138-2 2011 During this process MIA40 is reduced and regenerated to a functional state through the interaction with the flavin-dependent sulfhydryl oxidase ALR. 4,6-dinitro-o-cresol 108-114 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 20-25 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 21498682-7 2011 We also found an example of copper sparing in the N assimilation pathway: the replacement of copper amine oxidase by a flavin-dependent backup enzyme. 4,6-dinitro-o-cresol 119-125 uncharacterized protein Chlamydomonas reinhardtii 93-113 21383138-2 2011 During this process MIA40 is reduced and regenerated to a functional state through the interaction with the flavin-dependent sulfhydryl oxidase ALR. 4,6-dinitro-o-cresol 108-114 growth factor, augmenter of liver regeneration Homo sapiens 144-147 20561902-4 2010 NADPH cytochrome P450 reductase is a flavin-containing electron donor for cytochrome P450. 4,6-dinitro-o-cresol 37-43 cytochrome p450 oxidoreductase Rattus norvegicus 6-31 21308847-2 2011 The crystal structure of human ETF bound to medium chain acyl-CoA dehydrogenase indicates that the flavin adenine dinucleotide (FAD) domain (alphaII) is mobile, which permits more rapid electron transfer with donors and acceptors by providing closer access to the flavin and allows ETF to accept electrons from at least 10 different flavoprotein dehydrogenases. 4,6-dinitro-o-cresol 99-105 acyl-CoA dehydrogenase medium chain Homo sapiens 44-79 21141873-1 2011 Glycolate oxidase is a flavin-dependent enzyme that catalyzes the oxidation of alpha-hydroxy acids to the corresponding alpha-keto acids, with reduction of molecular oxygen to hydrogen peroxide. 4,6-dinitro-o-cresol 23-29 hydroxyacid oxidase 2 Homo sapiens 0-17 21558760-1 2011 This review focuses on the development of ruthenium and flavin catalysts for environmentally benign oxidation reactions based on mimicking the functions of cytochrome P-450 and flavoenzymes, and low valent transition-metal catalysts that replace conventional acids and bases. 4,6-dinitro-o-cresol 56-62 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 156-172 20136511-3 2010 This system consists of two essential proteins, a disulfide carrier Tim40/Mia40 and a flavin-dependent sulfhydryl oxidase Erv1, high-resolution structures that have recently become available. 4,6-dinitro-o-cresol 86-92 growth factor, augmenter of liver regeneration Homo sapiens 122-126 20167242-3 2010 The enzyme iodotyrosine deiodinase responsible for this salvage is unusual in its ability to catalyze a reductive dehalogenation reaction dependent on a flavin cofactor, FMN. 4,6-dinitro-o-cresol 153-159 formin 1 Homo sapiens 170-173 21385718-7 2011 The CRY-mediated light response requires a flavin redox-based mechanism and depends on potassium channel conductance, but is independent of the classical circadian CRY-TIMELESS interaction. 4,6-dinitro-o-cresol 43-49 cryptochrome Drosophila melanogaster 4-7 21182588-2 2011 We also have recently described channels that might allow access of oxygen to pockets at the active site of the flavoprotein D-amino acid oxidase (DAAO) that have a high affinity for dioxygen and are in close proximity to the flavin. 4,6-dinitro-o-cresol 226-232 D-amino acid oxidase Homo sapiens 125-145 21182588-2 2011 We also have recently described channels that might allow access of oxygen to pockets at the active site of the flavoprotein D-amino acid oxidase (DAAO) that have a high affinity for dioxygen and are in close proximity to the flavin. 4,6-dinitro-o-cresol 226-232 D-amino acid oxidase Homo sapiens 147-151 20093143-0 2010 The flavin inhibitor diphenyleneiodonium renders Trichomonas vaginalis resistant to metronidazole, inhibits thioredoxin reductase and flavin reductase, and shuts off hydrogenosomal enzymatic pathways. 4,6-dinitro-o-cresol 4-10 peroxiredoxin 5 Homo sapiens 108-129 20593814-1 2010 The sulfhydryl oxidase augmenter of liver regeneration (ALR) binds FAD in a helix-rich domain that presents a CxxC disulfide proximal to the isoalloxazine ring of the flavin. 4,6-dinitro-o-cresol 167-173 growth factor, augmenter of liver regeneration Homo sapiens 56-59 20450881-3 2010 Put1p was expressed and purified from Escherichia coli and shown to have a UV-visible absorption spectrum that is typical of a bound flavin cofactor. 4,6-dinitro-o-cresol 133-139 proline dehydrogenase Saccharomyces cerevisiae S288C 0-5 20593767-6 2010 Linear free energy relationships (LFERs) between the electronic properties of the flavin and the steady state kinetic parameters of the IDI-2 catalyzed reaction were observed. 4,6-dinitro-o-cresol 82-88 isopentenyl-diphosphate delta isomerase 2 Homo sapiens 136-141 20593767-8 2010 Cumulatively, the data presented in this work (and in other studies) suggest that the reduced FMN coenzyme of IDI-2 functions as an acid/base catalyst, with the N5 atom of the flavin likely playing a critical role in the deprotonation of IPP en route to DMAPP formation. 4,6-dinitro-o-cresol 176-182 isopentenyl-diphosphate delta isomerase 2 Homo sapiens 110-115 20353187-9 2010 A structural water (WAT1), found above the si-face of the flavin ring in all previously determined MSOX structures, is part of an apparent proton relay system that extends from FAD N(5) to bulk solvent. 4,6-dinitro-o-cresol 58-64 MTOR associated protein, LST8 homolog Homo sapiens 20-24 20093143-4 2010 In this study we added the flavin inhibitor diphenyleneiodonium (DPI) to T. vaginalis cultures in order to test our hypothesis that metronidazole reduction is catalyzed by flavin enzymes, e.g. thioredoxin reductase, and intracellular free flavins. 4,6-dinitro-o-cresol 172-178 peroxiredoxin 5 Homo sapiens 193-214 20101264-9 2010 Collectively, our study identifies AOF1 as the second histone demethylase in the family of flavin-dependent amine oxidases and reveals a demethylase-independent repression function of AOF1. 4,6-dinitro-o-cresol 91-97 lysine demethylase 1B Homo sapiens 35-39 19790248-2 2010 Nitric oxide (NO) formation might be a potential mechanism for photobiomodulation because it is synthesized in cells by nitric oxide synthase (NOS), which contains both flavin and heme groups that absorb visible light. 4,6-dinitro-o-cresol 169-175 nitric oxide synthase 2 Homo sapiens 120-141 20026040-0 2010 Electron transfer in the complex of membrane-bound human cytochrome P450 3A4 with the flavin domain of P450BM-3: the effect of oligomerization of the heme protein and intermittent modulation of the spin equilibrium. 4,6-dinitro-o-cresol 86-92 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 57-76 20101264-9 2010 Collectively, our study identifies AOF1 as the second histone demethylase in the family of flavin-dependent amine oxidases and reveals a demethylase-independent repression function of AOF1. 4,6-dinitro-o-cresol 91-97 methyl-CpG binding domain protein 2 Homo sapiens 62-73 20101264-9 2010 Collectively, our study identifies AOF1 as the second histone demethylase in the family of flavin-dependent amine oxidases and reveals a demethylase-independent repression function of AOF1. 4,6-dinitro-o-cresol 91-97 methyl-CpG binding domain protein 2 Homo sapiens 137-148 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 19626459-3 2010 Degenerate PCR amplification of the regions encoding the conserved flavin-binding domain of CRY proteins yielded seven bands, resulting from amplification of CRY1a, CRY1b and CRY2 homologous genes. 4,6-dinitro-o-cresol 67-73 cryptochrome-1 Triticum aestivum 158-163 19626459-3 2010 Degenerate PCR amplification of the regions encoding the conserved flavin-binding domain of CRY proteins yielded seven bands, resulting from amplification of CRY1a, CRY1b and CRY2 homologous genes. 4,6-dinitro-o-cresol 67-73 cryptochrome-1 Triticum aestivum 175-179 19948738-6 2010 Moreover, stopped-flow spectrophotometric experiments with the nNOS reductase domain indicate that the CaM-free mutants had faster flavin reduction kinetics and had less shielding of their FMN subdomains compared with wild type and no longer increased their level of FMN shielding in response to NADPH binding. 4,6-dinitro-o-cresol 131-137 nitric oxide synthase 1 Homo sapiens 63-67 19948738-6 2010 Moreover, stopped-flow spectrophotometric experiments with the nNOS reductase domain indicate that the CaM-free mutants had faster flavin reduction kinetics and had less shielding of their FMN subdomains compared with wild type and no longer increased their level of FMN shielding in response to NADPH binding. 4,6-dinitro-o-cresol 131-137 calmodulin 1 Homo sapiens 103-106 19911805-7 2009 These results are consistent with direct transfer of a hydride from the neutral CN bond of the substrate to the flavin as the mechanism of polyamine oxidase. 4,6-dinitro-o-cresol 112-118 polyamine oxidase Homo sapiens 139-156 19944667-2 2010 The flavin-oxygen adduct can be the C4a-peroxide anion, in which case it reacts as a nucleophile. 4,6-dinitro-o-cresol 4-10 complement C4A (Rodgers blood group) Homo sapiens 36-39 19897659-9 2010 The parallel phenotypes of Mtr mutants in flavin and electrode reduction blur the distinction between direct contact and the redox shuttling strategies of insoluble substrate reduction by MR-1. 4,6-dinitro-o-cresol 42-48 tryptophan permease Shewanella oneidensis MR-1 27-30 19758989-1 2009 Glycolate oxidase is a flavin-dependent, peroxisomal enzyme that oxidizes alpha-hydroxy acids to the corresponding alpha-keto acids, with reduction of oxygen to H(2)O(2). 4,6-dinitro-o-cresol 23-29 hydroxyacid oxidase 2 Homo sapiens 0-17 19921821-3 2009 The originally published repair mechanism involves rearrangement of the lesion into an oxetane intermediate upon binding to the (6-4) photolyase, followed by light-induced electron transfer from the reduced flavin cofactor. 4,6-dinitro-o-cresol 207-213 (6-4)-photolyase Drosophila melanogaster 129-144 19740970-5 2009 DESIGN: A fluorometric assay was optimized for the flavin-dependent enzyme PPO in erythrocytes. 4,6-dinitro-o-cresol 51-57 pyridoxamine 5'-phosphate oxidase Homo sapiens 75-78 19720617-4 2009 For their import into the IMS, they employ a disulphide relay system, made up of two essential proteins, Mia40/Tim40 and the flavin-dependent sulfhydryl-electron transferase Erv1. 4,6-dinitro-o-cresol 125-131 growth factor, augmenter of liver regeneration Homo sapiens 174-178 20095972-6 2009 A second means of targeting the chromatin-remodelling enzymes with polyamine analogues was facilitated by the recent identification of flavin-dependent LSD1 (lysine-specific demethylase 1). 4,6-dinitro-o-cresol 135-141 lysine demethylase 1A Homo sapiens 152-156 20095972-6 2009 A second means of targeting the chromatin-remodelling enzymes with polyamine analogues was facilitated by the recent identification of flavin-dependent LSD1 (lysine-specific demethylase 1). 4,6-dinitro-o-cresol 135-141 lysine demethylase 1A Homo sapiens 158-187 19747080-6 2009 PACalpha shows a basal AC activity in the dark which is unaffected by mutating the conserved tyrosines in the two flavin-binding domains (F1, F2), Y60 in F1 and Y472 in F2. 4,6-dinitro-o-cresol 114-120 pancreas associated transcription factor 1a Homo sapiens 0-8 20198185-5 2009 Our current work focuses on an attempted to dock this inhibitors Flavin and Phenosafranine to curtail the action of human RNR2. 4,6-dinitro-o-cresol 65-71 RNA, ribosomal 45S cluster 2 Homo sapiens 122-126 20198185-10 2009 The docking study was performed for the crystal structure of human RNR with the radical scavengers Flavin and Phenosafranine to inhibit the human RNR2. 4,6-dinitro-o-cresol 99-105 RNA, ribosomal 45S cluster 2 Homo sapiens 146-150 19645722-7 2009 Compared to purified wild-type and Ser209Ala MAO A proteins, the Ser209Glu MAO A mutant shows significant differences in covalent flavin fluorescence yield, CD spectra and thermal stability. 4,6-dinitro-o-cresol 130-136 monoamine oxidase A Homo sapiens 75-80 19470521-2 2009 Although 8-NH(2)-FAD-MCAD did not oxidize acyl-CoA the wavelength of the absorption maximum of the flavin was altered by acyl-CoAs binding. 4,6-dinitro-o-cresol 99-105 acyl-CoA dehydrogenase medium chain Homo sapiens 21-25 19618916-0 2009 Mechanism of flavin reduction and oxidation in the redox-sensing quinone reductase Lot6p from Saccharomyces cerevisiae. 4,6-dinitro-o-cresol 13-19 flavin-dependent quinone reductase Saccharomyces cerevisiae S288C 83-88 19618916-9 2009 This curious situation is consistent with the structure of Lot6p, which has a crease we propose to be the binding site for pyridine nucleotides and a space, but no obvious catalytic residues, near the flavin allowing the quinone to react. 4,6-dinitro-o-cresol 201-207 flavin-dependent quinone reductase Saccharomyces cerevisiae S288C 59-64 19436071-6 2009 Substrate coordination to IYD induces formation of an additional helix and coil that act as an active site lid to shield the resulting substrate.flavin complex from solvent. 4,6-dinitro-o-cresol 145-151 iodotyrosine deiodinase Homo sapiens 26-29 19320843-0 2009 Flavin-sensitized photo-oxidation of lysozyme and serum albumin. 4,6-dinitro-o-cresol 0-6 albumin Homo sapiens 50-63 19541622-6 2009 This study indicates that monooxygenase and oxidase flavoenzymes employ multiple funnel-shaped diffusion pathways to absorb O(2) from the solvent and direct it to the reacting C4a atom of the flavin cofactor. 4,6-dinitro-o-cresol 192-198 complement C4A (Rodgers blood group) Homo sapiens 176-179 18638483-7 2008 Intriguingly, the flavin bond lengths in oxidized GR are intermediate between those expected for oxidized and reduced flavin, but we present evidence that this may not be due to the protein environment but instead due to partial synchrotron reduction of the flavin by the synchrotron beam. 4,6-dinitro-o-cresol 18-24 glutathione-disulfide reductase Homo sapiens 50-52 19407342-3 2009 Among the histone demethylases so far identified, LSD1 has the unique feature of functioning through a flavin-dependent amine oxidation reaction. 4,6-dinitro-o-cresol 103-109 lysine demethylase 1A Homo sapiens 50-54 19397338-1 2009 Augmenter of liver regeneration (ALR) is both a growth factor and a sulfhydryl oxidase that binds FAD in an unusual helix-rich domain containing a redox-active CxxC disulfide proximal to the flavin ring. 4,6-dinitro-o-cresol 191-197 growth factor, augmenter of liver regeneration Homo sapiens 0-31 19397338-1 2009 Augmenter of liver regeneration (ALR) is both a growth factor and a sulfhydryl oxidase that binds FAD in an unusual helix-rich domain containing a redox-active CxxC disulfide proximal to the flavin ring. 4,6-dinitro-o-cresol 191-197 growth factor, augmenter of liver regeneration Homo sapiens 33-36 19397338-13 2009 Thus, catalysis involves a flow of reducing equivalents from the reduced CxC motif of Mia40 to distal and then proximal CxxC motifs of lfALR to the flavin ring and, finally, to cytochrome c or molecular oxygen. 4,6-dinitro-o-cresol 148-154 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 86-91 19397338-13 2009 Thus, catalysis involves a flow of reducing equivalents from the reduced CxC motif of Mia40 to distal and then proximal CxxC motifs of lfALR to the flavin ring and, finally, to cytochrome c or molecular oxygen. 4,6-dinitro-o-cresol 148-154 cytochrome c, somatic Homo sapiens 177-189 19017646-1 2009 The redox reactivity of the three disulfide bridges and the flavin present in each protomer of the wild-type Arabidopsis thaliana mitochondrial sulfhydryl oxidase (AtErv1) homodimer has been investigated. 4,6-dinitro-o-cresol 60-66 Erv1/Alr family protein Arabidopsis thaliana 164-170 19053775-6 2008 The X-ray crystal structure of the mofegiline-MAO-B adduct shows a covalent bond between the flavin cofactor N(5) with the distal allylamine carbon atom as well as the absence of the fluorine atom. 4,6-dinitro-o-cresol 93-99 monoamine oxidase B Homo sapiens 46-51 19445526-3 2009 These redox changes in NQO2, however, lead to unequal charge separation between the flavin ring and the active site, which must be stabilized by reorganization of the surrounding protein matrix. 4,6-dinitro-o-cresol 84-90 N-ribosyldihydronicotinamide:quinone reductase 2 Homo sapiens 23-27 19445526-4 2009 In this study, we have used a combined quantum mechanical/molecular mechanical method to simulate the electron and proton addition reactions of the flavin-bound NQO2. 4,6-dinitro-o-cresol 148-154 N-ribosyldihydronicotinamide:quinone reductase 2 Homo sapiens 161-165 19445526-6 2009 The present work demonstrates that upon reduction, the NQO2 active site stabilizes the flavin anionic hydroquinone state. 4,6-dinitro-o-cresol 87-93 N-ribosyldihydronicotinamide:quinone reductase 2 Homo sapiens 55-59 19290671-10 2009 This helps to explain the unique electron transfer and catalytic behaviors of nNOS, relative to other dual-flavin enzymes. 4,6-dinitro-o-cresol 107-113 nitric oxide synthase 1 Rattus norvegicus 78-82 19327354-3 2009 Here we show in purified preparations of Arabidopsis cry1 that ATP binding induces conformational change independently of light and increases the amount and stability of light-induced flavin radical formation. 4,6-dinitro-o-cresol 184-190 cryptochrome 1 Arabidopsis thaliana 53-57 19309736-0 2009 Relevance of weak flavin binding in human D-amino acid oxidase. 4,6-dinitro-o-cresol 18-24 D-amino acid oxidase Homo sapiens 42-62 19236722-4 2009 Using electronic absorption spectroscopy, we show that imatinib binding results in a perturbation of the protein environment around the flavin prosthetic group in NQO2. 4,6-dinitro-o-cresol 136-142 N-ribosyldihydronicotinamide:quinone reductase 2 Homo sapiens 163-167 18980384-0 2008 Impeded electron transfer from a pathogenic FMN domain mutant of methionine synthase reductase and its responsiveness to flavin supplementation. 4,6-dinitro-o-cresol 121-127 5-methyltetrahydrofolate-homocysteine methyltransferase reductase Homo sapiens 65-94 19704421-3 2008 Our recent analysis using yeast two-hybrid and Escherichia coli protein production systems reveals that the interactions of Arabidopsis PLPs with several proteins diminish under blue light illumination and that the PLP LOV domain may bind to a flavin chromophore. 4,6-dinitro-o-cresol 244-250 PAS/LOV protein B Arabidopsis thaliana 136-139 18638483-7 2008 Intriguingly, the flavin bond lengths in oxidized GR are intermediate between those expected for oxidized and reduced flavin, but we present evidence that this may not be due to the protein environment but instead due to partial synchrotron reduction of the flavin by the synchrotron beam. 4,6-dinitro-o-cresol 118-124 glutathione-disulfide reductase Homo sapiens 50-52 18629490-1 2008 Three cytosolic NADPH-dependent flavin-associated proteins (Gox2107, Gox0502, and Gox2684) from Gluconobacter oxydans 621H were overproduced in Escherichia coli, and the recombinant enzymes were purified and characterized. 4,6-dinitro-o-cresol 32-38 NAD(P)H-dependent oxidoreductase Gluconobacter oxydans 621H 60-67 18629490-1 2008 Three cytosolic NADPH-dependent flavin-associated proteins (Gox2107, Gox0502, and Gox2684) from Gluconobacter oxydans 621H were overproduced in Escherichia coli, and the recombinant enzymes were purified and characterized. 4,6-dinitro-o-cresol 32-38 alkene reductase Gluconobacter oxydans 621H 69-76 18629490-1 2008 Three cytosolic NADPH-dependent flavin-associated proteins (Gox2107, Gox0502, and Gox2684) from Gluconobacter oxydans 621H were overproduced in Escherichia coli, and the recombinant enzymes were purified and characterized. 4,6-dinitro-o-cresol 32-38 alkene reductase Gluconobacter oxydans 621H 82-89 18671962-6 2008 Urotensin II-increased cell proliferation and intracellular reactive oxygen species levels which were inhibited by antioxidants N-acetylcysteine, and the flavin inhibitor diphenyleneiodonium. 4,6-dinitro-o-cresol 154-160 urotensin 2 Rattus norvegicus 0-12 18500801-1 2008 Rat NADP-dependent leukotriene B4 12-hydroxydehydrogenase (Ltb4dh) catalyzes olefin reductions for some activated alkenes at the expense of NADPH in the absence of a flavin cofactor. 4,6-dinitro-o-cresol 166-172 prostaglandin reductase 1 Rattus norvegicus 4-57 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 18500801-1 2008 Rat NADP-dependent leukotriene B4 12-hydroxydehydrogenase (Ltb4dh) catalyzes olefin reductions for some activated alkenes at the expense of NADPH in the absence of a flavin cofactor. 4,6-dinitro-o-cresol 166-172 prostaglandin reductase 1 Rattus norvegicus 59-65 18426226-8 2008 The three-dimensional (2.3 A) structures of phenylethylhydrazine- and benzylhydrazine-inhibited MAO B show that alkylation occurs at the N(5) position on the re face of the covalent flavin with loss of the hydrazyl nitrogens. 4,6-dinitro-o-cresol 182-188 monoamine oxidase B Homo sapiens 96-101 18393449-9 2008 C452, of the proximal disulfide, is shown to be the charge-transfer donor to the flavin ring of QSOX, and its partner, C449, is expected to be the interchange thiol, forming a mixed disulfide with C70 in the thioredoxin domain. 4,6-dinitro-o-cresol 81-87 quiescin sulfhydryl oxidase 1 Homo sapiens 96-100 18414230-6 2008 The increase was reduced by tiron, a protein kinase C inhibitor (bisindolylmaleimide I hydrochloride), the flavin inhibitor (diphenylene iodonium), and by a short interfering RNA against the p22phox component of NADPH oxidase. 4,6-dinitro-o-cresol 107-113 cytochrome b-245 alpha chain Homo sapiens 191-198 18396913-1 2008 The Lotus japonicus EST database was searched against Arabidopsis thaliana AtFAO3, a full-length cDNA that encodes a membrane-bound, flavin-containing, hydrogen peroxide generating, long-chain fatty alcohol oxidase. 4,6-dinitro-o-cresol 133-139 fatty alcohol oxidase 3 Arabidopsis thaliana 75-81 18086551-0 2008 Kinetics of electron transfer in the complex of cytochrome P450 3A4 with the flavin domain of cytochrome P450BM-3 as evidence of functional heterogeneity of the heme protein. 4,6-dinitro-o-cresol 77-83 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 48-67 18345677-3 2008 Type I IPP isomerase (IDI-1) utilizes a divalent metal in a protonation-deprotonation reaction; whereas, the type II enzyme (IDI-2) requires reduced flavin. 4,6-dinitro-o-cresol 149-155 isopentenyl-diphosphate delta isomerase 1 Homo sapiens 22-27 18345677-3 2008 Type I IPP isomerase (IDI-1) utilizes a divalent metal in a protonation-deprotonation reaction; whereas, the type II enzyme (IDI-2) requires reduced flavin. 4,6-dinitro-o-cresol 149-155 isopentenyl-diphosphate delta isomerase 2 Homo sapiens 125-130 18345677-11 2008 These studies indicate that the irreversible inhibitors inactivate the reduced flavin required for catalysis by electrophilic alkylation and are consistent with a protonation-deprotonation mechanism for the isomerization catalyzed by IDI-2. 4,6-dinitro-o-cresol 79-85 isopentenyl-diphosphate delta isomerase 2 Homo sapiens 234-239 18370414-7 2008 The reduction of CB1954 catalyzed by the neuronal NOS (nNOS) was inhibited by O 2 and a flavin/NADPH binding inhibitor, diphenyliodonium (DPI), but insensitive to the addition of the heme ligands imidazole and carbon monoxide and of l-arginine analogues. 4,6-dinitro-o-cresol 88-94 nitric oxide synthase 1 Homo sapiens 41-53 18370414-7 2008 The reduction of CB1954 catalyzed by the neuronal NOS (nNOS) was inhibited by O 2 and a flavin/NADPH binding inhibitor, diphenyliodonium (DPI), but insensitive to the addition of the heme ligands imidazole and carbon monoxide and of l-arginine analogues. 4,6-dinitro-o-cresol 88-94 nitric oxide synthase 1 Homo sapiens 55-59 18241886-6 2008 Unlike the bent FMN ring structures present in most NTR complexes currently known, the flavin system in the Ec_ydjA structure maintains a flat ring conformation, which is sandwiched between a Trp and a His residue from each monomer. 4,6-dinitro-o-cresol 87-93 ydjA Escherichia coli K-12 111-115 18086551-1 2008 We used a rapid scanning stop-flow technique to study the kinetics of reduction of cytochrome P450 3A4 (CYP3A4) by the flavin domain of cytochrome P450-BM3 (BMR), which was shown to form a stoichiometric complex (K(D)=0.48 microM) with CYP3A4. 4,6-dinitro-o-cresol 119-125 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 83-102 18086551-1 2008 We used a rapid scanning stop-flow technique to study the kinetics of reduction of cytochrome P450 3A4 (CYP3A4) by the flavin domain of cytochrome P450-BM3 (BMR), which was shown to form a stoichiometric complex (K(D)=0.48 microM) with CYP3A4. 4,6-dinitro-o-cresol 119-125 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 104-110 18086551-1 2008 We used a rapid scanning stop-flow technique to study the kinetics of reduction of cytochrome P450 3A4 (CYP3A4) by the flavin domain of cytochrome P450-BM3 (BMR), which was shown to form a stoichiometric complex (K(D)=0.48 microM) with CYP3A4. 4,6-dinitro-o-cresol 119-125 cytochrome P450 family 3 subfamily A member 4 Homo sapiens 236-242 18225919-2 2008 Clinically significant inhibitors of human DHODH (e.g., A77 1726) bind to a pocket on the opposite face of the flavin cofactor from dihydroorotate (DHO). 4,6-dinitro-o-cresol 111-117 dihydroorotate dehydrogenase (quinone) Homo sapiens 43-48 17964805-2 2008 The hydroxylases obtain reducing equivalents from NAD(P)H via an electron transfer chain that is initiated by an oxidoreductase containing an N-terminal ferredoxin domain and C-terminal flavin- and NAD-binding domains. 4,6-dinitro-o-cresol 186-192 oxidoreductase Escherichia coli 113-127 18039463-3 2008 Recently, the crystal structure of LSD1 and tranylcypromine was solved at 2.75 A, revealing a five-membered ring fused to the flavin of LSD1. 4,6-dinitro-o-cresol 126-132 lysine demethylase 1A Homo sapiens 35-39 18039463-3 2008 Recently, the crystal structure of LSD1 and tranylcypromine was solved at 2.75 A, revealing a five-membered ring fused to the flavin of LSD1. 4,6-dinitro-o-cresol 126-132 lysine demethylase 1A Homo sapiens 136-140 17982713-7 2008 Furthermore, the possible binding of flavin chromophore to PLPA and PLPB was demonstrated. 4,6-dinitro-o-cresol 37-43 PAS/LOV protein B Arabidopsis thaliana 59-63 17982713-7 2008 Furthermore, the possible binding of flavin chromophore to PLPA and PLPB was demonstrated. 4,6-dinitro-o-cresol 37-43 PAS/LOV protein B Arabidopsis thaliana 68-72 20031915-6 2008 We further show that cry1 protein expressed in living insect cells responds with greater sensitivity to 380 nm light than to 450 nm, consistent with a light-harvesting antenna pigment that transfers excitation energy to the oxidized flavin of cry1. 4,6-dinitro-o-cresol 233-239 cryptochrome 1 Arabidopsis thaliana 21-25 20031915-6 2008 We further show that cry1 protein expressed in living insect cells responds with greater sensitivity to 380 nm light than to 450 nm, consistent with a light-harvesting antenna pigment that transfers excitation energy to the oxidized flavin of cry1. 4,6-dinitro-o-cresol 233-239 cryptochrome 1 Arabidopsis thaliana 243-247 20031924-2 2008 Light sensing is mediated by two flavin-binding motifs, known as LOV1 and LOV2, located within the N-terminal region of the protein. 4,6-dinitro-o-cresol 33-39 NAC domain containing protein 35 Arabidopsis thaliana 65-69 18044898-12 2007 DAAO contains a noncovalently bound flavin whereas MAO A contains a flavin covalently bound to a cysteinyl residue at C8alpha. 4,6-dinitro-o-cresol 36-42 D-amino acid oxidase Homo sapiens 0-4 18044898-12 2007 DAAO contains a noncovalently bound flavin whereas MAO A contains a flavin covalently bound to a cysteinyl residue at C8alpha. 4,6-dinitro-o-cresol 68-74 monoamine oxidase A Homo sapiens 51-56 17875556-5 2007 The 1,645-cm(-1) band containing C(2)=O stretching vibration shifted to 1,630 cm(-1) in the medium-chain acyl-CoA dehydrogenase (MCAD)-bound state, which can be explained by hydrogen bonds at C(2)=O of the flavin ring. 4,6-dinitro-o-cresol 206-212 acyl-CoA dehydrogenase medium chain Homo sapiens 92-127 18220846-8 2007 By a rational and/or a directed evolution approach, DAAO variants with altered substrate specificity (e.g., active on acidic or on all D-amino acids), increased stability (e.g., stable up to 60 degrees C), modified interaction with the flavin cofactor, and altered oligomeric state were produced. 4,6-dinitro-o-cresol 236-242 D-amino acid oxidase Homo sapiens 52-56 17892308-2 2007 MSR contains one FAD and one FMN cofactor per polypeptide and functions in the sequential transfer of reducing equivalents from NADPH to MS via its flavin centers. 4,6-dinitro-o-cresol 148-154 5-methyltetrahydrofolate-homocysteine methyltransferase reductase Homo sapiens 0-3 17892308-2 2007 MSR contains one FAD and one FMN cofactor per polypeptide and functions in the sequential transfer of reducing equivalents from NADPH to MS via its flavin centers. 4,6-dinitro-o-cresol 148-154 formin 1 Homo sapiens 29-32 17851108-1 2007 The recent discovery that histone demethylation can be catalyzed by the flavin-dependent amine oxidase LSD1 has ushered in a new chapter in the chromatin-remodeling community. 4,6-dinitro-o-cresol 72-78 lysine demethylase 1A Homo sapiens 103-107 17704763-7 2007 Furthermore, the ZTL-GI interaction is strongly and specifically enhanced by blue light, through the amino-terminal flavin-binding LIGHT, OXYGEN OR VOLTAGE (LOV) domain of ZTL. 4,6-dinitro-o-cresol 116-122 Galactose oxidase/kelch repeat superfamily protein Arabidopsis thaliana 17-20 17704763-7 2007 Furthermore, the ZTL-GI interaction is strongly and specifically enhanced by blue light, through the amino-terminal flavin-binding LIGHT, OXYGEN OR VOLTAGE (LOV) domain of ZTL. 4,6-dinitro-o-cresol 116-122 Galactose oxidase/kelch repeat superfamily protein Arabidopsis thaliana 172-175 17704763-9 2007 Notably, a C82A mutation in the LOV domain, implicated in the flavin-dependent photochemistry, eliminates blue-light-enhanced binding of GI to ZTL. 4,6-dinitro-o-cresol 62-68 gigantea protein (GI) Arabidopsis thaliana 137-139 17662034-6 2007 Our study shows that the earlier expression phases of the floral induction genes GIGANTEA, FLAVIN-BINDING KELCH REPEAT F-BOX1 and CONSTANS correlate with higher abundance of the FLOWERING LOCUS T transcript under short-day conditions. 4,6-dinitro-o-cresol 91-97 flavin-binding, kelch repeat, f box 1 Arabidopsis thaliana 119-125 17580897-4 2007 In particular, the catalytic mechanisms of two of these enzymes, UGM and IDI-2, may involve novel flavin chemistry. 4,6-dinitro-o-cresol 98-104 isopentenyl-diphosphate delta isomerase 2 Homo sapiens 73-78 17875556-5 2007 The 1,645-cm(-1) band containing C(2)=O stretching vibration shifted to 1,630 cm(-1) in the medium-chain acyl-CoA dehydrogenase (MCAD)-bound state, which can be explained by hydrogen bonds at C(2)=O of the flavin ring. 4,6-dinitro-o-cresol 206-212 acyl-CoA dehydrogenase medium chain Homo sapiens 129-133 17511474-5 2007 Spectral changes associated with the 1-LSD1 complex and reactivity to decreased pH and sodium borohydride treatment were suggestive of a structure involving a flavin-linked inhibitor conjugate between N5 of the flavin and the terminal carbon of the inhibitor. 4,6-dinitro-o-cresol 159-165 lysine demethylase 1A Homo sapiens 39-43 17567113-10 2007 In MCAD, the flavin ring interacts with four hydrophobic residues and has a significantly bent structure, even in the oxidized state. 4,6-dinitro-o-cresol 13-19 acyl-CoA dehydrogenase medium chain Homo sapiens 3-7 17511474-5 2007 Spectral changes associated with the 1-LSD1 complex and reactivity to decreased pH and sodium borohydride treatment were suggestive of a structure involving a flavin-linked inhibitor conjugate between N5 of the flavin and the terminal carbon of the inhibitor. 4,6-dinitro-o-cresol 211-217 lysine demethylase 1A Homo sapiens 39-43 17511474-7 2007 Kinetic analysis of the spectroscopic shift induced by 1 showed that the flavin adduct formed in a reaction with kinetic constants similar to those of the LSD1 inactivation process. 4,6-dinitro-o-cresol 73-79 lysine demethylase 1A Homo sapiens 155-159 17134376-1 2007 PPO (protoporphyrinogen IX oxidase) catalyses the flavin-dependent six-electron oxidation of protogen (protoporphyrinogen IX) to form proto (protoporphyrin IX), a crucial step in haem and chlorophyll biosynthesis. 4,6-dinitro-o-cresol 50-56 protoporphyrinogen oxidase, chloroplastic Nicotiana tabacum 0-3 17411075-2 2007 NADPH analogues and fragments have been used to map those regions of this substrate that are important in eliciting a conformational change, observed in both the fluorescence emission of the flavin cofactors of the enzyme and the EPR spectra of the FMN flavosemiquinone state. 4,6-dinitro-o-cresol 191-197 formin 1 Homo sapiens 249-252 17411075-5 2007 These studies support a model in which FMN domain mobility, triggered by Ca2+-calmodulin binding and antagonized by substrate binding, facilitates electron transfer in nitric oxide synthase through conformational change and effects a major change in the midpoint reduction potentials of the flavin redox couples. 4,6-dinitro-o-cresol 291-297 formin 1 Homo sapiens 39-42 17367163-1 2007 The catalytic domain of the flavin-dependent human histone demethylase lysine-specific demethylase 1 (LSD1) belongs to the family of amine oxidases including polyamine oxidase and monoamine oxidase (MAO). 4,6-dinitro-o-cresol 28-34 lysine demethylase 1A Homo sapiens 71-100 17367163-1 2007 The catalytic domain of the flavin-dependent human histone demethylase lysine-specific demethylase 1 (LSD1) belongs to the family of amine oxidases including polyamine oxidase and monoamine oxidase (MAO). 4,6-dinitro-o-cresol 28-34 lysine demethylase 1A Homo sapiens 102-106 17355959-7 2007 Here we have shown that Arabidopsis Cry2 undergoes a photocycle in which semireduced flavin (FADH(.)) 4,6-dinitro-o-cresol 85-91 cryptochrome 2 Arabidopsis thaliana 36-40 17355959-9 2007 Green light irradiation of Cry2 causes a change in the equilibrium of flavin oxidation states and attenuates Cry2-controlled responses such as flowering. 4,6-dinitro-o-cresol 70-76 cryptochrome 2 Arabidopsis thaliana 27-31 17298084-4 2007 Dithionite and photochemical reductions of Erv2p show full reduction of the flavin cofactor after the addition of 4 electrons with a midpoint potential of -200 mV at pH 7.5. 4,6-dinitro-o-cresol 76-82 flavin-linked sulfhydryl oxidase Saccharomyces cerevisiae S288C 43-48 17298084-9 2007 Rapid reaction studies confirm that reduction of the flavin center of Erv2p is rate-limiting during turnover with molecular oxygen. 4,6-dinitro-o-cresol 53-59 flavin-linked sulfhydryl oxidase Saccharomyces cerevisiae S288C 70-75 17134376-1 2007 PPO (protoporphyrinogen IX oxidase) catalyses the flavin-dependent six-electron oxidation of protogen (protoporphyrinogen IX) to form proto (protoporphyrin IX), a crucial step in haem and chlorophyll biosynthesis. 4,6-dinitro-o-cresol 50-56 protoporphyrinogen oxidase, chloroplastic Nicotiana tabacum 5-34 17480205-6 2007 Agmatine, a putative endogenous ligand for some imidazoline sites, reduced monoamine oxidase A under anaerobic conditions, indicating that it binds close to the flavin in the active site. 4,6-dinitro-o-cresol 161-167 monoamine oxidase A Homo sapiens 75-94 17489100-8 2007 In contrast, the cytochrome b5-NADH pathway becomes dominant under conditions of excess metHb accumulation, only after the capacity of the flavin-NADPH pathway has reached its limit. 4,6-dinitro-o-cresol 139-145 cytochrome b5 type A Homo sapiens 17-30 17029414-3 2006 Previously we found that the D1393V and D1393N mutations lowered the NO synthesis activity and the rates of heme and flavin reduction in full-length nNOS. 4,6-dinitro-o-cresol 117-123 nitric oxide synthase 1 Homo sapiens 149-153 17263536-3 2007 Specific binding of the nanotrigger to the reductase domain of the endothelial nitric oxide synthase (eNOSred) was demonstrated by competition between NADPH and the nanotrigger on the reduction of eNOSred flavin. 4,6-dinitro-o-cresol 205-211 nitric oxide synthase 3 Homo sapiens 67-100 17144671-10 2006 These findings are also discussed in relation to the function of FRP as a reduced flavin donor in the FRP-luciferase couple. 4,6-dinitro-o-cresol 82-88 secreted frizzled related protein 1 Homo sapiens 65-68 17144671-10 2006 These findings are also discussed in relation to the function of FRP as a reduced flavin donor in the FRP-luciferase couple. 4,6-dinitro-o-cresol 82-88 secreted frizzled related protein 1 Homo sapiens 102-105 17088322-0 2006 Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring. 4,6-dinitro-o-cresol 171-177 D-amino acid oxidase Homo sapiens 27-47 17088322-3 2006 We recently succeeded in purifying human DAO, and found that it weakly binds FAD and shows a significant slower rate of flavin reduction compared with porcine DAO. 4,6-dinitro-o-cresol 120-126 D-amino acid oxidase Homo sapiens 41-44 17088322-6 2006 The overall dimeric structure of human DAO is similar to porcine DAO, and the catalytic residues are fully conserved at the re-face of the flavin ring. 4,6-dinitro-o-cresol 139-145 D-amino acid oxidase Homo sapiens 39-42 16966328-4 2006 Both substitutions yielded proteins that exhibited decreased rates of electron transfer through the flavin domains, in the presence and absence of Ca2+/CaM, as measured by reduction of potassium ferricyanide and cytochrome c. 4,6-dinitro-o-cresol 100-106 cytochrome c, somatic Homo sapiens 212-224 16966328-9 2006 These data presented here suggest that hydrogen bonding of the hydroxyl group of serine or threonine with the isoalloxazine ring of FAD and with the amino acids in its immediate milieu, particularly nNOS Asp-1393, affects the redox potentials of various flavin states, influencing the rate of electron transfer. 4,6-dinitro-o-cresol 254-260 nitric oxide synthase 1 Homo sapiens 199-203 17049252-4 2007 Furthermore, AutoDock study has been done by binding of the flavin analogs into PTK pp60(c-src), where a good correlation between their IC(50) and AutoDock binding free energy was exhibited. 4,6-dinitro-o-cresol 60-66 SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens 89-94 17401535-5 2007 Decreased pH induced a blue shift in the spectral maximum of MAO-A indicative of a more hydrophobic environment around the flavin, and also influenced the redox properties of the flavin. 4,6-dinitro-o-cresol 123-129 monoamine oxidase A Homo sapiens 61-66 17401535-5 2007 Decreased pH induced a blue shift in the spectral maximum of MAO-A indicative of a more hydrophobic environment around the flavin, and also influenced the redox properties of the flavin. 4,6-dinitro-o-cresol 179-185 monoamine oxidase A Homo sapiens 61-66 17030739-2 2006 The 3A resolution structure of recombinant human MAO-B originally determined was of the enzyme complexed with pargyline, an irreversible inhibitor covalently bound to the N5 atom of the flavin coenzyme. 4,6-dinitro-o-cresol 186-192 monoamine oxidase B Homo sapiens 49-54 16820786-4 2006 Significant increases in O(2)(-) production with IFN-gamma were completely abolished by the flavin-containing enzyme inhibitor, diphenyleneiodonium (10 micromol/l), and the Janus-activated kinase (JAK)2 inhibitor, AG490 (100 micromol/l). 4,6-dinitro-o-cresol 92-98 interferon gamma Homo sapiens 49-58 16953568-1 2006 Flavin-binding Kelch repeat F-box (FKF1) protein plays important roles in the photoregulation of flowering in Arabidopsis. 4,6-dinitro-o-cresol 0-6 flavin-binding, kelch repeat, f box 1 Arabidopsis thaliana 35-39 16844764-0 2006 The C-terminal flavin domain of gp91phox bound to plasma membranes of granulocyte-like X-CGD PLB-985 cells is sufficient to anchor cytosolic oxidase components and support NADPH oxidase-associated diaphorase activity independent of cytosolic phospholipase A2 regulation. 4,6-dinitro-o-cresol 15-21 cytochrome b-245 beta chain Homo sapiens 32-40 16844764-0 2006 The C-terminal flavin domain of gp91phox bound to plasma membranes of granulocyte-like X-CGD PLB-985 cells is sufficient to anchor cytosolic oxidase components and support NADPH oxidase-associated diaphorase activity independent of cytosolic phospholipase A2 regulation. 4,6-dinitro-o-cresol 15-21 phospholipase A2 group IVA Homo sapiens 232-258 16844764-8 2006 Therefore, the assembled membrane-bound oxidase complex encompassing the flavin domain of gp91(phox) provides a docking site for cPLA(2) but is not the site of AA-based regulation of oxidase activity. 4,6-dinitro-o-cresol 73-79 pleckstrin Homo sapiens 95-99 16844764-8 2006 Therefore, the assembled membrane-bound oxidase complex encompassing the flavin domain of gp91(phox) provides a docking site for cPLA(2) but is not the site of AA-based regulation of oxidase activity. 4,6-dinitro-o-cresol 73-79 phospholipase A2 group IVA Homo sapiens 129-136 16910673-10 2006 On the basis of the crystal structure of the inactivated human enzyme and stopped-flow kinetic studies with two- and four-electron-reduced forms of the unreacted P. falciparum enzyme, a mechanism is proposed which explains naphthoquinone reduction at the flavin of glutathione reductase. 4,6-dinitro-o-cresol 255-261 glutathione-disulfide reductase Homo sapiens 265-286 16609803-0 2006 A lag-phase in the reduction of flavin dependent thymidylate synthase (FDTS) revealed a mechanistic missing link. 4,6-dinitro-o-cresol 32-38 thymidylate synthetase Homo sapiens 49-69 16627894-7 2006 PCL is a membrane-associated flavin-containing lysosomal monooxygenase that metabolizes prenylcysteine to prenyl aldehyde through a completely novel mechanism. 4,6-dinitro-o-cresol 29-35 prenylcysteine oxidase 1 Homo sapiens 0-3 16674058-1 2006 A new flavin catalyst 2 immobilized in an ionic liquid ([BMIm]PF6) was used for the highly selective oxidation of sulfides to sulfoxides by hydrogen peroxide. 4,6-dinitro-o-cresol 6-12 sperm associated antigen 17 Homo sapiens 62-65 16817897-0 2006 Characterization of the flavin association in hexose oxidase from Chondrus crispus. 4,6-dinitro-o-cresol 24-30 CHC_T00009130001 Chondrus crispus 46-60 16609803-1 2006 An unexpected substrate-dependent lag-phase, found in the single turnover reduction of FDTS bound flavin, sheds light on the molecular mechanism of this alternative thymidylate synthase. 4,6-dinitro-o-cresol 98-104 thymidylate synthetase Homo sapiens 165-185 16467939-7 2006 In addition, the calculated rate constants showed a correlation with the rate of reduction of the flavin in MAO-A. 4,6-dinitro-o-cresol 98-104 monoamine oxidase A Homo sapiens 108-113 16418228-10 2006 The action spectrum suggests that a blue/UV-A light photoreceptor with a flavin-based chromophore participates in the HL response of Lhl4 gene expression. 4,6-dinitro-o-cresol 73-79 uncharacterized protein Chlamydomonas reinhardtii 133-137 16605246-1 2006 Current structural results of several flavin-dependent amine oxidizing enzymes including human monoamine oxidases A and B (MAO A and MAO B) show aromatic amino acid residues oriented approximately perpendicular to the flavin ring, suggesting a functional role in catalysis. 4,6-dinitro-o-cresol 38-44 monoamine oxidase A Homo sapiens 95-121 16605246-1 2006 Current structural results of several flavin-dependent amine oxidizing enzymes including human monoamine oxidases A and B (MAO A and MAO B) show aromatic amino acid residues oriented approximately perpendicular to the flavin ring, suggesting a functional role in catalysis. 4,6-dinitro-o-cresol 38-44 monoamine oxidase A Homo sapiens 123-128 16605246-1 2006 Current structural results of several flavin-dependent amine oxidizing enzymes including human monoamine oxidases A and B (MAO A and MAO B) show aromatic amino acid residues oriented approximately perpendicular to the flavin ring, suggesting a functional role in catalysis. 4,6-dinitro-o-cresol 38-44 monoamine oxidase B Homo sapiens 133-138 16605246-2 2006 In the case of human MAO B, two tyrosyl residues (Y398 and Y435) are found in the substrate binding site on the re face of the covalent flavin ring [Binda et al. 4,6-dinitro-o-cresol 136-142 monoamine oxidase B Homo sapiens 21-26 16519537-4 2006 Each of the FMN residues is capable of only one-electron reduction: one from neutral flavosemiquinone to fully reduced flavin (E(m) = 20 mV) and the other from oxidized flavin to flavosemiquinone anion (E(m) = -150 mV). 4,6-dinitro-o-cresol 119-125 formin 1 Homo sapiens 12-15 16519537-4 2006 Each of the FMN residues is capable of only one-electron reduction: one from neutral flavosemiquinone to fully reduced flavin (E(m) = 20 mV) and the other from oxidized flavin to flavosemiquinone anion (E(m) = -150 mV). 4,6-dinitro-o-cresol 169-175 formin 1 Homo sapiens 12-15 16390129-0 2006 Determination of the distance between the two neutral flavin radicals in augmenter of liver regeneration by pulsed ELDOR. 4,6-dinitro-o-cresol 54-60 growth factor, augmenter of liver regeneration Homo sapiens 73-104 16274228-15 2005 The lack of activity results from the failure of the mutants to readily form the out conformation required for flavin reduction by NADPH. 4,6-dinitro-o-cresol 111-117 2,4-dienoyl-CoA reductase 1 Homo sapiens 131-136 17047361-9 2006 LSD1 is a flavin-dependent demethylase of histone H3. 4,6-dinitro-o-cresol 10-16 lysine demethylase 1A Homo sapiens 0-4 17047361-9 2006 LSD1 is a flavin-dependent demethylase of histone H3. 4,6-dinitro-o-cresol 10-16 Histone H3 Caenorhabditis elegans 42-52 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 16234921-3 2005 Distinct oxidative and reductive transitions of bound H4B cofactor occur during catalysis and are associated with distinct redox transitions of the NOS heme and flavin prosthetic groups. 4,6-dinitro-o-cresol 161-167 H4 clustered histone 4 Homo sapiens 54-57 15958387-0 2005 The human apoptosis-inducing protein AMID is an oxidoreductase with a modified flavin cofactor and DNA binding activity. 4,6-dinitro-o-cresol 79-85 thioredoxin reductase 1 Homo sapiens 48-62 15941276-1 2005 Medium-chain acyl-CoA dehydrogenase (MCAD) catalyzes the flavin-dependent oxidation of fatty acyl-CoAs to the corresponding trans-2-enoyl-CoAs. 4,6-dinitro-o-cresol 57-63 acyl-CoA dehydrogenase medium chain Sus scrofa 0-35 15950194-3 2005 Two types of spectral changes, either increasing the absorbance at 510 nm or decreasing it at 495 nm depending on the group nearest to the flavin cofactor, were seen on ligand binding to MAO A. 4,6-dinitro-o-cresol 139-145 monoamine oxidase A Homo sapiens 187-192 15941276-1 2005 Medium-chain acyl-CoA dehydrogenase (MCAD) catalyzes the flavin-dependent oxidation of fatty acyl-CoAs to the corresponding trans-2-enoyl-CoAs. 4,6-dinitro-o-cresol 57-63 acyl-CoA dehydrogenase medium chain Sus scrofa 37-41 15941276-9 2005 The large increase in shielding experienced by the C1 and C3 HD carbons in the HD-CoA/MCAD complex is proposed to arise from the ring current field from the isoalloxazine portion of the flavin cofactor. 4,6-dinitro-o-cresol 186-192 acyl-CoA dehydrogenase medium chain Sus scrofa 86-90 15941276-10 2005 The flavin ring current, which is only present when the enzyme is placed in an external magnetic field, also explains the differences in (13)C NMR chemical shifts for acetoacetyl-CoA when bound as an enolate to MCAD and enoyl-CoA hydratase and is used to rationalize the observation that the line widths of the C1 and C3 resonances are narrower when the ligands are bound to MCAD than when they are free in the protein solution. 4,6-dinitro-o-cresol 4-10 acyl-CoA dehydrogenase medium chain Sus scrofa 211-215 15941276-10 2005 The flavin ring current, which is only present when the enzyme is placed in an external magnetic field, also explains the differences in (13)C NMR chemical shifts for acetoacetyl-CoA when bound as an enolate to MCAD and enoyl-CoA hydratase and is used to rationalize the observation that the line widths of the C1 and C3 resonances are narrower when the ligands are bound to MCAD than when they are free in the protein solution. 4,6-dinitro-o-cresol 4-10 acyl-CoA dehydrogenase medium chain Sus scrofa 375-379 15811342-0 2005 Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process. 4,6-dinitro-o-cresol 45-51 lysine demethylase 1A Homo sapiens 35-39 15795226-3 2005 Dihydroorotate dehydrogenase (DHODH) is a flavin-dependent mitochondrial enzyme that catalyzes the fourth reaction in this essential pathway. 4,6-dinitro-o-cresol 42-48 dihydroorotate dehydrogenase (quinone) Homo sapiens 30-35 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 family 2 subfamily B member 6 Homo sapiens 0-12 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 15578214-0 2005 Cellular re-distribution of flavin-containing polyamine oxidase in differentiating root and mesocotyl of Zea mays L. seedlings. 4,6-dinitro-o-cresol 28-34 polyamine oxidase 1 Zea mays 46-63 15811342-4 2005 LSD1 converts oxygen to hydrogen peroxide although this reactivity is not as pronounced as that of other flavin-dependent oxidases. 4,6-dinitro-o-cresol 105-111 lysine demethylase 1A Homo sapiens 0-4 15734916-3 2005 Full-length cDNAs have been obtained encoding orthologs of CIRCADIAN CLOCK-ASSOCIATED1 (CCA1)/LATE ELONGATED HYPOCOTYL (LHY), TIMING OF CAB EXPRESSION1 (TOC1), EARLY FLOWERING4 (ELF4), ZEITLUPE (ZTL), FLAVIN-BINDING KELCH REPEAT F-BOX1 (FKF1), EARLY FLOWERING3 (ELF3), and a partial cDNA encoding GIGANTEA in the model stress-inducible CAM plant, Mesembryanthemum crystallinum (Common Ice Plant). 4,6-dinitro-o-cresol 201-207 circadian clock associated 1 Arabidopsis thaliana 88-92 15962105-4 2005 The crucial flavin-containing catalytic subunits, Nox1 and Nox4, are not found in leucocytes, but are highly expressed in vascular cells and upregulated with vascular remodeling, such as that found in hypertension and atherosclerosis. 4,6-dinitro-o-cresol 12-18 NADPH oxidase 1 Homo sapiens 50-54 15962105-4 2005 The crucial flavin-containing catalytic subunits, Nox1 and Nox4, are not found in leucocytes, but are highly expressed in vascular cells and upregulated with vascular remodeling, such as that found in hypertension and atherosclerosis. 4,6-dinitro-o-cresol 12-18 NADPH oxidase 4 Homo sapiens 59-63 15454452-3 2004 These results suggest that the rapid depolarization in wild-type GR originates from an interaction with the flavin-shielding tyrosine, and not from restricted reorientational motion of the flavin. 4,6-dinitro-o-cresol 108-114 glutathione-disulfide reductase Homo sapiens 65-67 15710392-1 2005 Flavin-binding, Kelch repeat, F-box (FKF1) protein is a photoreceptor to regulate flowering of Arabidopsis. 4,6-dinitro-o-cresol 0-6 flavin-binding, kelch repeat, f box 1 Arabidopsis thaliana 37-41 15366957-0 2004 Reduction of methemoglobin via electron transfer from photoreduced flavin: restoration of O2-binding of concentrated hemoglobin solution coencapsulated in phospholipid vesicles. 4,6-dinitro-o-cresol 67-73 hemoglobin subunit gamma 2 Homo sapiens 13-26 15454452-0 2004 Evidence for a novel mechanism of time-resolved flavin fluorescence depolarization in glutathione reductase. 4,6-dinitro-o-cresol 48-54 glutathione-disulfide reductase Homo sapiens 86-107 15454452-1 2004 Time-resolved flavin fluorescence anisotropy studies on glutathione reductase (GR) have revealed a remarkable new phenomenon: wild-type GR displays a rapid process of fluorescence depolarization, that is absent in mutant enzymes lacking a nearby tyrosine residue that blocks the NADPH-binding cleft. 4,6-dinitro-o-cresol 14-20 glutathione-disulfide reductase Homo sapiens 56-77 15454452-1 2004 Time-resolved flavin fluorescence anisotropy studies on glutathione reductase (GR) have revealed a remarkable new phenomenon: wild-type GR displays a rapid process of fluorescence depolarization, that is absent in mutant enzymes lacking a nearby tyrosine residue that blocks the NADPH-binding cleft. 4,6-dinitro-o-cresol 14-20 glutathione-disulfide reductase Homo sapiens 79-81 15454452-1 2004 Time-resolved flavin fluorescence anisotropy studies on glutathione reductase (GR) have revealed a remarkable new phenomenon: wild-type GR displays a rapid process of fluorescence depolarization, that is absent in mutant enzymes lacking a nearby tyrosine residue that blocks the NADPH-binding cleft. 4,6-dinitro-o-cresol 14-20 glutathione-disulfide reductase Homo sapiens 136-138 15447919-10 2004 CONCLUSION: Thyroid status affects the phenotypic expression of the MTHFR 677C-->T polymorphism, possibly by modifying the availability of flavin cofactors. 4,6-dinitro-o-cresol 142-148 methylenetetrahydrofolate reductase Homo sapiens 68-73 15301527-0 2004 Mechanistic studies of a flavin-dependent thymidylate synthase. 4,6-dinitro-o-cresol 25-31 thymidylate synthetase Homo sapiens 42-62 15180983-3 2004 Here we characterized the F1395S mutant of the nNOS flavoprotein domain (nNOSr) regarding its physical properties, NADP(+) binding characteristics, flavin reduction kinetics, steady-state and pre-steady-state cytochrome c reduction kinetics, and ability to shield its FMN cofactor in response to CaM or NADP(H) binding. 4,6-dinitro-o-cresol 148-154 nitric oxide synthase 1 Homo sapiens 47-51 15301527-3 2004 Thy1 encodes flavin-dependent TS (FDTS, previously denoted as TSCP) and shares no sequence homology with classical TS genes. 4,6-dinitro-o-cresol 13-19 Thy-1 cell surface antigen Homo sapiens 0-4 15281155-1 2004 The introduction of a flavin chromophore on the myoglobin (Mb) surface and an effective electron-transfer (ET) reaction through the flavin were successfully achieved by utilizing the self-assembly of heterostranded coiled-coil peptides. 4,6-dinitro-o-cresol 22-28 myoglobin Homo sapiens 48-57 15180991-2 2004 We found that inhibition of flavin- or heme-containing proteins eliminated H(2)O(2)-induced transactivation of the epidermal growth factor receptor and stimulation of its downstream targets, JNK and Akt. 4,6-dinitro-o-cresol 28-34 epidermal growth factor receptor Homo sapiens 115-147 15180991-2 2004 We found that inhibition of flavin- or heme-containing proteins eliminated H(2)O(2)-induced transactivation of the epidermal growth factor receptor and stimulation of its downstream targets, JNK and Akt. 4,6-dinitro-o-cresol 28-34 mitogen-activated protein kinase 8 Homo sapiens 191-194 15180991-2 2004 We found that inhibition of flavin- or heme-containing proteins eliminated H(2)O(2)-induced transactivation of the epidermal growth factor receptor and stimulation of its downstream targets, JNK and Akt. 4,6-dinitro-o-cresol 28-34 AKT serine/threonine kinase 1 Homo sapiens 199-202 15281155-1 2004 The introduction of a flavin chromophore on the myoglobin (Mb) surface and an effective electron-transfer (ET) reaction through the flavin were successfully achieved by utilizing the self-assembly of heterostranded coiled-coil peptides. 4,6-dinitro-o-cresol 132-138 myoglobin Homo sapiens 48-57 14715665-4 2004 The major flavin states are FMN, FMNH., FMNH(2), FAD, FADH., and FADH(2). 4,6-dinitro-o-cresol 10-16 formin 1 Homo sapiens 28-31 15069080-6 2004 S-Nitrosylation of SarDH by NO is best rationalized by a novel mechanism involving the covalently bound flavin of the enzyme. 4,6-dinitro-o-cresol 104-110 sarcosine dehydrogenase Homo sapiens 19-24 14697880-1 2004 The recently published crystal structure of monoamine oxidase (MAO) B was a major breakthrough for structural and functional understanding of flavin containing amine oxidases: it opens a new era of research and provides new opportunities to those interested in the biochemistry and pharmacology of those important drug targets. 4,6-dinitro-o-cresol 142-148 monoamine oxidase B Homo sapiens 44-69 15370067-4 2004 The crucial flavin-containing catalytic subunits Nox1 and Nox4 are not present in leucocytes, but are highly expressed in vascular cells and upregulated in vascular remodeling, such as that found in hypertension and atherosclerosis. 4,6-dinitro-o-cresol 12-18 NADPH oxidase 1 Homo sapiens 49-53 15370067-4 2004 The crucial flavin-containing catalytic subunits Nox1 and Nox4 are not present in leucocytes, but are highly expressed in vascular cells and upregulated in vascular remodeling, such as that found in hypertension and atherosclerosis. 4,6-dinitro-o-cresol 12-18 NADPH oxidase 4 Homo sapiens 58-62 14966111-6 2004 All had slower NADPH-dependent cytochrome c and ferricyanide reductase activities, which were associated with proportionally slower rates of NADPH-dependent flavin reduction in the CaM-free and CaM-bound states. 4,6-dinitro-o-cresol 157-163 cytochrome c, somatic Homo sapiens 31-43 14966111-12 2004 2) Control of flavin reduction is important because it ensures that the rate of heme reduction is sufficiently fast to enable NO synthesis by nNOS. 4,6-dinitro-o-cresol 14-20 nitric oxide synthase 1 Homo sapiens 142-146 15056494-1 2004 The structure of monoamine oxidase B revealed three aromatic amino acid residues within contact distance of the flavin cofactor and a large number of aromatic residues in the substrate binding site. 4,6-dinitro-o-cresol 112-118 monoamine oxidase B Homo sapiens 17-36 14967039-2 2004 In this study, anaerobic redox titrations were employed to determine the midpoint reduction potentials for the flavin cofactors in two highly prevalent polymorphic variants of MSR, I22/L175 and M22/S175. 4,6-dinitro-o-cresol 111-117 5-methyltetrahydrofolate-homocysteine methyltransferase reductase Homo sapiens 176-179 14967039-5 2004 Interestingly, this polymorphism is in the extended linker region between the two flavin domains, which may mediate or facilitate interaction with methionine synthase. 4,6-dinitro-o-cresol 82-88 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 147-166 14717604-8 2004 The observed rate constants associated with flavin reduction are dependent hyperbolically on NADPH and [4(R)-2H]NADPH concentration, and the observed primary kinetic isotope effect on this step is 2.2 and 1.7 for the isolated FAD domain and full-length MSR, respectively. 4,6-dinitro-o-cresol 44-50 5-methyltetrahydrofolate-homocysteine methyltransferase reductase Homo sapiens 253-256 14717604-11 2004 The stopped-flow kinetic data, in conjunction with the reported redox potentials of the flavin cofactors for MSR [Wolthers, K. R., Basran, J., Munro, A. W., and Scrutton, N. S. (2003) Biochemistry, 42, 3911-3920], are used to define the mechanism of electron transfer for the reductive half-reaction of MSR. 4,6-dinitro-o-cresol 88-94 5-methyltetrahydrofolate-homocysteine methyltransferase reductase Homo sapiens 109-112 14697881-6 2004 The normally flat oxidized flavin ring is in a bent, puckered conformation in the MAO B binding site which is suggested to contribute to its reactivity in catalysis. 4,6-dinitro-o-cresol 27-33 monoamine oxidase B Homo sapiens 82-87 14697881-7 2004 This structural information is then used to explain previous studies on flavin analog incorporation into either MAO B or into MAO A. 4,6-dinitro-o-cresol 72-78 monoamine oxidase B Homo sapiens 112-117 14697881-7 2004 This structural information is then used to explain previous studies on flavin analog incorporation into either MAO B or into MAO A. 4,6-dinitro-o-cresol 72-78 monoamine oxidase A Homo sapiens 126-131 12974644-4 2003 Studies with Zn(2+), as a redox inactive surrogate for copper, show that one Zn(2+) binds to four-electron-reduced QSOX by diverting electrons away from the flavin and into two of the three redox active disulfide bridges in the enzyme. 4,6-dinitro-o-cresol 157-163 quiescin sulfhydryl oxidase 1 Homo sapiens 115-119 13129931-11 2003 Our data also challenge the dogma that superoxide production by SDH is a flavin-mediated event rather than a quinone-mediated one. 4,6-dinitro-o-cresol 73-79 succinate dehydrogenase complex iron sulfur subunit B Homo sapiens 64-67 14580199-4 2003 The structures of the flavin-bound RFK obtained by soaking pre-existing crystals were also reported. 4,6-dinitro-o-cresol 22-28 riboflavin kinase Homo sapiens 35-38 14580199-5 2003 Because of crystal packing restraints, these flavin-bound RFK complexes adopt conformations nearly identical with that of corresponding flavin-free structures. 4,6-dinitro-o-cresol 45-51 riboflavin kinase Homo sapiens 58-61 14580199-5 2003 Because of crystal packing restraints, these flavin-bound RFK complexes adopt conformations nearly identical with that of corresponding flavin-free structures. 4,6-dinitro-o-cresol 136-142 riboflavin kinase Homo sapiens 58-61 14692513-1 2003 The interaction between the "electron transferring flavoprotein" (ETF) and medium chain acyl-CoA dehydrogenase (MCAD) enables successful flavin to flavin electron transfer, crucial for the beta-oxidation of fatty acids. 4,6-dinitro-o-cresol 137-143 acyl-CoA dehydrogenase medium chain Homo sapiens 75-110 14692513-1 2003 The interaction between the "electron transferring flavoprotein" (ETF) and medium chain acyl-CoA dehydrogenase (MCAD) enables successful flavin to flavin electron transfer, crucial for the beta-oxidation of fatty acids. 4,6-dinitro-o-cresol 137-143 acyl-CoA dehydrogenase medium chain Homo sapiens 112-116 14692513-1 2003 The interaction between the "electron transferring flavoprotein" (ETF) and medium chain acyl-CoA dehydrogenase (MCAD) enables successful flavin to flavin electron transfer, crucial for the beta-oxidation of fatty acids. 4,6-dinitro-o-cresol 147-153 acyl-CoA dehydrogenase medium chain Homo sapiens 75-110 14692513-1 2003 The interaction between the "electron transferring flavoprotein" (ETF) and medium chain acyl-CoA dehydrogenase (MCAD) enables successful flavin to flavin electron transfer, crucial for the beta-oxidation of fatty acids. 4,6-dinitro-o-cresol 147-153 acyl-CoA dehydrogenase medium chain Homo sapiens 112-116 12968028-10 2003 PheA2 is structurally related to ferric reductase, an NAD(P)H-dependent reductase from the hyperthermophilic Archaea Archaeoglobus fulgidus that catalyzes the flavin-mediated reduction of iron complexes. 4,6-dinitro-o-cresol 159-165 ferric reductase Parageobacillus thermoglucosidasius 33-49 14596603-5 2003 This intermediate is characteristic of a charge-transfer complex of oxidized FMN and an electron-rich donor and is formed prior to full reduction of the flavin. 4,6-dinitro-o-cresol 153-159 formin 1 Homo sapiens 77-80 14587735-0 2003 Model systems for flavoenzyme activity: flavin-functionalised SAMs as models for probing redox modulation through hydrogen bonding. 4,6-dinitro-o-cresol 40-46 methionine adenosyltransferase 1A Homo sapiens 62-66 12913124-7 2003 Inhibition of MAO-B with the clinically used trans-2-phenylcyclopropylamine results in the formation of a covalent C(4a) flavin adduct with an opened cyclopropyl ring and the phenyl ring in a parallel orientation to the flavin. 4,6-dinitro-o-cresol 121-127 monoamine oxidase B Homo sapiens 14-19 12816954-3 2003 Thioredoxin reductase has an N-terminal redox-active disulfide (Cys57-Cys62) adjacent to the flavin and a redox-active C-terminal cysteine pair (Cys489"-Cys490" in the other subunit) that transfer electrons from Cys57-Cys62 to the substrate thioredoxin. 4,6-dinitro-o-cresol 93-99 Thioredoxin reductase-1 Drosophila melanogaster 0-21 12913124-7 2003 Inhibition of MAO-B with the clinically used trans-2-phenylcyclopropylamine results in the formation of a covalent C(4a) flavin adduct with an opened cyclopropyl ring and the phenyl ring in a parallel orientation to the flavin. 4,6-dinitro-o-cresol 220-226 monoamine oxidase B Homo sapiens 14-19 12777376-8 2003 NADPH reduction of the FAD and FMN redox centers by the CaM-bound flavin domains was studied by stopped-flow and rapid scan spectrometry. 4,6-dinitro-o-cresol 66-72 formin 1 Homo sapiens 31-34 12777376-9 2003 Reduction of the air-stable semiquinone (FAD-FMNH*) of both domains with NADPH showed that the extent of conversion of FADH2/FMNH* to FADH*/FMNH2 in the iNOS flavin domain was greater than that of the nNOS flavin domain. 4,6-dinitro-o-cresol 158-164 nitric oxide synthase 1 Homo sapiens 201-205 12777376-9 2003 Reduction of the air-stable semiquinone (FAD-FMNH*) of both domains with NADPH showed that the extent of conversion of FADH2/FMNH* to FADH*/FMNH2 in the iNOS flavin domain was greater than that of the nNOS flavin domain. 4,6-dinitro-o-cresol 206-212 nitric oxide synthase 1 Homo sapiens 201-205 12777376-11 2003 The rate of intramolecular electron transfer between the two flavins in the iNOS flavin domain was faster than that of the nNOS flavin domain. 4,6-dinitro-o-cresol 61-67 nitric oxide synthase 1 Homo sapiens 123-127 12777376-11 2003 The rate of intramolecular electron transfer between the two flavins in the iNOS flavin domain was faster than that of the nNOS flavin domain. 4,6-dinitro-o-cresol 81-87 nitric oxide synthase 1 Homo sapiens 123-127 12667082-0 2003 Molecular dissection of human methionine synthase reductase: determination of the flavin redox potentials in full-length enzyme and isolated flavin-binding domains. 4,6-dinitro-o-cresol 82-88 5-methyltetrahydrofolate-homocysteine methyltransferase reductase Homo sapiens 30-59 12781338-9 2003 These results indicate that the active site of MAO A is far more sensitive to structural variation than would be predicted by the simple flavin stacking model. 4,6-dinitro-o-cresol 137-143 monoamine oxidase A Homo sapiens 47-52 12719523-3 2003 Studies of the plant phototropins have identified 11 flavin-contacting residues that are also conserved in the LOV domains of WC-1, VVD, and FKF1. 4,6-dinitro-o-cresol 53-59 flavin-binding, kelch repeat, f box 1 Arabidopsis thaliana 141-145 12804606-1 2003 The heme and flavin-binding domains of Drosophila nitric oxide synthase (DNOS) were expressed in Escherichia coli using the expression vector pCW. 4,6-dinitro-o-cresol 13-19 Nitric oxide synthase Drosophila melanogaster 50-71 12804606-1 2003 The heme and flavin-binding domains of Drosophila nitric oxide synthase (DNOS) were expressed in Escherichia coli using the expression vector pCW. 4,6-dinitro-o-cresol 13-19 Nitric oxide synthase Drosophila melanogaster 73-77 12667082-0 2003 Molecular dissection of human methionine synthase reductase: determination of the flavin redox potentials in full-length enzyme and isolated flavin-binding domains. 4,6-dinitro-o-cresol 141-147 5-methyltetrahydrofolate-homocysteine methyltransferase reductase Homo sapiens 30-59 12667082-3 2003 MSR and its individual flavin-binding domains were cloned as GST-tagged fusion proteins for expression and purification from Escherichia coli. 4,6-dinitro-o-cresol 23-29 5-methyltetrahydrofolate-homocysteine methyltransferase reductase Homo sapiens 0-3 12667082-4 2003 The isolated flavin domains of MSR retain UV-visible and secondary structural properties indicative of correctly folded flavoproteins. 4,6-dinitro-o-cresol 13-19 5-methyltetrahydrofolate-homocysteine methyltransferase reductase Homo sapiens 31-34 12646269-0 2003 Electron transfer is activated by calmodulin in the flavin domain of human neuronal nitric oxide synthase. 4,6-dinitro-o-cresol 52-58 calmodulin 1 Homo sapiens 34-44 12646269-0 2003 Electron transfer is activated by calmodulin in the flavin domain of human neuronal nitric oxide synthase. 4,6-dinitro-o-cresol 52-58 nitric oxide synthase 1 Homo sapiens 75-105 12646269-1 2003 The objective of this study was to clarify the mechanism of electron transfer in the human neuronal nitric oxide synthase (nNOS) flavin domain using the recombinant human nNOS flavin domains, the FAD/NADPH domain (contains FAD- and NADPH-binding sites), and the FAD/FMN domain (the flavin domain including a calmodulin-binding site). 4,6-dinitro-o-cresol 129-135 nitric oxide synthase 1 Homo sapiens 91-121 12646269-1 2003 The objective of this study was to clarify the mechanism of electron transfer in the human neuronal nitric oxide synthase (nNOS) flavin domain using the recombinant human nNOS flavin domains, the FAD/NADPH domain (contains FAD- and NADPH-binding sites), and the FAD/FMN domain (the flavin domain including a calmodulin-binding site). 4,6-dinitro-o-cresol 129-135 nitric oxide synthase 1 Homo sapiens 123-127 12646269-1 2003 The objective of this study was to clarify the mechanism of electron transfer in the human neuronal nitric oxide synthase (nNOS) flavin domain using the recombinant human nNOS flavin domains, the FAD/NADPH domain (contains FAD- and NADPH-binding sites), and the FAD/FMN domain (the flavin domain including a calmodulin-binding site). 4,6-dinitro-o-cresol 129-135 nitric oxide synthase 1 Homo sapiens 171-175 12646269-1 2003 The objective of this study was to clarify the mechanism of electron transfer in the human neuronal nitric oxide synthase (nNOS) flavin domain using the recombinant human nNOS flavin domains, the FAD/NADPH domain (contains FAD- and NADPH-binding sites), and the FAD/FMN domain (the flavin domain including a calmodulin-binding site). 4,6-dinitro-o-cresol 129-135 formin 1 Homo sapiens 266-269 12646269-1 2003 The objective of this study was to clarify the mechanism of electron transfer in the human neuronal nitric oxide synthase (nNOS) flavin domain using the recombinant human nNOS flavin domains, the FAD/NADPH domain (contains FAD- and NADPH-binding sites), and the FAD/FMN domain (the flavin domain including a calmodulin-binding site). 4,6-dinitro-o-cresol 129-135 calmodulin 1 Homo sapiens 308-318 12646269-1 2003 The objective of this study was to clarify the mechanism of electron transfer in the human neuronal nitric oxide synthase (nNOS) flavin domain using the recombinant human nNOS flavin domains, the FAD/NADPH domain (contains FAD- and NADPH-binding sites), and the FAD/FMN domain (the flavin domain including a calmodulin-binding site). 4,6-dinitro-o-cresol 176-182 nitric oxide synthase 1 Homo sapiens 91-121 12646269-1 2003 The objective of this study was to clarify the mechanism of electron transfer in the human neuronal nitric oxide synthase (nNOS) flavin domain using the recombinant human nNOS flavin domains, the FAD/NADPH domain (contains FAD- and NADPH-binding sites), and the FAD/FMN domain (the flavin domain including a calmodulin-binding site). 4,6-dinitro-o-cresol 176-182 nitric oxide synthase 1 Homo sapiens 123-127 12646269-1 2003 The objective of this study was to clarify the mechanism of electron transfer in the human neuronal nitric oxide synthase (nNOS) flavin domain using the recombinant human nNOS flavin domains, the FAD/NADPH domain (contains FAD- and NADPH-binding sites), and the FAD/FMN domain (the flavin domain including a calmodulin-binding site). 4,6-dinitro-o-cresol 176-182 nitric oxide synthase 1 Homo sapiens 91-121 12646269-1 2003 The objective of this study was to clarify the mechanism of electron transfer in the human neuronal nitric oxide synthase (nNOS) flavin domain using the recombinant human nNOS flavin domains, the FAD/NADPH domain (contains FAD- and NADPH-binding sites), and the FAD/FMN domain (the flavin domain including a calmodulin-binding site). 4,6-dinitro-o-cresol 176-182 nitric oxide synthase 1 Homo sapiens 123-127 12627958-5 2003 We find that hCRY2 exhibits fluorescence properties consistent with the presence of folate and flavin cofactors. 4,6-dinitro-o-cresol 95-101 cryptochrome circadian regulator 2 Homo sapiens 13-18 12658512-3 2003 CDH, containing a protease-sensitive linker region, can be cleaved by endogenous proteases into a catalytically active flavin fragment and an inactive heme domain. 4,6-dinitro-o-cresol 119-125 choline dehydrogenase Homo sapiens 0-3 12127078-1 2002 Natural substrate/product binding activates medium-chain acyl-CoA dehydrogenase (MCAD) to accept electrons from its substrate by inducing a positive flavin midpoint potential shift. 4,6-dinitro-o-cresol 149-155 acyl-CoA dehydrogenase medium chain Homo sapiens 44-79 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 NADPH dependent diflavin oxidoreductase 1 Homo sapiens 42-45 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 12623014-1 2003 Riboflavin kinase (RFK) is an essential enzyme catalyzing the phosphorylation of riboflavin (vitamin B(2)) to form FMN, an obligatory step in vitamin B(2) utilization and flavin cofactor synthesis. 4,6-dinitro-o-cresol 4-10 riboflavin kinase Homo sapiens 19-22 12445480-5 2002 The inhibitors, D-amphetamine, harmine, tetrindole, and befloxatone all induce similar (but not identical) changes in the spectrum of MAO A, consistent with stacking of inhibitor with the flavin in the active site. 4,6-dinitro-o-cresol 188-194 monoamine oxidase A Homo sapiens 134-139 12612135-3 2003 Here, human lymphoid cells (Jurkat cells) were used to model effects of cellular flavin supply on secretion of IL-2 (containing one disulfide bond) and cellular stress response. 4,6-dinitro-o-cresol 81-87 interleukin 2 Homo sapiens 111-115 12527797-4 2003 The flavin content of the expressed enzyme was consistent with immunodetectable dFMO1 protein levels. 4,6-dinitro-o-cresol 4-10 Flavin-containing monooxygenase 1 Drosophila melanogaster 80-85 12371853-9 2002 At the same time, the parent 3-phenyl analogue is a pure substrate for the flavin-dependent mitochondrial monoamine oxidase B from bovine liver. 4,6-dinitro-o-cresol 75-81 monoamine oxidase B Bos taurus 106-125 12359075-3 2002 All the expressed forms contained flavin, of which the semiquinone form was stable during dithionite titration after dithiothreitol treatment, indicating that the flavin domains of all the expressed molecules have the intact conformations interconvertible between NAD(+)-dependent dehydrogenase (XDH) and O(2)-dependent oxidase (XO) types. 4,6-dinitro-o-cresol 163-169 xanthine dehydrogenase Rattus norvegicus 296-299 12127078-1 2002 Natural substrate/product binding activates medium-chain acyl-CoA dehydrogenase (MCAD) to accept electrons from its substrate by inducing a positive flavin midpoint potential shift. 4,6-dinitro-o-cresol 149-155 acyl-CoA dehydrogenase medium chain Homo sapiens 81-85 11872165-7 2002 The flavin ring of FAD resides at the active site with its si-face attached to the beta-domain, and is surrounded by active-site residues in a mode similar to that found in MCAD. 4,6-dinitro-o-cresol 4-10 acyl-CoA dehydrogenase medium chain Rattus norvegicus 173-177 12214662-4 2002 The mechanism of FMO 1, 2, 3, and 4 are similar and differences in the substrate specificities of these isoforms can be attributed almost entirely to differences in the dimensions of the cleft or channel limiting access to the 4a-hydroperoxy flavin. 4,6-dinitro-o-cresol 242-248 flavin containing dimethylaniline monoxygenase 1 Sus scrofa 17-28 12009436-0 2002 Flavin photochemistry in the analysis of electron transfer reactions: role of charged and hydrophobic residues at the carboxyl terminus of ferredoxin-NADP(+) reductase in the interaction with its substrates. 4,6-dinitro-o-cresol 0-6 ferredoxin reductase Homo sapiens 139-167 11913972-3 2002 Sequence analysis indicated the heme and flavin domains were directly analogous to the corresponding domains in microsomal cytochrome b(5) (cb5) and cytochrome b(5) reductase (cb5r), respectively. 4,6-dinitro-o-cresol 41-47 cytochrome b5 type A Rattus norvegicus 123-138 11913972-3 2002 Sequence analysis indicated the heme and flavin domains were directly analogous to the corresponding domains in microsomal cytochrome b(5) (cb5) and cytochrome b(5) reductase (cb5r), respectively. 4,6-dinitro-o-cresol 41-47 cytochrome b5 type A Rattus norvegicus 140-143 11913972-3 2002 Sequence analysis indicated the heme and flavin domains were directly analogous to the corresponding domains in microsomal cytochrome b(5) (cb5) and cytochrome b(5) reductase (cb5r), respectively. 4,6-dinitro-o-cresol 41-47 cytochrome b5 type A Rattus norvegicus 149-164 12076317-8 2002 The results of the present study suggest that (i) delta-aminolevulinate dehydratase is a potential molecular target for phenyl selenoacetylene, due to the oxidation of enzyme sulfhydryl groups, and that (ii) the monooxygenation of this selenocompound, which in vivo could be possibly mediated by flavin-containing monooxigenases, increases its inhibitory effect. 4,6-dinitro-o-cresol 296-302 aminolevulinate dehydratase Homo sapiens 50-83 11872165-8 2002 However, the residues have weak interactions with the flavin ring due to the loss of some of the important hydrogen bonds with the flavin ring found in MCAD. 4,6-dinitro-o-cresol 54-60 acyl-CoA dehydrogenase medium chain Rattus norvegicus 152-156 11872165-8 2002 However, the residues have weak interactions with the flavin ring due to the loss of some of the important hydrogen bonds with the flavin ring found in MCAD. 4,6-dinitro-o-cresol 131-137 acyl-CoA dehydrogenase medium chain Rattus norvegicus 152-156 11872165-10 2002 The pyrimidine moiety of flavin is exposed to the solvent and can readily be attacked by molecular oxygen, while that in MCAD is protected from the solvent. 4,6-dinitro-o-cresol 25-31 acyl-CoA dehydrogenase medium chain Rattus norvegicus 121-125 11805294-1 2002 The light-induced electron transfer reaction of flavin cofactor photoactivation in Xenopus laevis (6-4) photolyase has been studied by continuous-wave and time-resolved electron paramagnetic resonance spectroscopy. 4,6-dinitro-o-cresol 48-54 6-4 photolyase Xenopus laevis 99-114 11747820-0 2001 A putative flavin electron transport pathway is differentially utilized in Xenopus CRY1 and CRY2. 4,6-dinitro-o-cresol 11-17 cryptochrome 4 L homeolog Xenopus laevis 83-87 11754736-0 2002 Effects of hydrogen bonds in association with flavin and substrate in flavoenzyme d-amino acid oxidase. 4,6-dinitro-o-cresol 46-52 D-amino acid oxidase Homo sapiens 82-102 11754736-2 2002 According to the three-dimensional structure of a porcine kidney D-amino acid oxidase-substrate (D-leucine) complex model, the G313 backbone carbonyl recognizes the substrate amino group by hydrogen bonding and the side-chain hydroxyl of T317 forms a hydrogen bond with C(2)=O of the flavin moiety of FAD [Miura et al. 4,6-dinitro-o-cresol 284-290 D-amino acid oxidase Homo sapiens 65-85 11836476-1 2002 Two blue light receptors in Arabidopsis, termed phot1 and phot2, which contain flavin chromophores and have intrinsic protein kinase activity, participate in several physiological processes. 4,6-dinitro-o-cresol 79-85 phototropin 1 Arabidopsis thaliana 48-53 11836476-1 2002 Two blue light receptors in Arabidopsis, termed phot1 and phot2, which contain flavin chromophores and have intrinsic protein kinase activity, participate in several physiological processes. 4,6-dinitro-o-cresol 79-85 phototropin 2 Arabidopsis thaliana 58-63 11788419-10 2002 These increases in superoxide were markedly reduced in the presence of polyethylene glycol-superoxide dismutase (300 U/ml) or diphenylene iodonium [0.1 mM, an inhibitor of flavin-containing enzymes, including NAD(P)H oxidase] but were not affected by indomethacin, N(G)-nitro-L-arginine, or allopurinol. 4,6-dinitro-o-cresol 172-178 NADPH oxidase 1 Oryctolagus cuniculus 209-224 11788419-11 2002 These data suggest that NADH- and NADPH-induced changes in cerebral vascular tone are mediated by superoxide, produced by a flavin-containing enzyme, most likely NAD(P)H oxidase, but not xanthine oxidase or nitric oxide synthase. 4,6-dinitro-o-cresol 124-130 NADPH oxidase 1 Oryctolagus cuniculus 162-177 11818067-5 2002 Using site-directed mutagenesis, three of the four conserved flavin binding residues in dCRY were found to be essential for light responses, whereas three of the four corresponding residues in mCRY1 did not abolish transcriptional responses. 4,6-dinitro-o-cresol 61-67 cryptochrome Drosophila melanogaster 88-92 11747820-0 2001 A putative flavin electron transport pathway is differentially utilized in Xenopus CRY1 and CRY2. 4,6-dinitro-o-cresol 11-17 cryptochrome circadian regulator 2 S homeolog Xenopus laevis 92-96 11747820-8 2001 Both CRYs seem to require an intact flavin binding domain, suggesting that electron transport is important in their ability to suppress CLOCK/BMAL1 activation. 4,6-dinitro-o-cresol 36-42 aryl hydrocarbon receptor nuclear translocator like L homeolog Xenopus laevis 142-147 11577105-2 2001 To elucidate the function of the flavin si-face tyrosine (Tyr-89 in pea FNR) on the enzyme structure and catalysis, we performed ab initio molecular orbital calculations and site-directed mutagenesis. 4,6-dinitro-o-cresol 33-39 ferredoxin reductase Homo sapiens 72-75 11577105-3 2001 Our results indicate that the position of Tyr-89 in pea FNR is mainly governed by the energetic minimum of the pairwise interaction between the phenol ring and the flavin. 4,6-dinitro-o-cresol 164-170 ferredoxin reductase Homo sapiens 56-59 11577105-4 2001 Moreover, most of FNR-like proteins displayed geometries for the si-face tyrosine phenol and the flavin, which correspond to the more negative free energy theoretical value. 4,6-dinitro-o-cresol 97-103 ferredoxin reductase Homo sapiens 18-21 11583577-0 2001 Effects of environment on flavin reactivity in morphinone reductase: analysis of enzymes displaying differential charge near the N-1 atom and C-2 carbonyl region of the active-site flavin. 4,6-dinitro-o-cresol 181-187 complement C2 Homo sapiens 142-145 11676611-1 2001 A gene has been constructed coding for a unique fusion protein, NADH:cytochrome c reductase, that comprises the soluble heme-containing domain of rat hepatic cytochrome b(5) as the amino-terminal portion of the protein and the soluble flavin-containing domain of rat hepatic cytochrome b(5) reductase as the carboxyl terminus. 4,6-dinitro-o-cresol 235-241 cytochrome b, mitochondrial Rattus norvegicus 158-170 11676611-8 2001 This work represents the first successful bacterial expression of a soluble, catalytically competent, rat hepatic cytochrome b(5)-cytochrome b(5) reductase fusion protein that retains the functional properties characteristic of the individual heme and flavin domain. 4,6-dinitro-o-cresol 252-258 cytochrome b, mitochondrial Rattus norvegicus 114-126 11676611-8 2001 This work represents the first successful bacterial expression of a soluble, catalytically competent, rat hepatic cytochrome b(5)-cytochrome b(5) reductase fusion protein that retains the functional properties characteristic of the individual heme and flavin domain. 4,6-dinitro-o-cresol 252-258 cytochrome b, mitochondrial Rattus norvegicus 130-142 11518705-5 2001 Kinetic difference spectra for nNOS reduction indicated that the second phase consisted of heme reoxidation accompanied by formation of a neutral flavin semiquinone, suggesting that it is heme to flavin electron transfer. 4,6-dinitro-o-cresol 146-152 nitric oxide synthase 1 Rattus norvegicus 31-35 11591145-1 2001 The medium chain acyl-CoA dehydrogenase is rapidly inhibited by racemic 3,4-dienoyl-CoA derivatives with a stoichiometry of two molecules of racemate per enzyme flavin. 4,6-dinitro-o-cresol 161-167 acyl-CoA dehydrogenase medium chain Homo sapiens 4-39 11765140-17 2001 One is enzymatic reduction by aldehyde oxidase; the other is non-enzymatic reduction catalysed by the haem group of catalase in the presence of reduced flavin. 4,6-dinitro-o-cresol 152-158 catalase Oryctolagus cuniculus 116-124 11583577-3 2001 The positioning of a positively charged side chain in the N-1/C-2 carbonyl region of protein-bound flavin is common to many flavoprotein enzymes. 4,6-dinitro-o-cresol 99-105 complement C2 Homo sapiens 62-65 11583577-10 2001 The data indicate, in contrast with dogma, that the presence of a positively charged side chain close to the N-1/C-2 carbonyl region of the flavin in MR is not required to stabilize the reduced flavin. 4,6-dinitro-o-cresol 140-146 complement C2 Homo sapiens 113-116 11761328-4 2001 Current knowledge on the mechanism of covalent flavin attachment is discussed based on studies on the 8alpha-S-cysteinylFAD of monoamine oxidases A and B, as well as studies on other flavoenzymes. 4,6-dinitro-o-cresol 47-53 monoamine oxidase A Homo sapiens 127-153 11473123-3 2001 The reductase domain, similar to NADPH-cytochrome P450 reductase, can be further divided into two different flavin-containing domains: (a) the N terminus, FMN-containing portion, and (b) the C terminus FAD- and NADPH-binding portion. 4,6-dinitro-o-cresol 108-114 cytochrome p450 oxidoreductase Rattus norvegicus 33-64 11473123-7 2001 A comparison of the structure of the neuronal NOS FAD/NADPH domain and CYPOR reveals the strict conservation of the flavin-binding site, including the tightly bound water molecules, the mode of NADP(+) binding, and the aromatic residue that lies at the re-face of the flavin ring, strongly suggesting that the hydride transfer mechanisms in the two enzymes are very similar. 4,6-dinitro-o-cresol 116-122 cytochrome p450 oxidoreductase Rattus norvegicus 71-76 11473123-7 2001 A comparison of the structure of the neuronal NOS FAD/NADPH domain and CYPOR reveals the strict conservation of the flavin-binding site, including the tightly bound water molecules, the mode of NADP(+) binding, and the aromatic residue that lies at the re-face of the flavin ring, strongly suggesting that the hydride transfer mechanisms in the two enzymes are very similar. 4,6-dinitro-o-cresol 268-274 cytochrome p450 oxidoreductase Rattus norvegicus 71-76 11473123-8 2001 In contrast, the putative FMN domain-binding surface of the NOS protein is less positively charged than that of its CYPOR counterpart, indicating a different nature of interactions between the two flavin domains and a different mode of regulation in electron transfer between the two flavins involving the autoinhibitory element and the C-terminal 33 residues, both of which are absent in CYPOR. 4,6-dinitro-o-cresol 197-203 cytochrome p450 oxidoreductase Rattus norvegicus 116-121 11473123-8 2001 In contrast, the putative FMN domain-binding surface of the NOS protein is less positively charged than that of its CYPOR counterpart, indicating a different nature of interactions between the two flavin domains and a different mode of regulation in electron transfer between the two flavins involving the autoinhibitory element and the C-terminal 33 residues, both of which are absent in CYPOR. 4,6-dinitro-o-cresol 197-203 cytochrome p450 oxidoreductase Rattus norvegicus 389-394 11279129-3 2001 EpiD, Dfp, and AtHAL3a are members of the homo-oligomeric flavin-containing Cys decarboxylase (HFCD) protein family. 4,6-dinitro-o-cresol 58-64 HAL3-like protein A Arabidopsis thaliana 15-22 11375751-5 2001 This redox cycling mechanism involves the reduction of MPP+ by a number of enzymes, especially flavin containing enzymes, some of which are found in mitochondria. 4,6-dinitro-o-cresol 95-101 M-phase phosphoprotein 6 Homo sapiens 55-58 11574067-0 2001 Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on protein stability and catalysis. 4,6-dinitro-o-cresol 11-17 cytochrome b5 type A Homo sapiens 65-78 11574067-1 2001 Porcine NADH-cytochrome b5 reductase catalytic domain (Pb5R) has the RXY(T/S)+(T/S) flavin-binding motif that is highly conserved among the structurally related family of flavoprotein reductases. 4,6-dinitro-o-cresol 84-90 cytochrome b5 type A Homo sapiens 13-26 11676020-4 2001 The absorption spectrum of rCDH shows that the protein contains one flavin and one heme cofactor per protein molecule, as does wtCDH. 4,6-dinitro-o-cresol 68-74 choline dehydrogenase Rattus norvegicus 27-31 11358972-2 2001 Dfp proteins, LanD proteins (for example EpiD, which is involved in epidermin biosynthesis), and the salt tolerance protein AtHAL3a from Arabidopsis thaliana are homooligomeric flavin-containing Cys decarboxylases (HFCD protein family). 4,6-dinitro-o-cresol 177-183 HAL3-like protein A Arabidopsis thaliana 124-130 11425554-0 2001 Inactivation of monoamine oxidase B by 1-phenylcyclopropylamine: mass spectral evidence for the flavin adduct. 4,6-dinitro-o-cresol 96-102 monoamine oxidase B Bos taurus 16-35 11325964-2 2001 Activity requires dimeric interaction between two oxygenase domains and calmodulin binding between the reductase and oxygenase domains, which triggers electron transfer between flavin and heme groups. 4,6-dinitro-o-cresol 177-183 calmodulin 1 Rattus norvegicus 72-82 11325964-9 2001 This reveals an active involvement of calmodulin in supporting transelectron transfer between flavin and heme groups on adjacent subunits in nNOS. 4,6-dinitro-o-cresol 94-100 calmodulin 1 Rattus norvegicus 38-48 11325964-9 2001 This reveals an active involvement of calmodulin in supporting transelectron transfer between flavin and heme groups on adjacent subunits in nNOS. 4,6-dinitro-o-cresol 94-100 nitric oxide synthase 1 Rattus norvegicus 141-145 11534062-1 2000 The acid phosphatase locus 1 (ACP1) codes for a low molecular weight phosphotyrosine protein phosphatase that has the important action of dephosphorylating tyrosine phosphorylated proteins and peptides and a second important role in modulating flavin cofactor levels and the activity of flavo-enzymes. 4,6-dinitro-o-cresol 244-250 acid phosphatase 1 Homo sapiens 4-28 11331009-1 2001 The spectral properties of the covalent adduct formed between the flavin cofactor of MAO N and 1-PCPA are similar to those reported for the irreversible inactivation product formed with 1-PCPA and mammalian mitochondrial monoamine oxidase B [Silverman, R. B., and Zieske, P. A. 4,6-dinitro-o-cresol 66-72 monoamine oxidase B Homo sapiens 221-240 11331018-0 2001 Determination of the midpoint potential of the FAD and FMN flavin cofactors and of the 3Fe-4S cluster of glutamate synthase. 4,6-dinitro-o-cresol 59-65 formin 1 Homo sapiens 55-58 11258887-2 2001 The active site of PAO consists of a 30 A long U-shaped catalytic tunnel, whose innermost part is located in front of the flavin ring. 4,6-dinitro-o-cresol 122-128 polyamine oxidase 1 Zea mays 19-22 11371007-4 2001 Our findings imply that the binding of NADP+ and AADP+ at the NADP(H)-binding site of A. thaliana TR, and/or the binding of TRX in the vicinity of the catalytic disulfide increase the content of fluorescent FR conformer (NADP(H)-binding site adjacent to flavin). 4,6-dinitro-o-cresol 254-260 thioredoxin H-type 1 Arabidopsis thaliana 124-127 11368012-8 2001 In stopped-flow kinetics experiments, the flavin reduction (approximately 90 s(-1)) and heme reduction (approximately 9 s(-1)) phases of the monooxygenase reaction of CYP4A7 were not altered by the presence of cytochrome b5. 4,6-dinitro-o-cresol 42-48 cytochrome P450 4A7 Oryctolagus cuniculus 167-173 11334263-14 2001 The N-oxide reduction appears to proceed non-enzymatically, catalysed by the haem group of cytochrome P450 in the presence of a reduced flavin. 4,6-dinitro-o-cresol 136-142 cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus 91-106 11005854-4 2000 Cleavage of surface-exposed loops of XDH causes major structural rearrangement of another loop close to the flavin ring (Gln 423Lys 433). 4,6-dinitro-o-cresol 108-114 xanthine dehydrogenase Bos taurus 37-40 11371181-7 2001 Reoxidation of the reduced flavin by CH(2)-H(4)folate is substantially rate limiting in the physiological NADH-CH(2)-H(4)folate oxidoreductase reaction. 4,6-dinitro-o-cresol 27-33 oxidoreductase Escherichia coli 128-142 11371181-8 2001 In the NADH-menadione oxidoreductase reaction, the reduction of the flavin by NADH is rate limiting as is the reduction of flavin by CH(3)-H(4)folate in the CH(3)-H(4)folate-menadione oxidoreductase reaction. 4,6-dinitro-o-cresol 68-74 oxidoreductase Escherichia coli 22-36 11371181-8 2001 In the NADH-menadione oxidoreductase reaction, the reduction of the flavin by NADH is rate limiting as is the reduction of flavin by CH(3)-H(4)folate in the CH(3)-H(4)folate-menadione oxidoreductase reaction. 4,6-dinitro-o-cresol 68-74 oxidoreductase Escherichia coli 184-198 11371181-8 2001 In the NADH-menadione oxidoreductase reaction, the reduction of the flavin by NADH is rate limiting as is the reduction of flavin by CH(3)-H(4)folate in the CH(3)-H(4)folate-menadione oxidoreductase reaction. 4,6-dinitro-o-cresol 123-129 oxidoreductase Escherichia coli 22-36 11371181-8 2001 In the NADH-menadione oxidoreductase reaction, the reduction of the flavin by NADH is rate limiting as is the reduction of flavin by CH(3)-H(4)folate in the CH(3)-H(4)folate-menadione oxidoreductase reaction. 4,6-dinitro-o-cresol 123-129 oxidoreductase Escherichia coli 184-198 11266081-0 2001 A novel deletion in the flavin-containing monooxygenase gene (FMO3) in a Greek patient with trimethylaminuria. 4,6-dinitro-o-cresol 24-30 flavin containing dimethylaniline monoxygenase 3 Homo sapiens 62-66 11266081-1 2001 Mutations of the flavin-containing monooxygenase type 3 gene (FMO3) that encode the major functional form present in adult human liver, have been shown to cause trimethylaminuria. 4,6-dinitro-o-cresol 17-23 flavin containing dimethylaniline monoxygenase 3 Homo sapiens 62-66 11329262-4 2001 Each flavin titrates through a blue semiquinone state, with the FMN semiquinone being most intense due to larger separation (approximately 200 mV) of its two couples. 4,6-dinitro-o-cresol 5-11 formin 1 Homo sapiens 64-67 11038355-6 2001 Reductase activity and two catalytic parameters (speed and amount of heme-NO complex formation) related directly to the speed of flavin and heme reduction. 4,6-dinitro-o-cresol 129-135 chalcone reductase CHR1 Glycine max 0-9 10871625-0 2000 The C termini of constitutive nitric-oxide synthases control electron flow through the flavin and heme domains and affect modulation by calmodulin. 4,6-dinitro-o-cresol 87-93 calmodulin 1 Homo sapiens 136-146 11534062-1 2000 The acid phosphatase locus 1 (ACP1) codes for a low molecular weight phosphotyrosine protein phosphatase that has the important action of dephosphorylating tyrosine phosphorylated proteins and peptides and a second important role in modulating flavin cofactor levels and the activity of flavo-enzymes. 4,6-dinitro-o-cresol 244-250 acid phosphatase 1 Homo sapiens 30-34 10973923-2 2000 We previously reported on the ability of TGF-beta1 to activate a cell surface-associated NADH:flavin:O(2) oxidoreductase (NADH oxidase) that generates extracellular H(2)O(2). 4,6-dinitro-o-cresol 94-100 transforming growth factor beta 1 Homo sapiens 41-50 11019818-1 2000 Squalene epoxidase (SE) (EC 1.14.99.7) is a flavin-requiring, non-cytochrome P-450 oxidase that catalyzes the conversion of squalene to (3S)-2,3-oxidosqualene. 4,6-dinitro-o-cresol 44-50 squalene epoxidase Rattus norvegicus 0-18 10950853-2 2000 This major metabolite has been demonstrated to be further metabolized predominately by the flavin-containing monooxygenases (FMOs) to the secondary hydroxylamine, N-deacetyl-N-hydroxyketoconazole (N-hydroxy-DAK) by adult and postnatal rat hepatic microsomes. 4,6-dinitro-o-cresol 91-97 triokinase and FMN cyclase Rattus norvegicus 207-210 10924112-12 2000 We conclude that the flavin of ETF does not penetrate fully the groove on the surface of TMADH, and that electron transfer from the 4Fe-4S center to ETF may involve a longer pathway involving Tyr-442. 4,6-dinitro-o-cresol 21-27 TEA domain transcription factor 2 Homo sapiens 31-34 10920257-10 2000 The largest factor in the substantially low pK(a) of reduced flavin in DAO is probably the steric hindrance between the hydrogen atom of H-N(1)(flavin) and the hydrogen atom of H-N of Gly315, which becomes significant when a hydrogen is bound to N(1) of flavin. 4,6-dinitro-o-cresol 61-67 D-amino acid oxidase Homo sapiens 71-74 10900176-9 2000 These data suggest that flavin binding proteins such as NADH/NADPH oxidase can regulate VCAM-1 gene expression independent of NF- kappa B. 4,6-dinitro-o-cresol 24-30 vascular cell adhesion molecule 1 Homo sapiens 88-94 10931200-12 2000 31P-NMR measurements show that the phosphate geometry has changed in enzyme bound FMN compared to the free flavin in water, indicating a strong interaction of the phosphate group with the apoenzyme. 4,6-dinitro-o-cresol 107-113 formin 1 Homo sapiens 82-85 10900176-0 2000 NF- kappa B independent suppression of endothelial vascular cell adhesion molecule-1 and intercellular adhesion molecule-1 gene expression by inhibition of flavin binding proteins and superoxide production. 4,6-dinitro-o-cresol 156-162 nuclear factor kappa B subunit 1 Homo sapiens 0-11 10900176-0 2000 NF- kappa B independent suppression of endothelial vascular cell adhesion molecule-1 and intercellular adhesion molecule-1 gene expression by inhibition of flavin binding proteins and superoxide production. 4,6-dinitro-o-cresol 156-162 vascular cell adhesion molecule 1 Homo sapiens 51-84 10900176-0 2000 NF- kappa B independent suppression of endothelial vascular cell adhesion molecule-1 and intercellular adhesion molecule-1 gene expression by inhibition of flavin binding proteins and superoxide production. 4,6-dinitro-o-cresol 156-162 intercellular adhesion molecule 1 Homo sapiens 89-122 10900176-3 2000 We explored the role of flavin containing proteins such as NADH/NADPH oxidase in the induction of vascular cell adhesion molecule-1 (VCAM-1) and intercellular adhesion molecule-1 (ICAM-1) gene expression in human aortic endothelial cells (HAECs) and human dermal microvascular endothelial cells (HMECs). 4,6-dinitro-o-cresol 24-30 vascular cell adhesion molecule 1 Homo sapiens 98-131 10900176-3 2000 We explored the role of flavin containing proteins such as NADH/NADPH oxidase in the induction of vascular cell adhesion molecule-1 (VCAM-1) and intercellular adhesion molecule-1 (ICAM-1) gene expression in human aortic endothelial cells (HAECs) and human dermal microvascular endothelial cells (HMECs). 4,6-dinitro-o-cresol 24-30 vascular cell adhesion molecule 1 Homo sapiens 133-139 10900176-3 2000 We explored the role of flavin containing proteins such as NADH/NADPH oxidase in the induction of vascular cell adhesion molecule-1 (VCAM-1) and intercellular adhesion molecule-1 (ICAM-1) gene expression in human aortic endothelial cells (HAECs) and human dermal microvascular endothelial cells (HMECs). 4,6-dinitro-o-cresol 24-30 intercellular adhesion molecule 1 Homo sapiens 145-178 10900176-3 2000 We explored the role of flavin containing proteins such as NADH/NADPH oxidase in the induction of vascular cell adhesion molecule-1 (VCAM-1) and intercellular adhesion molecule-1 (ICAM-1) gene expression in human aortic endothelial cells (HAECs) and human dermal microvascular endothelial cells (HMECs). 4,6-dinitro-o-cresol 24-30 intercellular adhesion molecule 1 Homo sapiens 180-186 10920257-10 2000 The largest factor in the substantially low pK(a) of reduced flavin in DAO is probably the steric hindrance between the hydrogen atom of H-N(1)(flavin) and the hydrogen atom of H-N of Gly315, which becomes significant when a hydrogen is bound to N(1) of flavin. 4,6-dinitro-o-cresol 144-150 D-amino acid oxidase Homo sapiens 71-74 10716694-0 2000 Design and properties of human D-amino acid oxidase with covalently attached flavin. 4,6-dinitro-o-cresol 77-83 D-amino acid oxidase Homo sapiens 31-51 10781602-0 2000 The C terminus of mouse macrophage inducible nitric-oxide synthase attenuates electron flow through the flavin domain. 4,6-dinitro-o-cresol 104-110 nitric oxide synthase 1, neuronal Mus musculus 45-66 10858451-8 2000 The flavin reductase activity of biliverdin-IXbeta reductase is potently inhibited by mesobiliverdin-XIIIalpha and protohemin, which is consistent with the hypothesis that the tetrapyrrole and flavin substrate bind at a common site. 4,6-dinitro-o-cresol 4-10 biliverdin reductase B Homo sapiens 33-60 10871048-3 2000 Incubations of the yeast DHOD with dideuterodihydroorotate (deuterated in the positions eliminated in the dehydrogenation) as the donor and [14C]orotate as the acceptor revealed that the C5 deuteron exchanged with H2O solvent at a rate equal to the 14C exchange rate, whereas the C6 deuteron was infrequently exchanged with H2O solvent, thus indicating that the C6 deuteron of the dihydroorotate is sticky on the flavin cofactor. 4,6-dinitro-o-cresol 413-419 dihydroorotate dehydrogenase Saccharomyces cerevisiae S288C 25-29 10869423-4 2000 Renox is homologous to gp91(phox) (91-kDa subunit of the phagocyte oxidase), the electron-transporting subunit of phagocytic NADPH oxidase, and contains all of the structural motifs considered essential for binding of heme, flavin, and nucleotide. 4,6-dinitro-o-cresol 224-230 NADPH oxidase 4 Homo sapiens 0-5 10869423-4 2000 Renox is homologous to gp91(phox) (91-kDa subunit of the phagocyte oxidase), the electron-transporting subunit of phagocytic NADPH oxidase, and contains all of the structural motifs considered essential for binding of heme, flavin, and nucleotide. 4,6-dinitro-o-cresol 224-230 cytochrome b-245 beta chain Homo sapiens 23-33 10847687-3 2000 We positionally cloned FKF1, which encodes a novel protein with a PAS domain similar to the flavin-binding region of certain photoreceptors, an F box characteristic of proteins that direct ubiquitin-mediated degradation, and six kelch repeats predicted to fold into a beta propeller. 4,6-dinitro-o-cresol 92-98 flavin-binding, kelch repeat, f box 1 Arabidopsis thaliana 23-27 10716694-1 2000 An "artificial flavinylation" approach was developed to replace a native noncovalent flavin prosthetic group with a covalently attached flavin analogue in recombinant human d-amino acid oxidase. 4,6-dinitro-o-cresol 15-21 D-amino acid oxidase Homo sapiens 173-193 10716694-1 2000 An "artificial flavinylation" approach was developed to replace a native noncovalent flavin prosthetic group with a covalently attached flavin analogue in recombinant human d-amino acid oxidase. 4,6-dinitro-o-cresol 85-91 D-amino acid oxidase Homo sapiens 173-193 10716694-5 2000 We conclude that, despite the implemented restraints on its mobility, the covalently attached flavin is properly positioned within the protein active site and acts efficiently during d-amino acid oxidase catalytic turnover. 4,6-dinitro-o-cresol 94-100 D-amino acid oxidase Homo sapiens 183-203 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 nitric oxide synthase 1 Homo sapiens 26-30 11213485-2 2000 Cytosolic thioredoxin reductase from mammalian cells is a dimeric flavin enzyme comprising a glutathione reductase-like equivalent elongated with 16 residues including the conserved carboxy-terminal sequence, Gly-Cys-SeCys-Gly, where SeCys is selenocysteine. 4,6-dinitro-o-cresol 66-72 thioredoxin Homo sapiens 10-21 10681501-10 2000 These data suggest that binding of the B2R 310-329 peptide blocks flavin to heme electron transfer. 4,6-dinitro-o-cresol 66-72 bradykinin receptor B2 Homo sapiens 39-42 10671564-3 2000 Phosphopeptide analysis by mass spectrometry identified Ser(1177), as well as Ser(633) which is situated in a recently defined CaM autoinhibitory domain within the flavin-binding region of human NOS-III. 4,6-dinitro-o-cresol 164-170 calmodulin 3 Homo sapiens 127-130 10671564-3 2000 Phosphopeptide analysis by mass spectrometry identified Ser(1177), as well as Ser(633) which is situated in a recently defined CaM autoinhibitory domain within the flavin-binding region of human NOS-III. 4,6-dinitro-o-cresol 164-170 nitric oxide synthase 3 Homo sapiens 195-202 10606764-0 2000 The FAD binding sites of human liver monoamine oxidases A and B: investigation of the role of flavin ribityl side chain hydroxyl groups in the covalent flavinylation reaction and catalytic activities. 4,6-dinitro-o-cresol 94-100 presenilin 1 Homo sapiens 4-7 10606764-0 2000 The FAD binding sites of human liver monoamine oxidases A and B: investigation of the role of flavin ribityl side chain hydroxyl groups in the covalent flavinylation reaction and catalytic activities. 4,6-dinitro-o-cresol 94-100 monoamine oxidase A Homo sapiens 37-63 10606764-1 2000 The role of ribityl side chain hydroxyl groups of the flavin moiety in the covalent flavinylation reaction and catalytic activities of recombinant human liver monoamine oxidases (MAO) A and B have been investigated using the riboflavin analogue: N(10)-omega-hydroxypentyl-isoalloxazine. 4,6-dinitro-o-cresol 54-60 monoamine oxidase A Homo sapiens 159-191 10606764-8 2000 This is in contrast to the suggestion based on mutagenesis studies that an interaction between the 3"-hydroxyl group of the flavin and the beta-carbonyl of Asp(227) is required for the covalent flavinylation reaction of MAO B (Zhou et al., J. Biol. 4,6-dinitro-o-cresol 124-130 monoamine oxidase B Homo sapiens 220-225 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 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 calmodulin 1 Homo sapiens 162-172 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 BRCA2 DNA repair associated Homo sapiens 174-177 10594372-2 1999 The aim of this study is to elucidate the mechanism of activation of the flavin domain by calcium/calmodulin (Ca(2+)/CaM). 4,6-dinitro-o-cresol 73-79 calmodulin 1 Homo sapiens 98-108 10594372-2 1999 The aim of this study is to elucidate the mechanism of activation of the flavin domain by calcium/calmodulin (Ca(2+)/CaM). 4,6-dinitro-o-cresol 73-79 calmodulin 1 Homo sapiens 117-120 10594372-3 1999 In this study, we used the recombinant nNOS flavin domains, which include or delete the calmodulin (CaM)-binding site. 4,6-dinitro-o-cresol 44-50 nitric oxide synthase 1 Homo sapiens 39-43 10594372-3 1999 In this study, we used the recombinant nNOS flavin domains, which include or delete the calmodulin (CaM)-binding site. 4,6-dinitro-o-cresol 44-50 calmodulin 1 Homo sapiens 88-98 10594372-3 1999 In this study, we used the recombinant nNOS flavin domains, which include or delete the calmodulin (CaM)-binding site. 4,6-dinitro-o-cresol 44-50 calmodulin 1 Homo sapiens 100-103 10594372-4 1999 The air-stable semiquinone of the nNOS flavin domains showed similar redox properties to the corresponding FAD-FMNH(&z.ccirf;) of P450R. 4,6-dinitro-o-cresol 39-45 nitric oxide synthase 1 Homo sapiens 34-38 10594372-4 1999 The air-stable semiquinone of the nNOS flavin domains showed similar redox properties to the corresponding FAD-FMNH(&z.ccirf;) of P450R. 4,6-dinitro-o-cresol 39-45 BRCA2 DNA repair associated Homo sapiens 107-110 10438531-10 1999 MAO A partially purified from yeast grown on 8-nor-8-chlororiboflavin exhibited an absorption spectrum indicating the covalent flavin is an 8-nor-8-S-thioflavin, suggesting a nucleophilic displacement mechanism that supports the quinone-methide mechanism previously suggested as a general mechanism for covalent flavin attachment. 4,6-dinitro-o-cresol 63-69 monoamine oxidase A Homo sapiens 0-5 10600101-0 1999 Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase. 4,6-dinitro-o-cresol 31-37 nitric oxide synthase 1 Rattus norvegicus 51-81 10600101-1 1999 Midpoint reduction potentials for the flavin cofactors in the reductase domain of rat neuronal nitric oxide synthase (nNOS) in calmodulin (CaM)-free and -bound forms have been determined by direct anaerobic titration. 4,6-dinitro-o-cresol 38-44 nitric oxide synthase 1 Rattus norvegicus 86-116 10600101-1 1999 Midpoint reduction potentials for the flavin cofactors in the reductase domain of rat neuronal nitric oxide synthase (nNOS) in calmodulin (CaM)-free and -bound forms have been determined by direct anaerobic titration. 4,6-dinitro-o-cresol 38-44 nitric oxide synthase 1 Rattus norvegicus 118-122 10438466-0 1999 The p67(phox) activation domain regulates electron flow from NADPH to flavin in flavocytochrome b(558). 4,6-dinitro-o-cresol 70-76 CD33 molecule Homo sapiens 4-13 10438466-7 1999 Omission of p67(phox) decreased the percent steady state reduction of the flavin to 4%, but omission of p47(phox) had little effect. 4,6-dinitro-o-cresol 74-80 CD33 molecule Homo sapiens 12-15 10438466-7 1999 Omission of p67(phox) decreased the percent steady state reduction of the flavin to 4%, but omission of p47(phox) had little effect. 4,6-dinitro-o-cresol 74-80 CD33 molecule Homo sapiens 16-20 10438466-8 1999 The activation domain on p67(phox) was critical for regulating flavin reduction, since mutations in this region that decreased O2(-.) 4,6-dinitro-o-cresol 63-69 CD33 molecule Homo sapiens 25-28 10438466-8 1999 The activation domain on p67(phox) was critical for regulating flavin reduction, since mutations in this region that decreased O2(-.) 4,6-dinitro-o-cresol 63-69 CD33 molecule Homo sapiens 29-33 10438531-0 1999 Influence of flavin analogue structure on the catalytic activities and flavinylation reactions of recombinant human liver monoamine oxidases A and B. 4,6-dinitro-o-cresol 13-19 monoamine oxidase A Homo sapiens 122-148 10438531-6 1999 The selectivities of MAO A and MAO B for flavin analogue incorporation are found to be similar, although 8alpha-methylation of the flavin resulted in a higher level of catalytic activity for MAO B than for MAO A. 4,6-dinitro-o-cresol 41-47 monoamine oxidase A Homo sapiens 21-26 10438531-6 1999 The selectivities of MAO A and MAO B for flavin analogue incorporation are found to be similar, although 8alpha-methylation of the flavin resulted in a higher level of catalytic activity for MAO B than for MAO A. 4,6-dinitro-o-cresol 41-47 monoamine oxidase B Homo sapiens 31-36 10438531-6 1999 The selectivities of MAO A and MAO B for flavin analogue incorporation are found to be similar, although 8alpha-methylation of the flavin resulted in a higher level of catalytic activity for MAO B than for MAO A. 4,6-dinitro-o-cresol 131-137 monoamine oxidase A Homo sapiens 21-26 10438531-6 1999 The selectivities of MAO A and MAO B for flavin analogue incorporation are found to be similar, although 8alpha-methylation of the flavin resulted in a higher level of catalytic activity for MAO B than for MAO A. 4,6-dinitro-o-cresol 131-137 monoamine oxidase B Homo sapiens 191-196 10438531-6 1999 The selectivities of MAO A and MAO B for flavin analogue incorporation are found to be similar, although 8alpha-methylation of the flavin resulted in a higher level of catalytic activity for MAO B than for MAO A. 4,6-dinitro-o-cresol 131-137 monoamine oxidase A Homo sapiens 206-211 10438531-10 1999 MAO A partially purified from yeast grown on 8-nor-8-chlororiboflavin exhibited an absorption spectrum indicating the covalent flavin is an 8-nor-8-S-thioflavin, suggesting a nucleophilic displacement mechanism that supports the quinone-methide mechanism previously suggested as a general mechanism for covalent flavin attachment. 4,6-dinitro-o-cresol 127-133 monoamine oxidase A Homo sapiens 0-5 10428852-6 1999 Furthermore, diphenylene iodonium, an inhibitor of flavin-containing oxidases, or overexpression of catalase to block angiotensin II-induced intracellular H(2)O(2) production significantly inhibits angiotensin II-induced Akt/PKB phosphorylation, indicating a role for ROS in agonist-induced Akt/PKB activation. 4,6-dinitro-o-cresol 51-57 angiotensinogen Homo sapiens 118-132 10428852-6 1999 Furthermore, diphenylene iodonium, an inhibitor of flavin-containing oxidases, or overexpression of catalase to block angiotensin II-induced intracellular H(2)O(2) production significantly inhibits angiotensin II-induced Akt/PKB phosphorylation, indicating a role for ROS in agonist-induced Akt/PKB activation. 4,6-dinitro-o-cresol 51-57 angiotensinogen Homo sapiens 198-212 10411952-7 1999 The LOV domain has therefore been proposed to reflect a flavin-binding site, regulating nph1 kinase activity in response to blue light-induced redox changes. 4,6-dinitro-o-cresol 56-62 phototropin 1 Arabidopsis thaliana 88-92 10423253-13 1999 These results indicate that the 4"-hydroxyl-N(1) hydrogen bond plays a major role in the stabilization of the anionic semiquinone and anionic hydroquinone oxidation states of ETF and that this hydrogen bond may provide a pathway for electron transfer between the ETF flavin and the flavin of ETF-QO. 4,6-dinitro-o-cresol 267-273 electron transfer flavoprotein dehydrogenase Homo sapiens 292-298 10423253-13 1999 These results indicate that the 4"-hydroxyl-N(1) hydrogen bond plays a major role in the stabilization of the anionic semiquinone and anionic hydroquinone oxidation states of ETF and that this hydrogen bond may provide a pathway for electron transfer between the ETF flavin and the flavin of ETF-QO. 4,6-dinitro-o-cresol 282-288 electron transfer flavoprotein dehydrogenase Homo sapiens 292-298 9614088-3 1998 Our previous studies identified two noncovalent flavin-binding regions in MAO B (residues 6-34 and 39-46) (Kwan, S.-W., Lewis, D. A., Zhou, B. P., and Abell, C. W. (1995) Arch. 4,6-dinitro-o-cresol 48-54 monoamine oxidase B Homo sapiens 74-79 10201405-8 1999 The mutation A177V does not affect Km or k(cat) but instead increases the propensity for bacterial MTHFR to lose its essential flavin cofactor. 4,6-dinitro-o-cresol 127-133 methylenetetrahydrofolate reductase Homo sapiens 99-104 9990125-9 1999 Resonance Raman spectra of the MCAD.3-thia-C8-CoA complex, with excitation at the CT band, showed enhanced bands, among which the 854- and 1,368-cm-1 bands were assigned to the S-C(2) stretching mode of the ligand and to flavin band VII, respectively. 4,6-dinitro-o-cresol 221-227 acyl-CoA dehydrogenase medium chain Homo sapiens 31-35 10215790-0 1999 Sequence variations in the flavin-containing mono-oxygenase 3 gene (FMO3) in fish odour syndrome. 4,6-dinitro-o-cresol 27-33 flavin containing dimethylaniline monoxygenase 3 Homo sapiens 68-72 10215790-2 1999 Flavin-containing mono-oxygenase 3 (FMO3) catalyses TMA oxidation and mutations in the FMO3 gene have recently been shown to underlie trimethylaminuria/fish odour syndrome. 4,6-dinitro-o-cresol 0-6 flavin containing dimethylaniline monoxygenase 3 Homo sapiens 36-40 10215790-2 1999 Flavin-containing mono-oxygenase 3 (FMO3) catalyses TMA oxidation and mutations in the FMO3 gene have recently been shown to underlie trimethylaminuria/fish odour syndrome. 4,6-dinitro-o-cresol 0-6 flavin containing dimethylaniline monoxygenase 3 Homo sapiens 87-91 10080695-12 1999 The flavin antagonist diphenyleneiodonium blocked light induction of gsa in both wild-type and mutant cells under conditions where respiration was not inhibited. 4,6-dinitro-o-cresol 4-10 uncharacterized protein Chlamydomonas reinhardtii 69-72 9860870-0 1998 Sensitivity of flavin fluorescence dynamics in neuronal nitric oxide synthase to cofactor-induced conformational changes and dimerization. 4,6-dinitro-o-cresol 15-21 nitric oxide synthase 1 Homo sapiens 47-77 9860870-1 1998 The fluorescence intensity of the two flavin prosthetic groups, FMN and FAD, in neuronal nitric oxide synthase (nNOS) was found to decay highly nonexponentially, being best described by four fluorescence lifetimes. 4,6-dinitro-o-cresol 38-44 nitric oxide synthase 1 Homo sapiens 80-110 9860870-1 1998 The fluorescence intensity of the two flavin prosthetic groups, FMN and FAD, in neuronal nitric oxide synthase (nNOS) was found to decay highly nonexponentially, being best described by four fluorescence lifetimes. 4,6-dinitro-o-cresol 38-44 nitric oxide synthase 1 Homo sapiens 112-116 9860870-3 1998 Investigating nNOS in the absence of one or more of Ca2+/calmodulin, tetrahydrobiopterin, and heme revealed an influence of these cofactors on the microenvironments of the flavin prosthetic groups. 4,6-dinitro-o-cresol 172-178 nitric oxide synthase 1 Homo sapiens 14-18 9860870-4 1998 Similar effects on the flavin rotational dynamics were found by analyzing the fluorescence anisotropy decay of the holo and of the different apo forms of nNOS. 4,6-dinitro-o-cresol 23-29 nitric oxide synthase 1 Homo sapiens 154-158 9712892-12 1998 Together, these data demonstrate that iNOS does generate O-2, and this mainly occurs at the flavin-binding sites of the reductase domain. 4,6-dinitro-o-cresol 92-98 nitric oxide synthase 2 Homo sapiens 38-42 9712892-12 1998 Together, these data demonstrate that iNOS does generate O-2, and this mainly occurs at the flavin-binding sites of the reductase domain. 4,6-dinitro-o-cresol 92-98 immunoglobulin kappa variable 1D-39 Homo sapiens 57-60 9671517-1 1998 The medium chain acyl-CoA dehydrogenase catalyzes the flavin-dependent oxidation of a variety of acyl-CoA thioesters with the transfer of reducing equivalents to electron-transferring flavoprotein. 4,6-dinitro-o-cresol 54-60 acyl-CoA dehydrogenase medium chain Homo sapiens 4-39 9622495-1 1998 Oxidation of thioester substrates in the medium-chain acyl-CoA dehydrogenase involves alpha-proton abstraction by the catalytic base, Glu376, with transfer of a beta-hydride equivalent to the flavin prosthetic group. 4,6-dinitro-o-cresol 192-198 acyl-CoA dehydrogenase medium chain Homo sapiens 41-76 10075667-6 1999 The flavin and iron-sulfur centers of inactivated XO were reduced by dithionite and reoxidized readily with oxygen, and inactivated XDH retained electron transfer activities from NADH to electron acceptors, consistent with the conclusion that the flavin and iron-sulfur centers of the inactivated enzyme both remained intact. 4,6-dinitro-o-cresol 247-253 xanthine dehydrogenase Homo sapiens 132-135 9988690-0 1999 Role of the flavin midpoint potential and NAD binding in determining NAD versus oxygen reactivity of xanthine oxidoreductase. 4,6-dinitro-o-cresol 12-18 xanthine dehydrogenase Bos taurus 101-124 9988690-8 1999 Reductive titrations indicate that both 1-deaza-XO and 1-deaza-XDH have a flavin midpoint potential similar to native XDH and that 8-CN-XO and 8-CN-XDH each have a flavin potential higher than XO. 4,6-dinitro-o-cresol 74-80 xanthine dehydrogenase Bos taurus 63-66 9988690-8 1999 Reductive titrations indicate that both 1-deaza-XO and 1-deaza-XDH have a flavin midpoint potential similar to native XDH and that 8-CN-XO and 8-CN-XDH each have a flavin potential higher than XO. 4,6-dinitro-o-cresol 164-170 xanthine dehydrogenase Bos taurus 63-66 10609886-4 1999 A model explaining the reactivity of dinitrohalobenzenes with thioredoxin reductase is presented, involving dinitrophenyl-derivatization of both the selenocysteine residue and its neighboring cysteine residue, reduction by NADPH of the enzyme-bound flavin in dinitrophenyl-alkylated enzyme (dnp-TrxR), followed by two consecutive one-electron transfers from the flavin to nitro groups of the dnp-moieties in dnp-TrxR, forming nitro anion radicals. 4,6-dinitro-o-cresol 249-255 thioredoxin Homo sapiens 62-73 10609886-4 1999 A model explaining the reactivity of dinitrohalobenzenes with thioredoxin reductase is presented, involving dinitrophenyl-derivatization of both the selenocysteine residue and its neighboring cysteine residue, reduction by NADPH of the enzyme-bound flavin in dinitrophenyl-alkylated enzyme (dnp-TrxR), followed by two consecutive one-electron transfers from the flavin to nitro groups of the dnp-moieties in dnp-TrxR, forming nitro anion radicals. 4,6-dinitro-o-cresol 362-368 thioredoxin Homo sapiens 62-73 9644264-3 1998 The 1,605-cm-1 Raman band of the anionic reduced flavin in the purple intermediate of D-amino acid oxidase (DAO) with D-proline or D-alanine does not shift in DAO reconstituted with [4-carbonyl-18O]FAD, although it shifts with [4,10a-13C2]- or [4a-13C]FAD. 4,6-dinitro-o-cresol 49-55 D-amino acid oxidase Homo sapiens 86-106 9644264-3 1998 The 1,605-cm-1 Raman band of the anionic reduced flavin in the purple intermediate of D-amino acid oxidase (DAO) with D-proline or D-alanine does not shift in DAO reconstituted with [4-carbonyl-18O]FAD, although it shifts with [4,10a-13C2]- or [4a-13C]FAD. 4,6-dinitro-o-cresol 49-55 D-amino acid oxidase Homo sapiens 108-111 9644264-6 1998 The frequencies of the reduced flavin in the purple intermediates of the dehydrogenases (medium-chain acyl-CoA, short-chain acyl-CoA, and isovaleryl-CoA dehydrogenases) are higher than those of the oxidases (DAO and L-phenylalanine oxidase). 4,6-dinitro-o-cresol 31-37 D-amino acid oxidase Homo sapiens 208-211 9644264-9 1998 Furthermore, strong hydrogen bonding of flavin at the N(1) moiety with the hydroxyl group of Thr136 in MCAD is probably responsible for the strong bond of the C(4a)=C(10a) of reduced flavin in the dehydrogenase. 4,6-dinitro-o-cresol 40-46 acyl-CoA dehydrogenase medium chain Homo sapiens 103-107 9644264-9 1998 Furthermore, strong hydrogen bonding of flavin at the N(1) moiety with the hydroxyl group of Thr136 in MCAD is probably responsible for the strong bond of the C(4a)=C(10a) of reduced flavin in the dehydrogenase. 4,6-dinitro-o-cresol 183-189 acyl-CoA dehydrogenase medium chain Homo sapiens 103-107 9535883-9 1998 In the case of 8-CN-FMN-OYE I, it was shown that the comproportionation reaction of a mixture of reduced and oxidized enzyme bound flavin is very rapid, compared with the same reaction with native protein, resulting in approximately 100% thermodynamically stable anionic semiquinone. 4,6-dinitro-o-cresol 131-137 formin 1 Homo sapiens 20-23 9578577-0 1998 Human protoporphyrinogen oxidase: relation between the herbicide binding site and the flavin cofactor. 4,6-dinitro-o-cresol 86-92 protoporphyrinogen oxidase Homo sapiens 6-32 9536088-0 1998 Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication. 4,6-dinitro-o-cresol 17-23 flavin containing dimethylaniline monoxygenase 3 Homo sapiens 55-59 9536088-2 1998 We show here that mutations in the human flavin-containing monooxygenase isoform 3 gene ( FMO3 ) impair N -oxygenation of xenobiotics and are responsible for the trimethylaminuria phenotype. 4,6-dinitro-o-cresol 41-47 flavin containing dimethylaniline monoxygenase 3 Homo sapiens 90-94 9535883-10 1998 In the case of 8-CN-OYE I, it was shown that the rate of reduction of the enzyme bound flavin by NADPH is approximately 40 times faster, and the rate of reoxidation of reduced enzyme bound flavin by oxygen is an order of magnitude slower than with the normal FMN enzyme. 4,6-dinitro-o-cresol 87-93 formin 1 Homo sapiens 259-262 9535883-10 1998 In the case of 8-CN-OYE I, it was shown that the rate of reduction of the enzyme bound flavin by NADPH is approximately 40 times faster, and the rate of reoxidation of reduced enzyme bound flavin by oxygen is an order of magnitude slower than with the normal FMN enzyme. 4,6-dinitro-o-cresol 189-195 formin 1 Homo sapiens 259-262 9546198-5 1998 In D-amino acid oxidase and cholesterol oxidase, a loop forms a "lid" controlling the active site accessibility, whereas in p-hydroxybenzoate hydroxylase is the flavin itself, which swings out to allow substrate binding. 4,6-dinitro-o-cresol 161-167 D-amino acid oxidase Homo sapiens 3-23 9398858-3 1997 TMA oxidation is catalyzed by flavin-containing mono-oxygenase (FMO; refs 7,8), and tissue localization and functional studies have established FMO3 as the form most likely to be defective in fish-odour syndrome. 4,6-dinitro-o-cresol 30-36 flavin containing dimethylaniline monoxygenase 3 Homo sapiens 144-148 9564616-5 1998 (b) It accelerates the reactivity of the covalently bound flavin with oxygen, effectively increasing the Vm (particularly for MAO-B). 4,6-dinitro-o-cresol 58-64 monoamine oxidase B Homo sapiens 126-131 9405347-3 1997 Sequence similarity with a known (NIFL) and a suspected (Aer) flavoprotein suggests that NPH1 LOV1 and LOV2 may be flavin-binding domains that regulate kinase activity in response to blue light-induced redox changes. 4,6-dinitro-o-cresol 115-121 phototropin 1 Arabidopsis thaliana 89-93 9405347-3 1997 Sequence similarity with a known (NIFL) and a suspected (Aer) flavoprotein suggests that NPH1 LOV1 and LOV2 may be flavin-binding domains that regulate kinase activity in response to blue light-induced redox changes. 4,6-dinitro-o-cresol 115-121 NAC domain containing protein 35 Arabidopsis thaliana 94-98 9485308-4 1998 This subunit contains FMN as the flavin cofactor which exhibits the properties of Flavin 2 of glutamate synthase: reactivity with sulfite to yield a flavin-N(5)-sulfite addition product (Kd = 2.6 +/- 0.22 mM), lack of reactivity with NADPH, reduction by L-glutamate, and reoxidation by 2-oxoglutarate and glutamine. 4,6-dinitro-o-cresol 33-39 formin 1 Homo sapiens 22-25 9485308-5 1998 Thus, FMN is the flavin located at the site of reduction of the iminoglutarate formed on the addition of glutamine amide group to the C(2) carbon of 2-oxoglutarate. 4,6-dinitro-o-cresol 17-23 formin 1 Homo sapiens 6-9 9220981-11 1997 Considering the high homology in the flavin catalytic sites of flavocytochrome b2 and L-lactate monooxygenase, the observed differences in H-bonding environment and conformation of the FMN ring are related to the different biological functions of the two flavoproteins. 4,6-dinitro-o-cresol 37-43 formin 1 Homo sapiens 185-188 9305407-1 1997 Variable amounts of flavin-containing monooxygenase isoforms 3 and 5 (FMO3 and FMO5) are present in microsomal preparations from adult, male, human liver. 4,6-dinitro-o-cresol 20-26 flavin containing dimethylaniline monoxygenase 3 Homo sapiens 70-74 9305407-1 1997 Variable amounts of flavin-containing monooxygenase isoforms 3 and 5 (FMO3 and FMO5) are present in microsomal preparations from adult, male, human liver. 4,6-dinitro-o-cresol 20-26 flavin containing dimethylaniline monoxygenase 5 Homo sapiens 79-83 9268712-7 1997 Superoxide generation by NOS III could be completely inhibited by diphenyleneiodonium (DPI), an inhibitor of the flavin moiety of the enzyme, indicating that this group is a main source of superoxide production by the enzyme. 4,6-dinitro-o-cresol 113-119 nitric oxide synthase 3 Homo sapiens 25-32 9268712-10 1997 NOS III thus appears to be a superoxide generating enzyme probably through its flavin moiety, as well as a BH4-dependent NO producing enzyme. 4,6-dinitro-o-cresol 79-85 nitric oxide synthase 3 Homo sapiens 0-7 9399588-7 1997 This model as well as DAO-OAB complex enables the evaluation of the substrate-flavin interaction prior to electron transfer from the substrate to flavin and provides two possible mechanisms for the reductive-half reaction of DAO, i.e., the electron-proton-electron transfer mechanism and the ionic mechanism. 4,6-dinitro-o-cresol 78-84 D-amino acid oxidase Homo sapiens 22-25 9399588-7 1997 This model as well as DAO-OAB complex enables the evaluation of the substrate-flavin interaction prior to electron transfer from the substrate to flavin and provides two possible mechanisms for the reductive-half reaction of DAO, i.e., the electron-proton-electron transfer mechanism and the ionic mechanism. 4,6-dinitro-o-cresol 78-84 D-amino acid oxidase Homo sapiens 225-228 9399588-7 1997 This model as well as DAO-OAB complex enables the evaluation of the substrate-flavin interaction prior to electron transfer from the substrate to flavin and provides two possible mechanisms for the reductive-half reaction of DAO, i.e., the electron-proton-electron transfer mechanism and the ionic mechanism. 4,6-dinitro-o-cresol 146-152 D-amino acid oxidase Homo sapiens 22-25 9399588-7 1997 This model as well as DAO-OAB complex enables the evaluation of the substrate-flavin interaction prior to electron transfer from the substrate to flavin and provides two possible mechanisms for the reductive-half reaction of DAO, i.e., the electron-proton-electron transfer mechanism and the ionic mechanism. 4,6-dinitro-o-cresol 146-152 D-amino acid oxidase Homo sapiens 225-228 9108027-14 1997 Titration of thioredoxin reductase from human placenta with dithionite takes place in two spectral phases: formation of a thiolate-flavin charge transfer complex followed by reduction of the flavin, just as with lipoamide dehydrogenase or glutathione reductase. 4,6-dinitro-o-cresol 131-137 peroxiredoxin 5 Homo sapiens 13-34 9201918-8 1997 3-Methyl-3-butenoyl-CoA requires activation by alpha-proton abstraction and rapidly yields a reduced flavin adduct with wild-type isovaleryl-CoA dehydrogenase. 4,6-dinitro-o-cresol 101-107 isovaleryl-CoA dehydrogenase Homo sapiens 130-158 9153426-3 1997 We have carried out the X-ray analysis of reduced DAAO in complex with the reaction product imino tryptophan (iTrp) and of the covalent adduct generated by the photoinduced reaction of the flavin with 3-methyl-2-oxobutyric acid (kVal). 4,6-dinitro-o-cresol 189-195 D-amino acid oxidase Homo sapiens 50-54 9108027-14 1997 Titration of thioredoxin reductase from human placenta with dithionite takes place in two spectral phases: formation of a thiolate-flavin charge transfer complex followed by reduction of the flavin, just as with lipoamide dehydrogenase or glutathione reductase. 4,6-dinitro-o-cresol 191-197 peroxiredoxin 5 Homo sapiens 13-34 9045710-7 1997 Both purified sarcosine oxidase and a recombinant fusion protein synthesized in Escherichia coli contain a covalently bound flavin, metabolize sarcosine, L-pipecolic acid, and L-proline, and cross-react with antibodies raised against L-pipecolic acid oxidase from monkey liver. 4,6-dinitro-o-cresol 124-130 peroxisomal sarcosine oxidase Oryctolagus cuniculus 14-31 9100014-4 1997 The hydroxyl hydrogen and a backbone amide hydrogen of alphaT266 are hydrogen bonded to N(5) and C(4)O of the flavin, respectively, and the corresponding alphaT244 has the same structural role in P. denitrificans ETF. 4,6-dinitro-o-cresol 110-116 TEA domain transcription factor 2 Homo sapiens 213-216 9100014-14 1997 The separation of flavin redox potentials between the oxidized/semiquinone couple and semiquinone/hydroquinone couple are -6 mV in the wild type ETF and -27 mV in the mutant ETF. 4,6-dinitro-o-cresol 18-24 TEA domain transcription factor 2 Homo sapiens 145-148 9100014-14 1997 The separation of flavin redox potentials between the oxidized/semiquinone couple and semiquinone/hydroquinone couple are -6 mV in the wild type ETF and -27 mV in the mutant ETF. 4,6-dinitro-o-cresol 18-24 TEA domain transcription factor 2 Homo sapiens 174-177 9092820-2 1997 In this work, we show that the two flavin-based enzymes ferredoxin-NADP+ reductase and xanthine oxidase catalyze the reductive activation of 1 by NADPH and NADH, respectively. 4,6-dinitro-o-cresol 35-41 ferredoxin reductase Homo sapiens 56-82 8910450-3 1996 Kinetic analysis of the activity with these substrates indicates that the reduction of the enzyme bound flavin by substrates is the rate-limiting step in A95G-LOX. 4,6-dinitro-o-cresol 104-110 lysyl oxidase Rattus norvegicus 159-162 11671373-7 1997 Comparison of the Bronsted-type plots for the dinitro and trinitro derivatives obtained in this work with those for the pyridinolysis of S-(2,4-dinitrophenyl) and S-(2,4,6-trinitrophenyl) O-ethyl thiocarbonates indicates that substitution of S(-) by O(-) in T(+/-) increases the amine/ArS(-) nucleofugality ratio from T(+/-). 4,6-dinitro-o-cresol 46-53 RIEG2 Homo sapiens 285-288 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 9076656-0 1997 Molecular cloning of mouse liver flavin containing monooxygenase (FMO1) cDNA and characterization of the expression product: metabolism of the neurotoxin, 1,2,3,4-tetrahydroisoquinoline (TIQ). 4,6-dinitro-o-cresol 33-39 flavin containing monooxygenase 1 Mus musculus 66-70 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 BRCA2 DNA repair associated Homo sapiens 68-71 8954538-10 1996 The free flavins, i.e., FMN, 8-OH-FAD, 8-NH2-FAD, and riboflavin, are able to support ferricyanide reduction at a rate of 0.40, 0.52, 0.87, and 0.16 mumol/min/nmol flavin, respectively. 4,6-dinitro-o-cresol 9-15 BRCA2 DNA repair associated Homo sapiens 34-37 8954538-10 1996 The free flavins, i.e., FMN, 8-OH-FAD, 8-NH2-FAD, and riboflavin, are able to support ferricyanide reduction at a rate of 0.40, 0.52, 0.87, and 0.16 mumol/min/nmol flavin, respectively. 4,6-dinitro-o-cresol 9-15 BRCA2 DNA repair associated Homo sapiens 45-48 12226388-10 1996 Tobacco NAD(P)H-QR resembles animal DT-diaphorase in some respects (identical reaction mechanism with a two-electron transfer to quinones, unusually high catalytic capability, and donor and acceptor substrate specificity), but it differs from DT-diaphorase in molecular structure, flavin cofactor, stereospecificity, and sensitivity to inhibitors. 4,6-dinitro-o-cresol 281-287 NAD(P)H quinone dehydrogenase 1 Homo sapiens 36-49 8881717-6 1996 Of the four enzymes involved in the synthesis and breakdown of the flavin coenzymes studied, the activity of hepatic flavokinase (ATP: riboflavin 5"-phosphotransferase; EC 2.7.1.26) was significantly lower, and that of FAD synthetase (ATP: FMN adenylyltransferase; EC 2.7.7.2) was higher during riboflavin restriction and infection. 4,6-dinitro-o-cresol 67-73 riboflavin kinase Mus musculus 117-128 8881717-6 1996 Of the four enzymes involved in the synthesis and breakdown of the flavin coenzymes studied, the activity of hepatic flavokinase (ATP: riboflavin 5"-phosphotransferase; EC 2.7.1.26) was significantly lower, and that of FAD synthetase (ATP: FMN adenylyltransferase; EC 2.7.7.2) was higher during riboflavin restriction and infection. 4,6-dinitro-o-cresol 67-73 riboflavin kinase Mus musculus 130-167 8880927-4 1996 The electrostatic potential of the surface near the flavin-protruding side (dimethylbenzene end of the flavin ring) of NADH-cytochrome b5 reductase was positive over a wide area while that of the surface near the heme-binding site of cytochrome b5 was negative. 4,6-dinitro-o-cresol 52-58 cytochrome b5 type A Homo sapiens 124-137 8880927-4 1996 The electrostatic potential of the surface near the flavin-protruding side (dimethylbenzene end of the flavin ring) of NADH-cytochrome b5 reductase was positive over a wide area while that of the surface near the heme-binding site of cytochrome b5 was negative. 4,6-dinitro-o-cresol 52-58 cytochrome b5 type A Homo sapiens 234-247 8880927-4 1996 The electrostatic potential of the surface near the flavin-protruding side (dimethylbenzene end of the flavin ring) of NADH-cytochrome b5 reductase was positive over a wide area while that of the surface near the heme-binding site of cytochrome b5 was negative. 4,6-dinitro-o-cresol 103-109 cytochrome b5 type A Homo sapiens 124-137 8880927-4 1996 The electrostatic potential of the surface near the flavin-protruding side (dimethylbenzene end of the flavin ring) of NADH-cytochrome b5 reductase was positive over a wide area while that of the surface near the heme-binding site of cytochrome b5 was negative. 4,6-dinitro-o-cresol 103-109 cytochrome b5 type A Homo sapiens 234-247 8880927-5 1996 This implied that the flavin-protruding side of NADH-cytochrome b5 reductase is suitable for interacting with its electron-transfer partner, cytochrome b5. 4,6-dinitro-o-cresol 22-28 cytochrome b5 type A Homo sapiens 53-66 8880927-5 1996 This implied that the flavin-protruding side of NADH-cytochrome b5 reductase is suitable for interacting with its electron-transfer partner, cytochrome b5. 4,6-dinitro-o-cresol 22-28 cytochrome b5 type A Homo sapiens 141-154 8780511-7 1996 These results suggest that the two flavin prosthetic groups that exist in catalytically active monoamine oxidase B are physically distinct. 4,6-dinitro-o-cresol 35-41 monoamine oxidase B Homo sapiens 95-114 8631763-9 1996 The lower concentration of mitochondrial FAD in flx1 mutants suggests that Flx1p is involved in flavin transport, a role that is also supported by biochemical evidence indicating more efficient flux of FAD across mitochondrial membrane vesicles prepared from wild-type strains than membrane vesicles from flx1 mutants. 4,6-dinitro-o-cresol 96-102 flavin adenine dinucleotide transporter FLX1 Saccharomyces cerevisiae S288C 48-52 8702805-8 1996 Calmodulin binding to the recombinant reductase protein increased its rate of NADPH-dependent flavin reduction and its rate of electron transfer to cytochrome c, FeCN6, or dichlorophenolindophenol to fully match the rate increases achieved when calmodulin bound to native full-length nNOS. 4,6-dinitro-o-cresol 94-100 calmodulin 1 Rattus norvegicus 0-10 8702805-8 1996 Calmodulin binding to the recombinant reductase protein increased its rate of NADPH-dependent flavin reduction and its rate of electron transfer to cytochrome c, FeCN6, or dichlorophenolindophenol to fully match the rate increases achieved when calmodulin bound to native full-length nNOS. 4,6-dinitro-o-cresol 94-100 calmodulin 1 Rattus norvegicus 245-255 8672477-7 1996 UV-visible spectra of both nNOS mutants retained the distinctive absorbance due to tightly associated oxidized flavin prosthetic groups. 4,6-dinitro-o-cresol 111-117 nitric oxide synthase 1 Homo sapiens 27-31 8702805-8 1996 Calmodulin binding to the recombinant reductase protein increased its rate of NADPH-dependent flavin reduction and its rate of electron transfer to cytochrome c, FeCN6, or dichlorophenolindophenol to fully match the rate increases achieved when calmodulin bound to native full-length nNOS. 4,6-dinitro-o-cresol 94-100 nitric oxide synthase 1 Rattus norvegicus 284-288 8702805-9 1996 Calmodulin"s activation of the reductase protein was associated with an increase in domain tryptophan and flavin fluorescence. 4,6-dinitro-o-cresol 106-112 calmodulin 1 Rattus norvegicus 0-10 8631763-9 1996 The lower concentration of mitochondrial FAD in flx1 mutants suggests that Flx1p is involved in flavin transport, a role that is also supported by biochemical evidence indicating more efficient flux of FAD across mitochondrial membrane vesicles prepared from wild-type strains than membrane vesicles from flx1 mutants. 4,6-dinitro-o-cresol 96-102 flavin adenine dinucleotide transporter FLX1 Saccharomyces cerevisiae S288C 75-80 8665924-3 1996 Analysis of the flavin spectrum of [(3)H]lazabemide-labeled human MAO-B indicated that insertion of the inhibitor did not occur into the isoalloxazine ring of FAD. 4,6-dinitro-o-cresol 16-22 monoamine oxidase B Homo sapiens 66-71 7499374-2 1995 Three flavin derivatives modified at the 2"-position of the flavin N-10 ribityl side chain were synthesized: arabinoflavin, 2"-F-2"-deoxyarabinoflavin, and 2"-deoxyriboflavin. 4,6-dinitro-o-cresol 6-12 nuclear receptor subfamily 4 group A member 1 Homo sapiens 67-71 8611587-2 1996 One flavin in resting nNOS exits as an air-stable semiquinone radical. 4,6-dinitro-o-cresol 4-10 nitric oxide synthase 1 Homo sapiens 22-26 8611587-7 1996 Analysis of an nNOS preparation that was devoid of heme but contained the flavin radical revealed that spin-spin coupling increased the rate of flavin radical relaxation by a factor of 15. 4,6-dinitro-o-cresol 74-80 nitric oxide synthase 1 Homo sapiens 15-19 8611587-11 1996 Together, the data indicate that the flavin and heme redox centers are positioned near each other in nNOS, consistent with their participating in an interdomain electron transfer. 4,6-dinitro-o-cresol 37-43 nitric oxide synthase 1 Homo sapiens 101-105 8867896-5 1996 S. acidocaldarius NADH oxidase is a monomeric protein with an estimated molecular mass of about 27 kDa, whereas S. solfataricus NADH oxidase is a dimeric protein with a molecular mass of 35 kDa per subunit; S. solfataricus NADH oxidase is purified as an FAD-containing protein, whereas S. acidocaldarius NADH oxidase does not contain a flavin molecule. 4,6-dinitro-o-cresol 336-342 ATZ20_RS09625 Sulfolobus acidocaldarius 128-140 8867896-5 1996 S. acidocaldarius NADH oxidase is a monomeric protein with an estimated molecular mass of about 27 kDa, whereas S. solfataricus NADH oxidase is a dimeric protein with a molecular mass of 35 kDa per subunit; S. solfataricus NADH oxidase is purified as an FAD-containing protein, whereas S. acidocaldarius NADH oxidase does not contain a flavin molecule. 4,6-dinitro-o-cresol 336-342 sulfurtransferase Saccharolobus solfataricus 128-140 8867896-5 1996 S. acidocaldarius NADH oxidase is a monomeric protein with an estimated molecular mass of about 27 kDa, whereas S. solfataricus NADH oxidase is a dimeric protein with a molecular mass of 35 kDa per subunit; S. solfataricus NADH oxidase is purified as an FAD-containing protein, whereas S. acidocaldarius NADH oxidase does not contain a flavin molecule. 4,6-dinitro-o-cresol 336-342 ATZ20_RS09625 Sulfolobus acidocaldarius 128-140 8605171-1 1996 Previous studies have established that 1-cyclopropyl-4-phenyl-1,2,3,6-tetrahydropyridine is an efficient time- and concentration-dependent inhibitor of the flavin-containing enzyme monoamine oxidase B (MAO-B). 4,6-dinitro-o-cresol 156-162 monoamine oxidase B Homo sapiens 181-200 8605171-1 1996 Previous studies have established that 1-cyclopropyl-4-phenyl-1,2,3,6-tetrahydropyridine is an efficient time- and concentration-dependent inhibitor of the flavin-containing enzyme monoamine oxidase B (MAO-B). 4,6-dinitro-o-cresol 156-162 monoamine oxidase B Homo sapiens 202-207 8845370-1 1995 The intense charge transfer complex between the enolate of 3-thia-octanoyl-CoA and the oxidized flavin of the medium-chain acyl-CoA dehydrogenase is discharged by the ferricenium ion with irreversible inactivation of the enzyme. 4,6-dinitro-o-cresol 96-102 acyl-CoA dehydrogenase medium chain Homo sapiens 110-145 7499374-2 1995 Three flavin derivatives modified at the 2"-position of the flavin N-10 ribityl side chain were synthesized: arabinoflavin, 2"-F-2"-deoxyarabinoflavin, and 2"-deoxyriboflavin. 4,6-dinitro-o-cresol 60-66 nuclear receptor subfamily 4 group A member 1 Homo sapiens 67-71 7499374-8 1995 It was found that NAD+ binding influences the interaction between the flavin and the reduced disulfide in the 2"-F-arabino-FAD-lipoamide dehydrogenase, presumably by altering the relative oxidation-reduction potentials. 4,6-dinitro-o-cresol 70-76 dihydrolipoamide dehydrogenase Homo sapiens 127-150 8690726-6 1995 (i) In the charge-transfer complex of reduced DAO, the reduced flavin is an electron donor. 4,6-dinitro-o-cresol 63-69 D-amino acid oxidase Homo sapiens 46-49 7559533-5 1995 Flavinylation of MAO B was achieved by introducing MAO B cDNA and different flavin derivatives simultaneously into Rib- COS-7 cells via electroporation. 4,6-dinitro-o-cresol 76-82 monoamine oxidase B Homo sapiens 17-22 7559533-6 1995 Since the addition of riboflavin, FMN, or FAD resulted in equal levels of MAO B activity, we conclude that the flavin which initially binds to apoMAO B is FAD. 4,6-dinitro-o-cresol 26-32 monoamine oxidase B Homo sapiens 74-79 8690726-7 1995 (ii) In the charge-transfer complex of reduced DAO, the reduced flavin is an electron donor and the ligand is an electron acceptor. 4,6-dinitro-o-cresol 64-70 D-amino acid oxidase Homo sapiens 47-50 8690726-8 1995 Resonance Raman studies on the charge-transfer complexes of oxidized DAO and those of reduced DAO, and calculated results of HOMO and LUMO for some enamine and imine forms, corroborated the structure of the stacking form between the flavin ring and the ligand in the active site of DAO. 4,6-dinitro-o-cresol 233-239 D-amino acid oxidase Homo sapiens 69-72 7788523-6 1995 Sequence analysis revealed the presence of flavodoxin motif, suggesting tha a cofactor of this enzyme is flavin mononucleotide, which is consistent with the previous report that the mammalian PPO had the flavin cofactor. 4,6-dinitro-o-cresol 105-111 protoporphyrinogen oxidase Homo sapiens 192-195 7628466-11 1995 Replacement of Arg44 by Lys however affects NADPH binding, resulting in a low yield of the charge-transfer species between reduced flavin and NADP+. 4,6-dinitro-o-cresol 131-137 2,4-dienoyl-CoA reductase 1 Homo sapiens 44-49 7473608-0 1995 Gender differences in hepatic expression of flavin-containing monooxygenase isoforms (FMO1, FMO3, and FMO5) in mice. 4,6-dinitro-o-cresol 44-50 flavin containing monooxygenase 1 Mus musculus 86-90 7473608-0 1995 Gender differences in hepatic expression of flavin-containing monooxygenase isoforms (FMO1, FMO3, and FMO5) in mice. 4,6-dinitro-o-cresol 44-50 flavin containing monooxygenase 3 Mus musculus 92-96 7473608-0 1995 Gender differences in hepatic expression of flavin-containing monooxygenase isoforms (FMO1, FMO3, and FMO5) in mice. 4,6-dinitro-o-cresol 44-50 flavin containing monooxygenase 5 Mus musculus 102-106 7737455-6 1995 The flavin ring structure moves substantially in the active site, probably to enable substrate and product exchange into this site and possibly to regulate the reduction of the flavin by NADPH. 4,6-dinitro-o-cresol 4-10 2,4-dienoyl-CoA reductase 1 Homo sapiens 187-192 7737455-6 1995 The flavin ring structure moves substantially in the active site, probably to enable substrate and product exchange into this site and possibly to regulate the reduction of the flavin by NADPH. 4,6-dinitro-o-cresol 177-183 2,4-dienoyl-CoA reductase 1 Homo sapiens 187-192 7757062-6 1995 These data suggest that in the normal protein the flavin center accepts electrons from ETF and that the 4Fe4S cluster reduces ubiquinone. 4,6-dinitro-o-cresol 50-56 TEA domain transcription factor 2 Homo sapiens 87-90 7530045-6 1995 Although neither purified fragment alone or in combination catalyzed NO synthesis from L-arginine, the flavin-containing fragment did catalyze cytochrome c reduction at a rate that was equivalent to that of native dimeric NOS. 4,6-dinitro-o-cresol 103-109 cytochrome c, somatic Homo sapiens 143-155 7608214-6 1995 Mixing of 8-mercapto-FAD with flavin-depleted cytochrome b558 caused a red-shift of the flavin absorption maximum from 520 nm to around 560 nm, as has been seen when a variety of other apoflavoprotein dehydrogenases bind this analog. 4,6-dinitro-o-cresol 30-36 mitochondrially encoded cytochrome b Homo sapiens 46-58 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 7713909-8 1995 The NH2-terminal amino acid sequence of the deduced PPO contains a conserved amino acid sequence that forms the dinucleotide-binding site in many flavin-containing proteins. 4,6-dinitro-o-cresol 146-152 protoporphyrinogen oxidase Homo sapiens 52-55 7896790-6 1995 Here, we provide direct evidence that p67phox alone can facilitate electron flow from NADPH to the flavin center of NADPH oxidase in the absence of p47phox, resulting in the reduction of enzyme FAD, whereas the presence of p47phox is required in order for electron transfer to proceed beyond the flavin center to the heme in cytochrome b-245 and thence to oxygen. 4,6-dinitro-o-cresol 99-105 neutrophil cytosolic factor 2 Homo sapiens 38-45 7896790-6 1995 Here, we provide direct evidence that p67phox alone can facilitate electron flow from NADPH to the flavin center of NADPH oxidase in the absence of p47phox, resulting in the reduction of enzyme FAD, whereas the presence of p47phox is required in order for electron transfer to proceed beyond the flavin center to the heme in cytochrome b-245 and thence to oxygen. 4,6-dinitro-o-cresol 99-105 neutrophil cytosolic factor 1 Homo sapiens 223-230 7896790-6 1995 Here, we provide direct evidence that p67phox alone can facilitate electron flow from NADPH to the flavin center of NADPH oxidase in the absence of p47phox, resulting in the reduction of enzyme FAD, whereas the presence of p47phox is required in order for electron transfer to proceed beyond the flavin center to the heme in cytochrome b-245 and thence to oxygen. 4,6-dinitro-o-cresol 99-105 mitochondrially encoded cytochrome b Homo sapiens 325-337 7896790-6 1995 Here, we provide direct evidence that p67phox alone can facilitate electron flow from NADPH to the flavin center of NADPH oxidase in the absence of p47phox, resulting in the reduction of enzyme FAD, whereas the presence of p47phox is required in order for electron transfer to proceed beyond the flavin center to the heme in cytochrome b-245 and thence to oxygen. 4,6-dinitro-o-cresol 296-302 neutrophil cytosolic factor 2 Homo sapiens 38-45 7896790-6 1995 Here, we provide direct evidence that p67phox alone can facilitate electron flow from NADPH to the flavin center of NADPH oxidase in the absence of p47phox, resulting in the reduction of enzyme FAD, whereas the presence of p47phox is required in order for electron transfer to proceed beyond the flavin center to the heme in cytochrome b-245 and thence to oxygen. 4,6-dinitro-o-cresol 296-302 neutrophil cytosolic factor 1 Homo sapiens 223-230 7896790-6 1995 Here, we provide direct evidence that p67phox alone can facilitate electron flow from NADPH to the flavin center of NADPH oxidase in the absence of p47phox, resulting in the reduction of enzyme FAD, whereas the presence of p47phox is required in order for electron transfer to proceed beyond the flavin center to the heme in cytochrome b-245 and thence to oxygen. 4,6-dinitro-o-cresol 296-302 mitochondrially encoded cytochrome b Homo sapiens 325-337 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 7840627-7 1995 In the range of 0-1 M urea, a completely reversible dissociation of FMN occurs and, at 3 M urea, the fluorescence values representing flavin dissociation and protein conformation changes have reached a maximum. 4,6-dinitro-o-cresol 134-140 formin 1 Homo sapiens 68-71 7528206-10 1994 Further analysis showed that CaM increased the rate of electron transfer from NADPH into the flavin centers by a factor of 20, revealing a direct activation of the NOS reductase domain by CaM. 4,6-dinitro-o-cresol 93-99 calmodulin 1 Homo sapiens 29-32 7528206-10 1994 Further analysis showed that CaM increased the rate of electron transfer from NADPH into the flavin centers by a factor of 20, revealing a direct activation of the NOS reductase domain by CaM. 4,6-dinitro-o-cresol 93-99 calmodulin 1 Homo sapiens 188-191 7528206-11 1994 In contrast, CaM"s activation of NO synthesis and substrate-independent NADPH oxidation appeared to involve flavin-to-heme electron transfer because these reactions were not activated in apo-NOS and were blocked in native NOS by agents that prevent heme iron reduction. 4,6-dinitro-o-cresol 108-114 calmodulin 1 Homo sapiens 13-16 7881908-5 1994 Complexes of OYE with p-hydroxybenzaldehyde, beta-estradiol, and an NADPH analog show all three binding at a common site, stacked on the flavin. 4,6-dinitro-o-cresol 137-143 2,4-dienoyl-CoA reductase 1 Homo sapiens 68-73 7696527-1 1994 Previous studies have established that 1-cyclopropyl-4-phenyl-1,2,3,6- tetrahydropyridine (6) is an efficient time and concentration dependent inhibitor of the flavin containing enzyme monoamine oxidase B (MAO-B). 4,6-dinitro-o-cresol 160-166 monoamine oxidase B Homo sapiens 185-204 7696527-1 1994 Previous studies have established that 1-cyclopropyl-4-phenyl-1,2,3,6- tetrahydropyridine (6) is an efficient time and concentration dependent inhibitor of the flavin containing enzyme monoamine oxidase B (MAO-B). 4,6-dinitro-o-cresol 160-166 monoamine oxidase B Homo sapiens 206-211 7928966-5 1994 Distinct homology was found between the putative MET10-encoded polypeptide and flavin-interacting parts of the sulfite reductase flavoprotein subunit (encoded by cysJ) from Escherichia coli and several other flavoproteins. 4,6-dinitro-o-cresol 79-85 sulfite reductase subunit alpha Saccharomyces cerevisiae S288C 49-54 8175767-1 1994 A gene has been constructed coding for a chimeric flavocytochrome b5 protein that comprises the soluble domain of rat hepatic cytochrome b5 as the NH2-terminal portion of the chimera and the flavin-containing domain of spinach assimilatory NADH:nitrate reductase as the C terminus. 4,6-dinitro-o-cresol 191-197 cytochrome b5 type A Rattus norvegicus 55-68 7969060-3 1994 In this paper we provide evidence, using EPR techniques, that phenyl radicals are formed during reaction of iodonium diphenyl with reduced free flavin (FMN) and protein-bound (cytochrome P450 reductase or xanthine oxidase) flavin. 4,6-dinitro-o-cresol 144-150 formin 1 Homo sapiens 152-155 7969060-3 1994 In this paper we provide evidence, using EPR techniques, that phenyl radicals are formed during reaction of iodonium diphenyl with reduced free flavin (FMN) and protein-bound (cytochrome P450 reductase or xanthine oxidase) flavin. 4,6-dinitro-o-cresol 223-229 formin 1 Homo sapiens 152-155 7519607-15 1994 In contrast, bound calmodulin does not alter the NOS affinity for L-arginine or heme ligands and may function solely as a switch that enables electrons to pass from the flavin domain onto the heme iron. 4,6-dinitro-o-cresol 169-175 calmodulin 1 Homo sapiens 19-29 7515050-3 1994 In addition, the presence of a putative calmodulin-binding sequence between the heme- and flavin-binding domains of the enzyme suggests a role for calmodulin in modulating a spatial orientation of these domains that is required for catalytic activity. 4,6-dinitro-o-cresol 90-96 calmodulin 1 Homo sapiens 40-50 7515050-3 1994 In addition, the presence of a putative calmodulin-binding sequence between the heme- and flavin-binding domains of the enzyme suggests a role for calmodulin in modulating a spatial orientation of these domains that is required for catalytic activity. 4,6-dinitro-o-cresol 90-96 calmodulin 1 Homo sapiens 147-157 8203904-1 1994 A fusion protein containing the heme domain of bovine cytochrome P450 17A and the flavin domains of rat NADPH-cytochrome P450 reductase has been genetically engineered by linking the modified cDNAs for each gene with the codons for serine and threonine. 4,6-dinitro-o-cresol 82-88 cytochrome p450 oxidoreductase Rattus norvegicus 104-135 8307196-5 1994 It is shown that, depending on the composition of the phospholipid environment, cytochrome b599 binds FAD with high or low affinity, this being accompanied by changes in flavin absorbance and fluorescence. 4,6-dinitro-o-cresol 170-176 mitochondrially encoded cytochrome b Homo sapiens 80-92 8118042-1 1994 Indoleamine 2,3-dioxygenase (IDO), a flavin-dependent enzyme that catalyzes the conversion of tryptophan to kynurenine, is induced in peripheral blood mononuclear cells by interferon-gamma (IFN gamma). 4,6-dinitro-o-cresol 37-43 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 8118042-1 1994 Indoleamine 2,3-dioxygenase (IDO), a flavin-dependent enzyme that catalyzes the conversion of tryptophan to kynurenine, is induced in peripheral blood mononuclear cells by interferon-gamma (IFN gamma). 4,6-dinitro-o-cresol 37-43 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 8118042-1 1994 Indoleamine 2,3-dioxygenase (IDO), a flavin-dependent enzyme that catalyzes the conversion of tryptophan to kynurenine, is induced in peripheral blood mononuclear cells by interferon-gamma (IFN gamma). 4,6-dinitro-o-cresol 37-43 interferon gamma Homo sapiens 172-188 8118042-1 1994 Indoleamine 2,3-dioxygenase (IDO), a flavin-dependent enzyme that catalyzes the conversion of tryptophan to kynurenine, is induced in peripheral blood mononuclear cells by interferon-gamma (IFN gamma). 4,6-dinitro-o-cresol 37-43 interferon gamma Homo sapiens 190-199 8292608-3 1994 After flavin (FMN) reduction by the substrate, reducing equivalents are transferred one by one to heme b2, and from there on to cytochrome c. 4,6-dinitro-o-cresol 6-12 cytochrome c, somatic Homo sapiens 128-140 8232555-7 1993 As photolyases are a rare class of flavoprotein that catalyse blue-light-dependent reactions, the protein encoded by HY4 has a structure consistent with that of a flavin-type blue-light photoreceptor. 4,6-dinitro-o-cresol 163-169 cryptochrome 1 Arabidopsis thaliana 117-120 7931244-3 1994 The calculation using ab initio molecular orbital methods of the electronic properties of flavin and befloxatone, a reversible inhibitor of MAO A, led to a description of the interaction between aryl-oxazolidinones and the cofactor of the enzyme. 4,6-dinitro-o-cresol 90-96 monoamine oxidase A Homo sapiens 140-145 8097689-7 1993 In this way it could be demonstrated that the major phase I biotransformation reactions for formation of urine excretable metabolites are (i) the cytochrome P-450-catalyzed N-demethylation followed by aromatic ring hydroxylation of the 4-fluoroaniline formed, and (ii) flavin-containing monooxygenase and cytochrome P-450-dependent formation of defluorinated 4-hydroxy-N-methylaniline. 4,6-dinitro-o-cresol 269-275 cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus 146-162 8218225-0 1993 Microscopic pathway for the medium-chain fatty acyl CoA dehydrogenase catalyzed oxidative half-reaction: changes in the electronic structures of flavin and CoA derivatives during catalysis. 4,6-dinitro-o-cresol 145-151 acyl-CoA dehydrogenase medium chain Homo sapiens 28-69 8218225-1 1993 In a previous communication, we demonstrated that the medium-chain fatty acyl CoA dehydrogenase (MCAD) catalyzed conversion of 3-indolepropionyl CoA (IPCoA) to trans-3-indoleacryloyl CoA (IACoA) proceeds via the formation of an intermediary species X that possesses the electronic properties of reduced flavin and highly conjugated CoA product. 4,6-dinitro-o-cresol 303-309 acyl-CoA dehydrogenase medium chain Homo sapiens 54-95 8218225-1 1993 In a previous communication, we demonstrated that the medium-chain fatty acyl CoA dehydrogenase (MCAD) catalyzed conversion of 3-indolepropionyl CoA (IPCoA) to trans-3-indoleacryloyl CoA (IACoA) proceeds via the formation of an intermediary species X that possesses the electronic properties of reduced flavin and highly conjugated CoA product. 4,6-dinitro-o-cresol 303-309 acyl-CoA dehydrogenase medium chain Homo sapiens 97-101 8443155-1 1993 Monoamine oxidases A and B have identical flavin sites but different, although overlapping, amine substrate specificity. 4,6-dinitro-o-cresol 42-48 monoamine oxidase A Homo sapiens 0-26 8395516-4 1993 By titrating XDH with redox indicator dyes of various potentials, the potentials have been determined for the flavin as well as for the 2Fe/2S centers of the enzyme at pH 7.5, 25 degrees C. The redox potential for the FAD/FADH. 4,6-dinitro-o-cresol 110-116 xanthine dehydrogenase Bos taurus 13-16 8391315-7 1993 It is concluded that the reduction of flavin leads to a strong decrease of FMN affinity to its specific binding site, and possible implications of the redox-dependent affinity changes in operation of NADH-ubiquinone reductase are discussed. 4,6-dinitro-o-cresol 38-44 formin 1 Homo sapiens 75-78 8429016-4 1993 In the second half-reaction, uracil is reduced at C-6 by flavin and protonated on the opposite face at C-5 by an enzymatic general acid with a pK of 9. 4,6-dinitro-o-cresol 57-63 complement C6 Sus scrofa 50-53 8475177-2 1993 Protonation of the flavin prior to excitation resulted in excited singlet and triplet states that abstracted an electron from the dimers and yielded the protonated flavin radical (FlH2.+), which was detected by absorption spectroscopy. 4,6-dinitro-o-cresol 19-25 perforin 1 Homo sapiens 180-184 8429016-5 1993 The hydride transfer from N-5 of the flavin to C-5 of uracil is facilitated by an enzymatic general base with a pK of 5.6 that accepts a proton from N-1 of the flavin. 4,6-dinitro-o-cresol 37-43 complement C5 Sus scrofa 47-50 8429016-5 1993 The hydride transfer from N-5 of the flavin to C-5 of uracil is facilitated by an enzymatic general base with a pK of 5.6 that accepts a proton from N-1 of the flavin. 4,6-dinitro-o-cresol 160-166 complement C5 Sus scrofa 47-50 1328233-4 1992 There is evidence that the two forms of the enzyme have different flavin environments: XDH stabilizes the neutral form of the flavin semiquinone and XO does not. 4,6-dinitro-o-cresol 66-72 xanthine dehydrogenase Homo sapiens 87-90 1328233-6 1992 XDH can be converted back to the XO form by the addition of three to four equivalents of the disulfide-forming reagent 4,4"-dithiodipyridine, suggesting that, in the XDH form of the enzyme, disulfide bonds are broken; this may cause a conformational change which creates a binding site for NAD and changes the protein structure near the flavin. 4,6-dinitro-o-cresol 337-343 xanthine dehydrogenase Homo sapiens 0-3 1328233-6 1992 XDH can be converted back to the XO form by the addition of three to four equivalents of the disulfide-forming reagent 4,4"-dithiodipyridine, suggesting that, in the XDH form of the enzyme, disulfide bonds are broken; this may cause a conformational change which creates a binding site for NAD and changes the protein structure near the flavin. 4,6-dinitro-o-cresol 337-343 xanthine dehydrogenase Homo sapiens 166-169 1328233-5 1992 Further, XDH binds the artificial flavin 8-mercapto-FAD in its neutral form, shifting the pK of this flavin by 5 pH units, while XO binds 8-mercapto-FAD in its benzoquinoid anionic form. 4,6-dinitro-o-cresol 34-40 xanthine dehydrogenase Homo sapiens 9-12 1328233-5 1992 Further, XDH binds the artificial flavin 8-mercapto-FAD in its neutral form, shifting the pK of this flavin by 5 pH units, while XO binds 8-mercapto-FAD in its benzoquinoid anionic form. 4,6-dinitro-o-cresol 101-107 xanthine dehydrogenase Homo sapiens 9-12 1456954-0 1992 Reduction of nitrofuran compounds by heart lipoamide dehydrogenase: role of flavin and the reactive disulfide groups. 4,6-dinitro-o-cresol 76-82 dihydrolipoamide dehydrogenase Homo sapiens 43-66 1456954-4 1992 The role of flavin in the nitroreductase activity was supported by (a) the nitrofuran effect on the spectral properties of anaerobic, arsenite-inhibited, NADH-reduced LipDH; (b) FAD catalytic activity in a NADH-nitrofuran model system; and (c) the nitroreductase activity of LipDH monomer. 4,6-dinitro-o-cresol 12-18 dihydrolipoamide dehydrogenase Homo sapiens 167-172 1456954-4 1992 The role of flavin in the nitroreductase activity was supported by (a) the nitrofuran effect on the spectral properties of anaerobic, arsenite-inhibited, NADH-reduced LipDH; (b) FAD catalytic activity in a NADH-nitrofuran model system; and (c) the nitroreductase activity of LipDH monomer. 4,6-dinitro-o-cresol 12-18 dihydrolipoamide dehydrogenase Homo sapiens 275-280 1631094-5 1992 DHPR is structurally and mechanistically distinct from dihydrofolate reductase, appearing to more closely resemble certain nicotinamide dinucleotide-requiring flavin-dependent enzymes, such as glutathione reductase. 4,6-dinitro-o-cresol 159-165 quinoid dihydropteridine reductase Rattus norvegicus 0-4 1627569-7 1992 Analysis of the light product of 6-azido-3-methyllumiflavin with 1H NMR and FAB mass spectrometry suggested its possible structure with a new five-membered ring, C(6) = N-O-CH = C(7), adjacent to the benzene ring of the flavin. 4,6-dinitro-o-cresol 53-59 FA complementation group B Homo sapiens 76-79 1643038-0 1992 Comparison of the dynamical structures of lipoamide dehydrogenase and glutathione reductase by time-resolved polarized flavin fluorescence. 4,6-dinitro-o-cresol 119-125 dihydrolipoamide dehydrogenase Homo sapiens 42-65 1643038-0 1992 Comparison of the dynamical structures of lipoamide dehydrogenase and glutathione reductase by time-resolved polarized flavin fluorescence. 4,6-dinitro-o-cresol 119-125 glutathione-disulfide reductase Homo sapiens 70-91 1643038-9 1992 Furthermore, it is revealed that only the flavin in glutathione reductase exhibits rapid restricted reorientational motion. 4,6-dinitro-o-cresol 42-48 glutathione-disulfide reductase Homo sapiens 52-73 1370824-3 1992 The observed marked decreases in catalytic efficiencies of substitutions of a negative charge at the normally positively charged residues with the catalytic domain of cytochrome b5 are consistent with their participation in the formation of charge pairs with carboxylate groups of the hemeprotein to optimize rapid electron transfer from the reductase flavin to the heme of the cytochrome. 4,6-dinitro-o-cresol 352-358 cytochrome b5 type A Bos taurus 167-180 1575514-5 1992 In contrast, the 14C-labeled flavin content of egg yolk, egg albumen, and blood plasma from RfBP-deficient birds was less than 10% of normal. 4,6-dinitro-o-cresol 29-35 riboflavin binding protein Gallus gallus 92-96 1567869-8 1992 The latter experiments, taking advantage of mutations in residues putatively on either side of the FMN isoalloxazine ring, suggest subtle to severe changes in the binding of the flavin prosthetic groups and, perhaps, cooperative interactions of flavin binding to NADPH-cytochrome P450 reductase. 4,6-dinitro-o-cresol 178-184 cytochrome p450 oxidoreductase Rattus norvegicus 263-294 1567869-8 1992 The latter experiments, taking advantage of mutations in residues putatively on either side of the FMN isoalloxazine ring, suggest subtle to severe changes in the binding of the flavin prosthetic groups and, perhaps, cooperative interactions of flavin binding to NADPH-cytochrome P450 reductase. 4,6-dinitro-o-cresol 245-251 cytochrome p450 oxidoreductase Rattus norvegicus 263-294 1577005-7 1992 In addition, the enzyme is able to catalyze electron transfer from NADH to various other electron acceptors (methylene blue, cytochrome c, p-nitroblue tetrazolium, 2,6-dichloroindophenol and potassium ferricyanide), even in the absence of flavin shuttles. 4,6-dinitro-o-cresol 239-245 sulfur oxidation c-type cytochrome SoxA Thermus thermophilus HB8 125-137 1946360-1 1991 The enzyme p-cresol methylhydroxylase [4-cresol: (acceptor) oxidoreductase (methyl-hydroxylating), EC 1.17.99.1] contains two subunits: a cytochrome c (electron transfer) subunit (cytochrome cpc) and a flavin (catalytic) subunit. 4,6-dinitro-o-cresol 202-208 cytochrome c, somatic Homo sapiens 138-150 1731621-8 1992 ETFB contains substoichiometric levels of an unusual FAD analogue which yields a pink flavin species on photochemical or dithionite reduction. 4,6-dinitro-o-cresol 86-92 electron transfer flavoprotein subunit beta Homo sapiens 0-4 1751496-8 1991 Therefore, Ile184 is shown to be an important residue in modulating the properties of the flavin in lipoamide dehydrogenase. 4,6-dinitro-o-cresol 90-96 dihydrolipoamide dehydrogenase Homo sapiens 100-123 2023912-1 1991 Monoamine oxidases A and B [MAOA and MAOB; amine:oxygen oxidoreductase (deaminating) (flavin-containing), EC 1.4.3.4] play important roles in the metabolism of neuroactive, vasoactive amines and the Parkinsonism-producing neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). 4,6-dinitro-o-cresol 86-92 monoamine oxidase A Homo sapiens 0-26 1761511-5 1991 The 1,602 cm-1 band, which does not shift upon isotopic substitution of phenylalanine, corresponds to the 1,605 cm-1 band of DAO purple intermediates and was assigned to a vibrational mode associated with the C(10a) = C(4a) - C(4) = O moiety of reduced flavin. 4,6-dinitro-o-cresol 253-259 D-amino acid oxidase Homo sapiens 125-128 1802973-5 1991 The activity coefficient of erythrocyte glutathione reductase showed a significant increase before the decrease of flavin content and the elevation of lipid peroxide level. 4,6-dinitro-o-cresol 115-121 glutathione-disulfide reductase Rattus norvegicus 40-61 2023912-1 1991 Monoamine oxidases A and B [MAOA and MAOB; amine:oxygen oxidoreductase (deaminating) (flavin-containing), EC 1.4.3.4] play important roles in the metabolism of neuroactive, vasoactive amines and the Parkinsonism-producing neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). 4,6-dinitro-o-cresol 86-92 monoamine oxidase A Homo sapiens 28-32 2023912-1 1991 Monoamine oxidases A and B [MAOA and MAOB; amine:oxygen oxidoreductase (deaminating) (flavin-containing), EC 1.4.3.4] play important roles in the metabolism of neuroactive, vasoactive amines and the Parkinsonism-producing neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). 4,6-dinitro-o-cresol 86-92 monoamine oxidase B Homo sapiens 37-41 24193851-0 1991 Flavin-mediated reduction of ferric leghemoglobin from soybean nodules. 4,6-dinitro-o-cresol 0-6 leghemoglobin A Glycine max 36-49 2016263-0 1991 On the ligand-protein and ligand-flavin interactions in NADPH-adrenodoxin reductase as studied by 31P- and 13C-NMR. 4,6-dinitro-o-cresol 33-39 ferredoxin reductase Bos taurus 62-83 1718826-3 1991 DT-diaphorase functions via a ping pong bi-bi kinetic mechanism involving oxidized and reduced flavin forms of the free enzyme. 4,6-dinitro-o-cresol 95-101 NAD(P)H quinone dehydrogenase 1 Homo sapiens 0-13 2016263-8 1991 These results suggest that in the complex of the enzyme with NADP+ the pyridine moiety is located in the vicinity of C(4 alpha)-C(4) region and that the pi-electron density of the 4 alpha-position of flavin is decreased in the enzyme-NADP+ complex. 4,6-dinitro-o-cresol 200-206 complement C4 Bos taurus 117-126 2016263-9 1991 This argues in favor of the electron transfer from the dihydropyridine moiety of NADPH to the electron-deficient N(5) = C(4 alpha) region of flavin. 4,6-dinitro-o-cresol 141-147 complement C4 Bos taurus 120-129 33971967-1 2021 Human dihydroorotate dehydrogenase (DHODH) is a flavin-dependent mitochondrial enzyme catalyzing the fourth step in the de novo pyrimidine synthesis pathway. 4,6-dinitro-o-cresol 48-54 dihydroorotate dehydrogenase (quinone) Homo sapiens 6-34 2233694-0 1990 Stereoselective S-oxygenation of 2-aryl-1,3-dithiolanes by the flavin-containing and cytochrome P-450 monooxygenases. 4,6-dinitro-o-cresol 63-69 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 85-101 2078640-0 1990 [Purification of flavin-containing liver polyamine oxidase and luminescent properties of the ferment]. 4,6-dinitro-o-cresol 17-23 polyamine oxidase Bos taurus 41-58 2078640-2 1990 The molecular mass, subunit composition and flavin content of the enzyme were determined; flavin, was shown to be covalently bound to the protein fragment of the polyamine oxidase molecule. 4,6-dinitro-o-cresol 44-50 polyamine oxidase Bos taurus 162-179 2078640-2 1990 The molecular mass, subunit composition and flavin content of the enzyme were determined; flavin, was shown to be covalently bound to the protein fragment of the polyamine oxidase molecule. 4,6-dinitro-o-cresol 90-96 polyamine oxidase Bos taurus 162-179 18595085-5 1990 It enables optimization of the flow rates used as well as of the methemoglobin/flavin ratio and is the forerunner of an industrial reactor. 4,6-dinitro-o-cresol 79-85 hemoglobin subunit gamma 2 Homo sapiens 65-78 2404494-9 1990 Inhibition of glutathione reductase might contribute to, or account for, the antimalarial activity of this group of flavin analogs. 4,6-dinitro-o-cresol 116-122 glutathione-disulfide reductase Homo sapiens 14-35 13382846-0 1956 Flavin stimulation of methemoglobin reduction in cell-free bacterial extracts. 4,6-dinitro-o-cresol 0-6 hemoglobin subunit gamma 2 Homo sapiens 22-35 2167843-2 1990 In order to compare the oxidation and reduction reactions of c-type cytochromes (cytochrome c552 from the green alga Monoraphidium braunii and horse heart cytochrome c) by different flavins (lumiflavin, riboflavin and FMN), laser flash photolysis studies have been carried out using either reduced or oxidized protein in the presence of triplet or semiquinone flavin, respectively. 4,6-dinitro-o-cresol 182-188 cytochrome c, somatic Equus caballus 81-93 2167843-6 1990 The rate constants for both the reduction and oxidation of cytochrome c552 by riboflavin are significantly smaller than those obtained with lumiflavin, suggesting a steric interference of the ribityl side chain in the flavin-cytochrome interaction. 4,6-dinitro-o-cresol 82-88 cytochrome c, somatic Equus caballus 59-71 2202258-6 1990 In seven isolates, a flavin compound (riboflavin, flavin adenine dinucleotide, or flavin mononucleotide) was required for azoreductase activity. 4,6-dinitro-o-cresol 21-27 NAD(P)H quinone dehydrogenase 1 Homo sapiens 122-134 2329585-16 1990 The interaction of Lys349 with atoms N-1 and O-2 of the flavin ring is probably responsible for stabilization of the anionic form of the flavin semiquinone and hydroquinone and enhancing the reactivity of atom N-5 toward sulfite. 4,6-dinitro-o-cresol 56-62 immunoglobulin kappa variable 1D-39 Homo sapiens 37-48 2404494-0 1990 Flavin analogs with antimalarial activity as glutathione reductase inhibitors. 4,6-dinitro-o-cresol 0-6 glutathione-disulfide reductase Homo sapiens 45-66 2404494-2 1990 This flavin analog and two of its derivatives were found to inhibit the antioxidant flavoenzyme glutathione reductase from human erythrocytes in its isolated form as well as in hemolysates. 4,6-dinitro-o-cresol 5-11 glutathione-disulfide reductase Homo sapiens 96-117 2113027-0 1990 On the mechanism of one-electron reduction of quinones by microsomal flavin enzymes: the kinetic analysis between cytochrome B5 and menadione. 4,6-dinitro-o-cresol 69-75 cytochrome b5 type A Homo sapiens 114-127 33971967-1 2021 Human dihydroorotate dehydrogenase (DHODH) is a flavin-dependent mitochondrial enzyme catalyzing the fourth step in the de novo pyrimidine synthesis pathway. 4,6-dinitro-o-cresol 48-54 dihydroorotate dehydrogenase (quinone) Homo sapiens 36-41 34667943-1 2021 A flavin-dependent enzyme quiescin Q6 sulfhydryl oxidase 1 (QSOX1) catalyzes the oxidation of thiol groups into disulfide bonds. 4,6-dinitro-o-cresol 2-8 quiescin Q6 sulfhydryl oxidase 1 Mus musculus 26-58 34833955-1 2021 NAD(P)H:quinone acceptor oxidoreductase-1 (NQO1) is a ubiquitous flavin adenine dinucleotide-dependent flavoprotein that promotes obligatory two-electron reductions of quinones, quinonimines, nitroaromatics, and azo dyes. 4,6-dinitro-o-cresol 65-71 NAD(P)H quinone dehydrogenase 1 Homo sapiens 0-41 34833955-1 2021 NAD(P)H:quinone acceptor oxidoreductase-1 (NQO1) is a ubiquitous flavin adenine dinucleotide-dependent flavoprotein that promotes obligatory two-electron reductions of quinones, quinonimines, nitroaromatics, and azo dyes. 4,6-dinitro-o-cresol 65-71 NAD(P)H quinone dehydrogenase 1 Homo sapiens 43-47 33818628-2 2021 The process is catalysed by proline dehydrogenase/proline oxidase (PRODH/POX), a mitochondrial flavin-dependent enzyme converting proline into 1-pyrroline-5-carboxylate (P5C). 4,6-dinitro-o-cresol 95-101 proline dehydrogenase 1 Homo sapiens 67-72 33818628-2 2021 The process is catalysed by proline dehydrogenase/proline oxidase (PRODH/POX), a mitochondrial flavin-dependent enzyme converting proline into 1-pyrroline-5-carboxylate (P5C). 4,6-dinitro-o-cresol 95-101 proline dehydrogenase 1 Homo sapiens 73-76 34224983-2 2021 Calculated spectra were compared to experimental Fourier-transform infrared (FTIR) spectra in the diagnostic 1450-1800 cm-1 range, where intense nuC=C, nuC=N, (Formula: see text) , and (Formula: see text) stretching modes of flavin"s isoalloxazine ring are found. 4,6-dinitro-o-cresol 225-231 nucleobindin 1 Homo sapiens 145-148 34224983-2 2021 Calculated spectra were compared to experimental Fourier-transform infrared (FTIR) spectra in the diagnostic 1450-1800 cm-1 range, where intense nuC=C, nuC=N, (Formula: see text) , and (Formula: see text) stretching modes of flavin"s isoalloxazine ring are found. 4,6-dinitro-o-cresol 225-231 nucleobindin 1 Homo sapiens 152-155 34800454-5 2022 The addition of Fe2O3@CNTs also not only showed a clearly electrochemical response to flavin and cytochrome C, but also reduced the electron transfer resistance when compared to the control. 4,6-dinitro-o-cresol 86-92 cytochrome c, somatic Homo sapiens 97-109 34164859-1 2021 Dihydrolipoamide dehydrogenase (DLDH) is a homodimeric flavin-dependent enzyme that catalyzes the NAD+ -dependent oxidation of dihydrolipoamide. 4,6-dinitro-o-cresol 55-61 dihydrolipoamide dehydrogenase Homo sapiens 0-30 34164859-1 2021 Dihydrolipoamide dehydrogenase (DLDH) is a homodimeric flavin-dependent enzyme that catalyzes the NAD+ -dependent oxidation of dihydrolipoamide. 4,6-dinitro-o-cresol 55-61 dihydrolipoamide dehydrogenase Homo sapiens 32-36 34605505-0 2021 Ultrafast dynamics of fully reduced flavin in catalytic structures of thymidylate synthase ThyX. 4,6-dinitro-o-cresol 36-42 thymidylate synthetase Homo sapiens 70-90 34605505-2 2021 ThyX is a flavin-dependent thymidylate synthase found in several human pathogens and absent in humans, which makes it a potential target for antimicrobial drugs. 4,6-dinitro-o-cresol 10-16 thymidylate synthetase Homo sapiens 27-47 34611047-6 2022 TMA then enters the liver through the portal vein circulation and is oxidised to trimethylamine oxide (TMAO) by the hepatic flavin-containing mono-oxygenase (FMO) family, especially FMO3. 4,6-dinitro-o-cresol 124-130 flavin containing dimethylaniline monoxygenase 3 Homo sapiens 182-186 34667943-1 2021 A flavin-dependent enzyme quiescin Q6 sulfhydryl oxidase 1 (QSOX1) catalyzes the oxidation of thiol groups into disulfide bonds. 4,6-dinitro-o-cresol 2-8 quiescin Q6 sulfhydryl oxidase 1 Mus musculus 60-65 34558787-5 2021 Silencing flad-1 resulted in a significant decrease in total flavin content, paralleled by a decrease in the level of the FAD-dependent ETFDH protein and by a secondary transcriptional down-regulation of the Rf transporter 1 (rft-1) possibly responsible for the total flavin content decrease. 4,6-dinitro-o-cresol 61-67 FAD synthase;FLavin Adenine Dinucleotide synthetase;Molybdenum cofactor biosynthesis protein-like region Caenorhabditis elegans 10-16 34442729-3 2021 Here, we discovered that proline oxidation, catalyzed by the proline oxidase Put1, a mitochondrial flavin-dependent enzyme converting proline into 1-pyrroline-5-carboxylate, controls the chronological lifespan of the yeast Saccharomyces cerevisiae. 4,6-dinitro-o-cresol 99-105 proline dehydrogenase Saccharomyces cerevisiae S288C 77-81 34558787-5 2021 Silencing flad-1 resulted in a significant decrease in total flavin content, paralleled by a decrease in the level of the FAD-dependent ETFDH protein and by a secondary transcriptional down-regulation of the Rf transporter 1 (rft-1) possibly responsible for the total flavin content decrease. 4,6-dinitro-o-cresol 268-274 FAD synthase;FLavin Adenine Dinucleotide synthetase;Molybdenum cofactor biosynthesis protein-like region Caenorhabditis elegans 10-16 34558787-5 2021 Silencing flad-1 resulted in a significant decrease in total flavin content, paralleled by a decrease in the level of the FAD-dependent ETFDH protein and by a secondary transcriptional down-regulation of the Rf transporter 1 (rft-1) possibly responsible for the total flavin content decrease. 4,6-dinitro-o-cresol 268-274 Riboflavin transporter rft-1 Caenorhabditis elegans 208-224 34558787-5 2021 Silencing flad-1 resulted in a significant decrease in total flavin content, paralleled by a decrease in the level of the FAD-dependent ETFDH protein and by a secondary transcriptional down-regulation of the Rf transporter 1 (rft-1) possibly responsible for the total flavin content decrease. 4,6-dinitro-o-cresol 268-274 Riboflavin transporter rft-1 Caenorhabditis elegans 226-231 34391120-1 2021 Flavin-Dependent Thymidylate Synthase (FDTS) encoded by ThyX gene was discovered as a new class of thymidylate synthase involved in the de novo synthesis of dTMP named only in 30 % of human pathogenic bacteria. 4,6-dinitro-o-cresol 0-6 thymidylate synthetase Homo sapiens 99-119 34435784-1 2021 This study utilizes the FMN-dependent NADH:quinone oxidoreductase from Pseudomonas aeruginosa PAO1 to investigate the effect of introducing an active site negative charge on the flavin absorption spectrum both in the absence and presence of a long-range electrostatic potential coming from solution ions. 4,6-dinitro-o-cresol 178-184 quinone oxidoreductase Pseudomonas aeruginosa PAO1 43-65 34076541-3 2021 Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively. 4,6-dinitro-o-cresol 170-176 phenylalanine hydroxylase Homo sapiens 34-36 34076541-3 2021 Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively. 4,6-dinitro-o-cresol 170-176 phenylalanine hydroxylase Homo sapiens 58-60 34076541-3 2021 Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively. 4,6-dinitro-o-cresol 170-176 phenylalanine hydroxylase Homo sapiens 68-70 34076541-3 2021 Comparison of spectra measured at pH 7 with data obtained pH 10 and pH 3 shows characteristic changes when pH is increased or lowered, mainly due to deprotonation of the flavin and nicotinamide moieties, and protonation of the adenine, respectively. 4,6-dinitro-o-cresol 170-176 phenylalanine hydroxylase Homo sapiens 107-109 34184886-2 2021 Homologues of TYW1 are found in both archaea and eukarya; archaeal homologues consist of a single domain, while eukaryal homologues contain a flavin binding domain in addition to the radical SAM domain shared with archaeal homologues. 4,6-dinitro-o-cresol 142-148 putative tRNA 4-demethylwyosine synthase Saccharomyces cerevisiae S288C 14-18 34095235-1 2021 The biliverdin reductase B (BLVRB) class of enzymes catalyze the NADPH-dependent reduction of multiple flavin substrates and are emerging as critical players in cellular redox regulation. 4,6-dinitro-o-cresol 103-109 biliverdin reductase B Homo sapiens 4-26 34095235-1 2021 The biliverdin reductase B (BLVRB) class of enzymes catalyze the NADPH-dependent reduction of multiple flavin substrates and are emerging as critical players in cellular redox regulation. 4,6-dinitro-o-cresol 103-109 biliverdin reductase B Homo sapiens 28-33 34095235-1 2021 The biliverdin reductase B (BLVRB) class of enzymes catalyze the NADPH-dependent reduction of multiple flavin substrates and are emerging as critical players in cellular redox regulation. 4,6-dinitro-o-cresol 103-109 2,4-dienoyl-CoA reductase 1 Homo sapiens 65-70 2656672-1 1989 Macroscopic pKa values associated with the influence of pH on the visible spectrum of 2-electron reduced pig heart lipoamide dehydrogenase and yeast glutathione reductase have been determined by monitoring changes in the principal flavin band near 460 nm and the charge transfer band at 540 nm. 4,6-dinitro-o-cresol 231-237 protein kinase cAMP-activated catalytic subunit alpha Sus scrofa 12-15 35397203-2 2022 Undocking of a helical C-terminal tail (CTT) in response to photoreduction of the CRY flavin cofactor gates TIM recognition. 4,6-dinitro-o-cresol 86-92 cryptochrome Drosophila melanogaster 82-85 35397203-2 2022 Undocking of a helical C-terminal tail (CTT) in response to photoreduction of the CRY flavin cofactor gates TIM recognition. 4,6-dinitro-o-cresol 86-92 timeless Drosophila melanogaster 108-111 35397203-4 2022 The assay was used to study CRY variants with residue substitutions in the flavin pocket and correlate their TIM affinities with CTT undocking, as measured by pulse-dipolar ESR spectroscopy and evaluated by molecular dynamics simulations. 4,6-dinitro-o-cresol 75-81 cryptochrome Drosophila melanogaster 28-31 35397203-4 2022 The assay was used to study CRY variants with residue substitutions in the flavin pocket and correlate their TIM affinities with CTT undocking, as measured by pulse-dipolar ESR spectroscopy and evaluated by molecular dynamics simulations. 4,6-dinitro-o-cresol 75-81 timeless Drosophila melanogaster 109-112 35397203-6 2022 In response to the flavin redox state, two conserved histidine residues contributed to a robust on/off switch by mediating CTT interactions with the flavin pocket and TIM. 4,6-dinitro-o-cresol 19-25 timeless Drosophila melanogaster 167-170 35151222-1 2022 Human dihydroorotate dehydrogenase (hDHODH) is a flavin-dependent enzyme catalyzing the fourth step of pyrimidine de novo biosynthesis. 4,6-dinitro-o-cresol 49-55 dihydroorotate dehydrogenase (quinone) Homo sapiens 36-42 2553814-1 1989 Indoleamine 2,3-dioxygenase (IDO) is a flavin-dependent enzyme which uses superoxide anion as a cosubstrate to catalyze the decyclization of the pyrrole ring of L-tryptophan to form formylkynurenine. 4,6-dinitro-o-cresol 39-45 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-27 2553814-1 1989 Indoleamine 2,3-dioxygenase (IDO) is a flavin-dependent enzyme which uses superoxide anion as a cosubstrate to catalyze the decyclization of the pyrrole ring of L-tryptophan to form formylkynurenine. 4,6-dinitro-o-cresol 39-45 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 2557903-1 1989 Substrate specificity and product inhibition have been evaluated by using purified rat liver FAD synthetase (ATP:FMN adenylyltransferase, EC 2.7.7.2), obtained by an improved purification protocol with optimized flavin affinity chromatography. 4,6-dinitro-o-cresol 212-218 flavin adenine dinucleotide synthetase 1 Rattus norvegicus 93-107 2764982-11 1989 NADPH-dependent reduction rate was inhibited by thallium chloride (an inhibitor of the flavin-centered cytochrome P-450 reductase), superoxide dismutase, and by N-ethylmaleimide; menadione increased it. 4,6-dinitro-o-cresol 87-93 cytochrome p450 oxidoreductase Rattus norvegicus 103-129 2747630-1 1989 Monoamine oxidases (MAOs) A and B, flavin-containing enzymes found in the outer mitochondrial membrane, oxidize many important biogenic and xenobiotic amines. 4,6-dinitro-o-cresol 35-41 monoamine oxidase A Homo sapiens 0-33 2732238-0 1989 Differences in protein structure of xanthine dehydrogenase and xanthine oxidase revealed by reconstitution with flavin active site probes. 4,6-dinitro-o-cresol 112-118 xanthine dehydrogenase Gallus gallus 36-58 2732238-1 1989 The native flavin, FAD, was removed from chicken liver xanthine dehydrogenase and milk xanthine oxidase by incubation with CaCl2. 4,6-dinitro-o-cresol 11-17 xanthine dehydrogenase Gallus gallus 55-77 2656672-1 1989 Macroscopic pKa values associated with the influence of pH on the visible spectrum of 2-electron reduced pig heart lipoamide dehydrogenase and yeast glutathione reductase have been determined by monitoring changes in the principal flavin band near 460 nm and the charge transfer band at 540 nm. 4,6-dinitro-o-cresol 231-237 dihydrolipoamide dehydrogenase Sus scrofa 115-138 2774489-8 1989 These results suggest that in some patients with multiple acyl-CoA dehydrogenase deficiency riboflavin supplementation may be effective in restoring the activity of SCAD, and possibly of other mitochondrial flavin-dependent enzymes. 4,6-dinitro-o-cresol 96-102 acyl-CoA dehydrogenase short chain Homo sapiens 165-169 2503499-2 1989 The reduction rate with the covalent AR-AD complex was very slow (0.030 min-1, as the flavin turnover number) compared with the reduction catalyzed by AR and AD (4.6 min-1). 4,6-dinitro-o-cresol 86-92 ferredoxin reductase Homo sapiens 37-39 2912730-4 1989 Laser-photochemically-induced dynamic nuclear polarization experiments identified tryptophan and tyrosine residues, but not histidine residues, in Ca(II)-independent discharged aequorin to be accessible to the flavin dye used. 4,6-dinitro-o-cresol 210-216 carbonic anhydrase 2 Homo sapiens 147-153 2566599-6 1989 The remarkably large downfield shift of the o-fluorobenzoate when bound to DAO was attributed to the close proximity of the ortho-fluorine atom to the flavin nucleus in comparison with meta- or para-fluorine. 4,6-dinitro-o-cresol 151-157 D-amino acid oxidase Homo sapiens 75-78 3223948-9 1988 The rate constant for cytochrome b reduction, unlike that for flavin reduction, increased with enzyme concentration, prompting the conclusion that any given cytochrome b centre is reduced preferentially by flavin groups in different molecules rather than by its partner flavin within the same monomer. 4,6-dinitro-o-cresol 62-68 mitochondrially encoded cytochrome b Homo sapiens 157-169 2531098-13 1989 The flavin compounds have been shown to be much more efficient reductans of nitroso compounds, compared to pyridine coenzymes, both in enzymatic and nonenzymatic systems; the only exception to this rule presented the extremely efficient reduction of p-substituted aryl-nitroso compounds by liver alcohol dehydrogenase. 4,6-dinitro-o-cresol 4-10 aldo-keto reductase family 1 member A1 Homo sapiens 296-317 2847775-7 1988 These results showed that in the greater part of the complexes, the flavin-mediated pathway for reduction of cytochrome c or cytochrome b5 by pyridine nucleotide was intact. 4,6-dinitro-o-cresol 68-74 cytochrome c, somatic Homo sapiens 109-121 3223948-9 1988 The rate constant for cytochrome b reduction, unlike that for flavin reduction, increased with enzyme concentration, prompting the conclusion that any given cytochrome b centre is reduced preferentially by flavin groups in different molecules rather than by its partner flavin within the same monomer. 4,6-dinitro-o-cresol 206-212 mitochondrially encoded cytochrome b Homo sapiens 22-34 3223948-9 1988 The rate constant for cytochrome b reduction, unlike that for flavin reduction, increased with enzyme concentration, prompting the conclusion that any given cytochrome b centre is reduced preferentially by flavin groups in different molecules rather than by its partner flavin within the same monomer. 4,6-dinitro-o-cresol 206-212 mitochondrially encoded cytochrome b Homo sapiens 157-169 3223948-9 1988 The rate constant for cytochrome b reduction, unlike that for flavin reduction, increased with enzyme concentration, prompting the conclusion that any given cytochrome b centre is reduced preferentially by flavin groups in different molecules rather than by its partner flavin within the same monomer. 4,6-dinitro-o-cresol 206-212 mitochondrially encoded cytochrome b Homo sapiens 22-34 3223948-9 1988 The rate constant for cytochrome b reduction, unlike that for flavin reduction, increased with enzyme concentration, prompting the conclusion that any given cytochrome b centre is reduced preferentially by flavin groups in different molecules rather than by its partner flavin within the same monomer. 4,6-dinitro-o-cresol 206-212 mitochondrially encoded cytochrome b Homo sapiens 157-169 2847775-7 1988 These results showed that in the greater part of the complexes, the flavin-mediated pathway for reduction of cytochrome c or cytochrome b5 by pyridine nucleotide was intact. 4,6-dinitro-o-cresol 68-74 cytochrome b5 type A Homo sapiens 125-138 2887428-1 1987 The presence of arginine in the active center of D-amino-acid oxidase is well documented although its role has been differently interpreted as being part of the substrate-binding site or the positively charged residue near the N1-C2 = O locus of the flavin coenzyme. 4,6-dinitro-o-cresol 250-256 D-amino acid oxidase Homo sapiens 49-69 2838087-1 1988 The spin-labeled substrate, tryptamine, was used as a structural probe of the active site of bovine liver monoamine oxidase B (amine:oxygen oxidoreductase (deaminating) (flavin-containing), EC 1.4.3.4). 4,6-dinitro-o-cresol 170-176 monoamine oxidase B Bos taurus 106-125 2898258-3 1988 L-Lactate oxidase and D-lactate dehydrogenase used the si face of the modified flavin ring while the other three enzymes showed re-side specificity. 4,6-dinitro-o-cresol 79-85 lactate dehydrogenase D Homo sapiens 22-45 3338984-1 1988 L-Gulono-gamma-lactone oxidase, one of the microsomal flavin enzymes, catalyzes the last step of L-ascorbic acid biosynthesis in many animals; however, it is missing in scurvy-prone animals such as humans, primates, and guinea pigs. 4,6-dinitro-o-cresol 54-60 gulonolactone (L-) oxidase Rattus norvegicus 0-30 3624223-6 1987 For the oxyhemoglobin-methemoglobin mixture, flavin makes a fast deoxygenation of oxyhemoglobin without a change in the oxidation state of the iron. 4,6-dinitro-o-cresol 45-51 hemoglobin subunit gamma 2 Homo sapiens 22-35 3595857-0 1987 Flavin binding site differences between lipoamide dehydrogenase and glutathione reductase as revealed by static and time-resolved flavin fluorescence. 4,6-dinitro-o-cresol 0-6 dihydrolipoamide dehydrogenase Homo sapiens 40-63 3595857-0 1987 Flavin binding site differences between lipoamide dehydrogenase and glutathione reductase as revealed by static and time-resolved flavin fluorescence. 4,6-dinitro-o-cresol 0-6 glutathione-disulfide reductase Homo sapiens 68-89 3595857-0 1987 Flavin binding site differences between lipoamide dehydrogenase and glutathione reductase as revealed by static and time-resolved flavin fluorescence. 4,6-dinitro-o-cresol 130-136 dihydrolipoamide dehydrogenase Homo sapiens 40-63 3595857-0 1987 Flavin binding site differences between lipoamide dehydrogenase and glutathione reductase as revealed by static and time-resolved flavin fluorescence. 4,6-dinitro-o-cresol 130-136 glutathione-disulfide reductase Homo sapiens 68-89 3595857-2 1987 The flavin fluorescence in glutathione reductase is quenched mainly via a dynamic mechanism, in agreement with enhanced flexibility of the flavin as inferred from rapid depolarization of the fluorescence. 4,6-dinitro-o-cresol 4-10 glutathione-disulfide reductase Homo sapiens 27-48 3595857-2 1987 The flavin fluorescence in glutathione reductase is quenched mainly via a dynamic mechanism, in agreement with enhanced flexibility of the flavin as inferred from rapid depolarization of the fluorescence. 4,6-dinitro-o-cresol 139-145 glutathione-disulfide reductase Homo sapiens 27-48 2879563-6 1986 In contrast, 6-azido-FMN Old Yellow Enzyme undergoes a very facile light-induced change, in which approximately 50% of the flavin is attached in a stable covalent linkage to the protein. 4,6-dinitro-o-cresol 123-129 formin 1 Homo sapiens 21-24 3663132-12 1987 The increased mitochondrial specific activity of short-chain acyl-CoA dehydrogenase during starvation may result from an increased availability of flavin coenzyme or an increase in enzyme catalytic efficiency. 4,6-dinitro-o-cresol 147-153 acyl-CoA dehydrogenase short chain Rattus norvegicus 49-83 3801494-9 1987 In contrast, apo-L-amino-acid oxidase binds flavin tightly (the Ka is greater than 10(7)) and the enzyme binds to anthranilate much less tightly, with a Ka of 10(3). 4,6-dinitro-o-cresol 44-50 apolipoprotein L1 Homo sapiens 13-18 3099790-0 1986 Modulation of rat polymorphonuclear leukocyte 5-lipoxygenase activity by 5-HPETE and NADH-dependent flavin inhibition. 4,6-dinitro-o-cresol 100-106 arachidonate 5-lipoxygenase Rattus norvegicus 46-60 3099790-1 1986 The effect of nicotinamide and flavin coenzymes on the 5-lipoxygenase activity has been determined in cell-free extracts from rat polymorphonuclear leukocytes. 4,6-dinitro-o-cresol 31-37 arachidonate 5-lipoxygenase Rattus norvegicus 55-69 3099790-7 1986 These results show that the 5-lipoxygenase activity is stimulated by 5-HPETE and inhibited by flavin-dependent redox transformations. 4,6-dinitro-o-cresol 94-100 arachidonate 5-lipoxygenase Rattus norvegicus 28-42 3996602-2 1985 Five of the 12 tyrosine, tryptophan and histidine residues of human lysozyme are found to be accessible to flavin dye in solution. 4,6-dinitro-o-cresol 107-113 lysozyme Homo sapiens 68-76 3801411-5 1986 The deflavo formate dehydrogenase was amenable to reconstitution with flavin analogues. 4,6-dinitro-o-cresol 70-76 SagB/ThcOx family dehydrogenase Methanobacterium formicicum 20-33 3527256-1 1986 A photochemically induced dynamic nuclear polarization (photo-CIDNP) study of yeast and horse muscle phosphoglycerate kinase with flavin dyes was undertaken to identify the histidine, tryptophan, and tyrosine resonances in the aromatic region of the simplified 1H NMR spectra of these enzymes and to investigate the effect of substrates on the resonances observable by CIDNP. 4,6-dinitro-o-cresol 130-136 phosphoglycerate kinase Saccharomyces cerevisiae S288C 101-124 3707573-0 1986 The EH2 reduced intermediate of glutathione reductase contains oxidised flavin-while EH4 does not. 4,6-dinitro-o-cresol 72-78 glutathione-disulfide reductase Homo sapiens 32-53 2992579-4 1985 We conclude for both proteins that CO2- must reduce an as yet unidentified group or groups, which in turn reduce(s) the disulfide of RNase or the flavin of riboflavin binding protein. 4,6-dinitro-o-cresol 146-152 riboflavin binding protein Gallus gallus 156-182 2992579-6 1985 The CO2--initiated reductions of the disulfide in ribonuclease and the flavin in the riboflavin binding protein are mixed first- and second-order processes. 4,6-dinitro-o-cresol 71-77 riboflavin binding protein Gallus gallus 85-111 3094532-3 1986 According to data on spectrophotometric titration of muscle glycogen phosphorylase b by FMN, each subunit of the enzyme contains one flavin-binding site. 4,6-dinitro-o-cresol 133-139 LOW QUALITY PROTEIN: glycogen phosphorylase, brain form Oryctolagus cuniculus 60-84 4055729-5 1985 Automated sequence analysis showed that the flavin-peptide from dimethylglycine dehydrogenase contained 25 amino acid residues in the following sequence: Ser-Glu-Leu-Thr-Ala-Gly-Ser- Thr-Trp-His(flavin)-Ala-Ala-Gly-Leu-Thr-Thr-Tyr-Phe-His-Pro-Gly-Ile-A sn-Leu-Lys. 4,6-dinitro-o-cresol 44-50 dimethylglycine dehydrogenase Rattus norvegicus 64-93 4055729-6 1985 The sequence determined for the flavin-peptide from sarcosine dehydrogenase contained 14 amino acid residues Leu-Thr-Ser-Gly-Thr-Thr-Trp-His(flavin)-Thr-Ala-Gly-Leu-Gly-Arg. 4,6-dinitro-o-cresol 32-38 sarcosine dehydrogenase Rattus norvegicus 52-75 3899177-1 1985 Monoamine oxidases A and B (amino: oxygen oxidoreductase (deaminating) (flavin-containing), EC 1.4.3.4) have been identified in the outer membranes of rat liver mitochondria by their covalent reaction with the inhibitor, [3H]pargyline. 4,6-dinitro-o-cresol 72-78 monoamine oxidase A Rattus norvegicus 0-56 2861204-7 1985 Only small extents of covalent attachment of the flavin to the protein were found with flavodoxin, D-amino acid oxidase, and Old Yellow Enzyme; much more extensive labeling was obtained with glucose oxidase and riboflavin-binding protein. 4,6-dinitro-o-cresol 49-55 D-amino acid oxidase Sus scrofa 99-119 6490600-3 1984 The 13C signals of 13C-enriched riboflavin or 3-methylriboflavin bound to RBP are broader than those of the free form, reflecting the restriction of flavin mobility. 4,6-dinitro-o-cresol 36-42 retinol binding protein 4 Homo sapiens 74-77 3858811-3 1985 On a nondenaturing gel, the enzyme ran as two closely spaced bands, the faster of which contained flavin. 4,6-dinitro-o-cresol 98-104 RAN, member RAS oncogene family Homo sapiens 35-38 2990445-9 1985 The protein-bound flavin of the isolated flavin subunit was reduced rapidly by the deazariboflavin semiquinone radical (k = 2.2 X 10(9) M-1 X s-1), as was the haem of the pure cytochrome c subunit (k = 3.7 X 10(9) M-1 X s-1). 4,6-dinitro-o-cresol 18-24 cytochrome c, somatic Homo sapiens 176-188 2990445-9 1985 The protein-bound flavin of the isolated flavin subunit was reduced rapidly by the deazariboflavin semiquinone radical (k = 2.2 X 10(9) M-1 X s-1), as was the haem of the pure cytochrome c subunit (k = 3.7 X 10(9) M-1 X s-1). 4,6-dinitro-o-cresol 41-47 cytochrome c, somatic Homo sapiens 176-188 6490627-0 1984 Identification of the covalently bound flavin of dimethylglycine dehydrogenase and sarcosine dehydrogenase from rat liver mitochondria. 4,6-dinitro-o-cresol 39-45 dimethylglycine dehydrogenase Rattus norvegicus 49-78 6490627-0 1984 Identification of the covalently bound flavin of dimethylglycine dehydrogenase and sarcosine dehydrogenase from rat liver mitochondria. 4,6-dinitro-o-cresol 39-45 sarcosine dehydrogenase Rattus norvegicus 83-106 6490627-9 1984 Amino acid composition and sequence analysis showed that the flavin-peptide from dimethylglycine dehydrogenase was His(flavin)-Ala-Ala-Gly-Leu. 4,6-dinitro-o-cresol 119-126 dimethylglycine dehydrogenase Rattus norvegicus 81-110 6490627-10 1984 Amino acid composition and N-terminal analysis suggested the sequence of the flavin-peptide of sarcosine dehydrogenase was His(flavin)-(Ala, Gly,Thr)-Leu. 4,6-dinitro-o-cresol 77-83 sarcosine dehydrogenase Rattus norvegicus 95-118 6149848-4 1984 It appears that, in addition to the most important regulator of GR activity, namely the flavin content of the red blood cells, there are other mechanisms which are operating in the red blood cells of anaemic animals and that these mechanisms vary among different species of animals. 4,6-dinitro-o-cresol 88-94 glutathione-disulfide reductase Bos taurus 64-66 6589590-1 1984 We have examined the affinity of two recently synthesized flavin analogs for the isoalloxazine binding site of riboflavin-binding protein (RBP). 4,6-dinitro-o-cresol 58-64 retinol binding protein 4 Homo sapiens 111-137 6589590-1 1984 We have examined the affinity of two recently synthesized flavin analogs for the isoalloxazine binding site of riboflavin-binding protein (RBP). 4,6-dinitro-o-cresol 58-64 retinol binding protein 4 Homo sapiens 139-142 6589590-3 1984 This suggested that, at the FMN or FAD level, these analogs might also bind to other apoflavoproteins, thereby providing a high potential probe for flavin enzymology. 4,6-dinitro-o-cresol 148-154 formin 1 Homo sapiens 28-31 6375661-6 1984 The results indicate that protein-bound FAD is reversibly removed from the coenzyme F420-reducing hydrogenase and that this flavin is required for the reduction of coenzyme F420. 4,6-dinitro-o-cresol 124-130 coenzyme F420 hydrogenase subunit beta Methanobacterium formicicum 75-109 6326802-1 1984 The one-electron oxidation-reduction properties of flavin in hepatic NADH-cytochrome b5 reductase were investigated by optical absorption spectroscopy, electron paramagnetic resonance (EPR), and potentiometric titration. 4,6-dinitro-o-cresol 51-57 cytochrome b5 type A Homo sapiens 74-87 6326802-4 1984 This indicates that electron transfer from flavin to cytochrome b5 proceeds in two successive one-electron steps. 4,6-dinitro-o-cresol 43-49 cytochrome b5 type A Homo sapiens 53-66 6304088-6 1983 Since reduction of cytochrome c by L-lactate requires the catalytic action of flavocytochrome b2, it is concluded that the structure of the crystalline enzyme not only allows for electron transfer from L-lactate to flavin and intramolecular electron transfer from flavin to heme, but also for the formation of a productive complex with cytochrome c. 4,6-dinitro-o-cresol 215-221 cytochrome c, somatic Homo sapiens 19-31 6304088-6 1983 Since reduction of cytochrome c by L-lactate requires the catalytic action of flavocytochrome b2, it is concluded that the structure of the crystalline enzyme not only allows for electron transfer from L-lactate to flavin and intramolecular electron transfer from flavin to heme, but also for the formation of a productive complex with cytochrome c. 4,6-dinitro-o-cresol 215-221 cytochrome c, somatic Homo sapiens 336-348 6304088-6 1983 Since reduction of cytochrome c by L-lactate requires the catalytic action of flavocytochrome b2, it is concluded that the structure of the crystalline enzyme not only allows for electron transfer from L-lactate to flavin and intramolecular electron transfer from flavin to heme, but also for the formation of a productive complex with cytochrome c. 4,6-dinitro-o-cresol 264-270 cytochrome c, somatic Homo sapiens 19-31 6304088-6 1983 Since reduction of cytochrome c by L-lactate requires the catalytic action of flavocytochrome b2, it is concluded that the structure of the crystalline enzyme not only allows for electron transfer from L-lactate to flavin and intramolecular electron transfer from flavin to heme, but also for the formation of a productive complex with cytochrome c. 4,6-dinitro-o-cresol 264-270 cytochrome c, somatic Homo sapiens 336-348 6832359-2 1983 Using the structure of glutathione reductase as a model, we suggest the following topography for leukocyte NADPH-oxidase: The binding sites of NADPH and O2 are separated from each other by the flavin ring and are thus exposed to opposite sides of the plasma membrane. 4,6-dinitro-o-cresol 193-199 glutathione-disulfide reductase Homo sapiens 23-44 7151784-7 1982 Flavin-free apoflavodoxin was reconstituted with 1-deaza-1-carbaflavin mononucleotide (1-deaza-FMN). 4,6-dinitro-o-cresol 0-6 formin 1 Homo sapiens 95-98 7165731-7 1982 Phagocytic vesicles were prepared from normal neutrophils and found to contain FAD and cytochrome b in a ratio 2.22:1, suggesting that activation of neutrophils many involve the incorporation of an additional flavin into the membrane. 4,6-dinitro-o-cresol 209-215 mitochondrially encoded cytochrome b Homo sapiens 87-99 7165731-8 1982 Under anaerobic conditions in the presence of EDTA to act as an electron donor to a flavin, the cytochrome b(-245) of neutrophil membranes was partly (12%) photoreducible, an effect increased to 100% by the addition of FMN. 4,6-dinitro-o-cresol 84-90 mitochondrially encoded cytochrome b Homo sapiens 96-108 7165731-8 1982 Under anaerobic conditions in the presence of EDTA to act as an electron donor to a flavin, the cytochrome b(-245) of neutrophil membranes was partly (12%) photoreducible, an effect increased to 100% by the addition of FMN. 4,6-dinitro-o-cresol 84-90 formin 1 Homo sapiens 219-222 24875606-6 1983 In addition, SDS-PAGE of embryonic quail [(3)H]pargyiine-labeled MAO demonstrates that the quail MAO-A and MAO-B flavin-containing subunits have apparent molecular weights of 63,000 and 62,000 respectively. 4,6-dinitro-o-cresol 113-119 monoamine oxidase B Homo sapiens 107-112 6807985-2 1982 In recent studies in this laboratory, a procedure was devised for selective removal of FMN from the purified enzyme, thus leading to the identification of FMN and FAD as the prosthetic groups of high and low reduction potential, respectively, and to the assignment of known reduction potentials to the individual flavin half-reactions. 4,6-dinitro-o-cresol 313-319 BRCA2 DNA repair associated Homo sapiens 163-166 6461017-0 1982 Photoreduction of cytochrome b557 of partially purified Neurospora nitrate reductase via its internal flavin. 4,6-dinitro-o-cresol 102-108 mitochondrially encoded cytochrome b Homo sapiens 18-30 7050653-5 1982 A complex set of factors govern the sequential protein-protein interactions which comprise this adrenodoxin shuttle mechanism; among these factors, reduction of the iron sulfur center by the flavin weakens the adrenodoxin-adrenodoxin reductase interaction, thus promoting dissociation of this complex to yield free reduced adrenodoxin. 4,6-dinitro-o-cresol 191-197 ferredoxin reductase Homo sapiens 222-243 6285959-1 1982 Laser flash photolysis has been used to determine the rate constants for the reduction of bovine cytochrome oxidase and the cytochrome c-cytochrome oxidase complex by the semiquinone and fully reduced forms of various flavin analogues (FH. 4,6-dinitro-o-cresol 218-224 LOC104968582 Bos taurus 124-136 6288003-6 1982 The simplest explanation is that NAD+ activation of hydroxylamine reduction derives solely from activation of steps involved in the reduction of cytochrome c, a flavin-mediated reaction, but these steps are only partly rate-limiting for the reduction of hydroxylamine. 4,6-dinitro-o-cresol 161-167 cytochrome c, somatic Homo sapiens 145-157 7081998-0 1982 Calorimetric studies of flavin-binding proteins: FMN and FAD binding to hen egg riboflavin-binding proteins. 4,6-dinitro-o-cresol 24-30 formin 1 Homo sapiens 49-52 7310534-2 1981 One-stage prothrombin times and Factor VII activities were lower in flavin-deficient rats than in ad libitum or pair-fed controls. 4,6-dinitro-o-cresol 68-74 coagulation factor II Rattus norvegicus 10-21 7039853-4 1982 These are (i) initial flavin-mediated (hepatic) azo reduction resulting in the formation of proximate mutagenic metabolites followed by (ii) the oxidative metabolism by S-9 resulting in the formation of ultimately mutagenic products. 4,6-dinitro-o-cresol 22-28 ribosomal protein S9 Homo sapiens 169-172 6975779-1 1982 Methylenetetrahydrofolate reductase from pig liver has been purified to homogeneity, as judged by several criteria: (i) a single band with a subunit molecular weight of 77,300 following polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate; (ii) a molecular weight determined by amino acid analysis of 74,500 per flavin, in agreement with the subunit molecular weight; and (iii) constant specific activities in the peak fractions during the final chromatography step. 4,6-dinitro-o-cresol 336-342 methylenetetrahydrofolate reductase Sus scrofa 0-35 7310534-4 1981 Hepatic vitamin K-dependent carboxylase activity was severely depressed in flavin-deficient rats when assayed with [vitamin K + NADH] and somewhat depressed with reduced vitamin K (vitamin KH2) as substrate. 4,6-dinitro-o-cresol 75-81 potassium voltage-gated channel modifier subfamily G member 1 Rattus norvegicus 189-192 7310534-7 1981 This dehydrogenase may differ from the cytosolic Warfarin-inhibitable "DT-diaphorase" in that the activity of the latter, which is reduced 50% in flavin-deficient rats, is not at all restored by one-hour flavin repletion. 4,6-dinitro-o-cresol 146-152 NAD(P)H quinone dehydrogenase 1 Rattus norvegicus 71-84 7310534-7 1981 This dehydrogenase may differ from the cytosolic Warfarin-inhibitable "DT-diaphorase" in that the activity of the latter, which is reduced 50% in flavin-deficient rats, is not at all restored by one-hour flavin repletion. 4,6-dinitro-o-cresol 204-210 NAD(P)H quinone dehydrogenase 1 Rattus norvegicus 71-84 7310534-8 1981 Flavin status-dependent differences in NADH-dependent or vitamin KH2-dependent epoxidation of vitamin K paralleled differences in the carboxylase. 4,6-dinitro-o-cresol 0-6 potassium voltage-gated channel modifier subfamily G member 1 Rattus norvegicus 65-68 6790537-1 1981 Homogenates of isolated pancreatic islets contain 40-70 times as much flavin-linked glycerol-3-phosphate dehydrogenase (EC 1.1.99.5) as homogenates of whole pancreas, liver, heart, or skeletal muscle when the activity is assayed with either iodonitrotetrazolium or with dichloroindophenol as an electron acceptor. 4,6-dinitro-o-cresol 70-76 glycerol-3-phosphate dehydrogenase 1 Rattus norvegicus 84-118 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 6273886-1 1981 Laser flash photolysis has been used to determine the second-order rate constants for the reduction of horse heart cytochrome c by the semiquinone and fully reduced forms of various flavin analogs. 4,6-dinitro-o-cresol 182-188 cytochrome c, somatic Equus caballus 115-127 6121792-2 1981 The RR spectra of complexes of DAO with benzoate derivatives excited at 514.5 nm are similar to one another and also similar to that of oxidized flavin. 4,6-dinitro-o-cresol 145-151 D-amino acid oxidase Homo sapiens 31-34 7196439-6 1981 With one exception, only lines containing the human X chromosome and human forms of two X-linked enzymes (phosphoglycerate kinase and glucose-6-phosphate dehydrogenase) expressed the human form of the flavin polypeptide of type A MAO. 4,6-dinitro-o-cresol 201-207 glucose-6-phosphate dehydrogenase Homo sapiens 134-167 6894755-7 1981 These studies indicated that position 8 of flavin bound to melilotate hydroxylase, D-amino acid oxidase, old yellow enzyme, p-OH-benzoate hydroxylase, and flavodoxin is accessible to solvent, while position 8 on L-lactate oxidase, glucose oxidase, putrescine oxidase, and riboflavin-binding protein appears to be inaccessible. 4,6-dinitro-o-cresol 43-49 D-amino acid oxidase Homo sapiens 83-103 7196439-8 1981 This evidence indicates that the structural gene for the flavin polypeptide of MAO-A is on the human X chromosome. 4,6-dinitro-o-cresol 57-63 monoamine oxidase A Homo sapiens 79-84 7459380-7 1980 Since these spectral changes occur in two metal flavin complexes with very different electronic spectra, they would seem to be due to vibrational changes induced by metal complexation at N-5 and the oxygen at C-4 of flavin rather than the details of the vibronic interactions which give rise to the resonance enhancement of the spectrum. 4,6-dinitro-o-cresol 48-54 complement C4A (Rodgers blood group) Homo sapiens 209-212 6778861-1 1981 Rat liver microsomal NADPH-cytochrome P-450 reductase was prepared free of detectable amounts of FMN by a new procedure based on the exchange of this flavin into apoflavodoxin. 4,6-dinitro-o-cresol 150-156 cytochrome p450 oxidoreductase Rattus norvegicus 21-53 7440566-5 1980 These results apparently indicate that the limiting step for the reduction of methemoglobin by the NADPH-flavin reductase system in human erythrocytes is the enzymatic reduction of flavin. 4,6-dinitro-o-cresol 105-111 hemoglobin subunit gamma 2 Homo sapiens 78-91 6249208-0 1980 Electron paramagnetic resonance properties and oxidation-reduction potentials of the molybdenum, flavin, and iron-sulfur centers of chicken liver xanthine dehydrogenase. 4,6-dinitro-o-cresol 97-103 xanthine dehydrogenase Gallus gallus 146-168 6786369-7 1980 Chlorgyline blocks primarily the "flavin moiety" of the MAO molecule, essential for the catalytic act, while the effect of deprenyl is directed to the hydrophobic part of the enzyme active center essential for the enzyme binding to tyramine. 4,6-dinitro-o-cresol 34-40 monoamine oxidase A Rattus norvegicus 56-59 7400118-0 1980 Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes. 4,6-dinitro-o-cresol 35-41 hemoglobin subunit gamma 2 Homo sapiens 13-26 7400118-0 1980 Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes. 4,6-dinitro-o-cresol 35-41 biliverdin reductase B Homo sapiens 80-102 7400118-1 1980 The reduction of methemoglobin by NADPH-flavin reductase of human erythrocytes through flavin was studied under various conditions using a reconstituted methemoglobin reductase system. 4,6-dinitro-o-cresol 40-46 hemoglobin subunit gamma 2 Homo sapiens 17-30 7400118-1 1980 The reduction of methemoglobin by NADPH-flavin reductase of human erythrocytes through flavin was studied under various conditions using a reconstituted methemoglobin reductase system. 4,6-dinitro-o-cresol 40-46 hemoglobin subunit gamma 2 Homo sapiens 153-166 7400118-2 1980 The reduction of methemoglobin by the reconstituted enzyme system could be easily detected with flavin at the physiological concentration (e.g., 0.1-1.0 microM), and the rates obtained with 0.1 and 1.0 microM FMN were 0.19 and 2.2 nmol heme reduced per min per ml, respectively, in the absence of oxygen. 4,6-dinitro-o-cresol 96-102 hemoglobin subunit gamma 2 Homo sapiens 17-30 7400118-4 1980 The reduction of methemoglobin by the reconstituted enzyme system with flavin at a physiological concentration proceeded as a zero order reaction. 4,6-dinitro-o-cresol 71-77 hemoglobin subunit gamma 2 Homo sapiens 17-30 7400118-5 1980 These results apparently suggest that the NADPH-flavin reductase system is able to reduce methemoglobin in erythrocytes at a moderate speed with about 1 microM flavin, and the reduction was estimated to vary from less than 1% to about 20% of that by the NADH-cytochrome b5 reductase system with 1 microM cytochrome b5, depending on the uptake of flavin by human erythrocytes. 4,6-dinitro-o-cresol 48-54 hemoglobin subunit gamma 2 Homo sapiens 90-103 6893275-0 1980 Magnetic circular dichroism studies on the active-site flavin of lipoamide dehydrogenase. 4,6-dinitro-o-cresol 55-61 dihydrolipoamide dehydrogenase Homo sapiens 65-88 7400118-5 1980 These results apparently suggest that the NADPH-flavin reductase system is able to reduce methemoglobin in erythrocytes at a moderate speed with about 1 microM flavin, and the reduction was estimated to vary from less than 1% to about 20% of that by the NADH-cytochrome b5 reductase system with 1 microM cytochrome b5, depending on the uptake of flavin by human erythrocytes. 4,6-dinitro-o-cresol 160-166 biliverdin reductase B Homo sapiens 42-64 7400118-5 1980 These results apparently suggest that the NADPH-flavin reductase system is able to reduce methemoglobin in erythrocytes at a moderate speed with about 1 microM flavin, and the reduction was estimated to vary from less than 1% to about 20% of that by the NADH-cytochrome b5 reductase system with 1 microM cytochrome b5, depending on the uptake of flavin by human erythrocytes. 4,6-dinitro-o-cresol 160-166 hemoglobin subunit gamma 2 Homo sapiens 90-103 220262-1 1979 Two binuclear iron-sulfur clusters (designated S-1 and S-2) are present in succinate dehydrogenase in approximately equal concentration to that of flavin. 4,6-dinitro-o-cresol 147-153 proteasome 26S subunit, non-ATPase 1 Homo sapiens 47-50 6785574-1 1980 Until recently little was known concerning the chemical details of the mechanism of interaction of flavin-linked mitochondrial membrane bound monoamine oxidase (MAO) with its substrates and inhibitors. 4,6-dinitro-o-cresol 99-105 monoamine oxidase A Rattus norvegicus 161-164 6785574-11 1980 Thus it is apparent that brain MAO also contains cysteinyl-flavin at the active center and therefore it is expected that acetylenic as well as hydrazine inhibitors form the same linkage with the flavin moiety as that formed with enzyme from peripheral tissues. 4,6-dinitro-o-cresol 59-65 monoamine oxidase A Rattus norvegicus 31-34 220262-1 1979 Two binuclear iron-sulfur clusters (designated S-1 and S-2) are present in succinate dehydrogenase in approximately equal concentration to that of flavin. 4,6-dinitro-o-cresol 147-153 ribosomal protein S2 Homo sapiens 55-58 7358682-9 1980 These results apparently indicate that FAD in the enzyme functions as a prosthetic group, and that circular dichroic spectroscopy is a good measure of the bound form of flavin in the enzyme. 4,6-dinitro-o-cresol 169-175 BRCA2 DNA repair associated Homo sapiens 39-42 16660435-3 1978 Photoreduction by blue light of the purified Cyt b requires the addition of flavin; flavoprotein isolated from D. discoideum was the most active of four flavoproteins tested in catalyzing the photoreduction while diaphorase and l-amino-acid oxidase were inactive. 4,6-dinitro-o-cresol 76-82 cytb Dictyostelium discoideum 45-50 728387-0 1978 Importance of C4a- and N5-covalent adducts in the flavin oxidation of carbanions. 4,6-dinitro-o-cresol 50-56 complement C4A (Rodgers blood group) Homo sapiens 14-17 681358-0 1978 Production of a covalent flavin linkage in lipoamide dehydrogenase. 4,6-dinitro-o-cresol 25-31 dihydrolipoamide dehydrogenase Homo sapiens 43-66 681358-10 1978 The products of the model reaction and the covalently bound FAD of lipoamide dehydrogenase appear to be the result of a nucleophilic attack on the carbon at position 8 of the flavin ring by a thiolate anion, displacing the chloride. 4,6-dinitro-o-cresol 175-181 dihydrolipoamide dehydrogenase Homo sapiens 67-90 16008-3 1977 For ferricyanide reduction, adrenodoxin reductase cycles between oxidized and 2-electron-reduced forms, reoxidation proceeding via the neutral flavin (FAD) semiquinone form (Fig. 4,6-dinitro-o-cresol 143-149 ferredoxin reductase Homo sapiens 28-49 194892-0 1977 Evidence for a thioether linkage between the flavin and polypeptide chain of Chromatium cytochrome c 552. 4,6-dinitro-o-cresol 45-51 cytochrome c, somatic Homo sapiens 88-100 269430-9 1977 By analogy with the reaction of nitroethane with D-amino acid oxidase, the data are consistent with the hypothesis that the carbanionic inhibitor forms a covalent N-5 adduct with the active site flavin. 4,6-dinitro-o-cresol 195-201 D-amino-acid oxidase Rattus norvegicus 49-69 16008-13 1977 For ferricyanide reduction by adrenodoxin reductase, the fully reduced and semiquinone forms of flavin each transfer 1 electron at oxidation-reduction potentials which differ by approximately 130 mV. 4,6-dinitro-o-cresol 96-102 ferredoxin reductase Homo sapiens 30-51 16008-14 1977 However, adrenodoxin in a complex with adrenodoxin reductase allows electrons of constant potential to be delivered from flavin to cytochrome c via the iron sulfur center... 4,6-dinitro-o-cresol 121-127 ferredoxin reductase Homo sapiens 39-60 16008-14 1977 However, adrenodoxin in a complex with adrenodoxin reductase allows electrons of constant potential to be delivered from flavin to cytochrome c via the iron sulfur center... 4,6-dinitro-o-cresol 121-127 cytochrome c, somatic Homo sapiens 131-143 15051-1 1977 D-Amino acid oxidase and xanthine oxidase, two enzymes possessing ionically bound flavin coenzymes have been studied with their flavin coenzymes derived from either 7-ethyl-8-methyl-flavin or 7-methyl-8-ethyl-flavin, vitamin-like homologues of riboflavin. 4,6-dinitro-o-cresol 82-88 D-amino acid oxidase Homo sapiens 0-20 15051-1 1977 D-Amino acid oxidase and xanthine oxidase, two enzymes possessing ionically bound flavin coenzymes have been studied with their flavin coenzymes derived from either 7-ethyl-8-methyl-flavin or 7-methyl-8-ethyl-flavin, vitamin-like homologues of riboflavin. 4,6-dinitro-o-cresol 128-134 D-amino acid oxidase Homo sapiens 0-20 856833-5 1977 MFGM contained much more flavin and much higher activities of xanthine oxidase than the RER membranes. 4,6-dinitro-o-cresol 25-31 milk fat globule EGF and factor V/VIII domain containing Homo sapiens 0-4 187594-0 1976 Spectral evidence for a flavin adduct in a monoalkylated derivative of pig heart lipoamide dehydrogenase. 4,6-dinitro-o-cresol 24-30 dihydrolipoamide dehydrogenase Sus scrofa 81-104 14671-3 1977 Aerobic titration of cytochrome P-450 reductase with NADPH indicates that an air-stable reduced form of the enzyme is generated by the addition of 0.5 mol of NADPH per mole of flavin, as judged by spectral characteristics. 4,6-dinitro-o-cresol 176-182 cytochrome p450 oxidoreductase Rattus norvegicus 21-47 12969-0 1976 The dissociation of flavin coenzymes from trypsin-solubilized NADPH/Cytochrome c (P-450) reductase of pig-liver microsomes. 4,6-dinitro-o-cresol 20-26 cytochrome c Sus scrofa 68-80 12969-1 1976 The change in fluorescence emission at 520 nm after excitation at 365 nm was used to investigate the effect of pH and ionic strength on the dissociation of flavin cofactors from microsomal NADPH/cytochrome c (P-450) reductase. 4,6-dinitro-o-cresol 156-162 cytochrome c Sus scrofa 195-207 178656-4 1976 Thus, even freshly prepared reconstitutively active enzyme preparations show EPR spectra of Center S-3 which correspond approximately to 0.5 eq per flavin; in particulate preparations this component was found in a 1:1 ratio to flavin. 4,6-dinitro-o-cresol 148-154 ribosomal protein S3 Homo sapiens 99-102 6475-8 1976 Titration of dithionite-reduced adrenodoxin reductase with NADPH also produces a distinctive spectrum, with a sharp endpoint at 1 NADPH added per reduced flavin, indicating formation of a four-electron-containing complex between reduced adrenodoxin reductase and NADPH. 4,6-dinitro-o-cresol 154-160 ferredoxin reductase Homo sapiens 32-53 6475-8 1976 Titration of dithionite-reduced adrenodoxin reductase with NADPH also produces a distinctive spectrum, with a sharp endpoint at 1 NADPH added per reduced flavin, indicating formation of a four-electron-containing complex between reduced adrenodoxin reductase and NADPH. 4,6-dinitro-o-cresol 154-160 ferredoxin reductase Homo sapiens 237-258 6475-16 1976 Comparison of these rate constants to catalytic flavin turnover numbers for reduction of various oxidants by NADPH, suggests an ordered sequential mechanism in which reduction of oxidant is accomplished by the ARH2-NADP+ complex, followed by dissociation of NADP+. 4,6-dinitro-o-cresol 48-54 low density lipoprotein receptor adaptor protein 1 Homo sapiens 210-214 8450-7 1976 The relative stability observed for the sulfite and cyanide complexes formed with various deazaflavin systems (glycolate oxidase greater than D-amino acid oxidase greater than free deazaFMN) follows the same trend observed for the stability of the sulfite complexes formed with the corresponding flavin system. 4,6-dinitro-o-cresol 95-101 hydroxyacid oxidase 2 Homo sapiens 111-128 8450-10 1976 In the case of cyanide, a complex is formed only with native glycolate oxidase, which is the flavin-containing system most susceptible to attack by the more reactive sulfite. 4,6-dinitro-o-cresol 93-99 hydroxyacid oxidase 2 Homo sapiens 61-78 804480-5 1975 The absorption spectrum of luciferase-bound FMN shows considerable alteration relative to that of free flavin. 4,6-dinitro-o-cresol 103-109 formin 1 Homo sapiens 44-47 240721-8 1975 Earlier reports on "anomalous" flavin photodegradation products absorbing around 410 nm [Holmstrom (1964) Ark. 4,6-dinitro-o-cresol 31-37 AXL receptor tyrosine kinase Homo sapiens 106-109 1244531-4 1976 The flavin was localized to the Fab fragment and was bound to IgGGar with high affinity. 4,6-dinitro-o-cresol 4-10 FA complementation group B Homo sapiens 32-35 804480-7 1975 The circular dichroism spectrum of FMN bound to luciferase has structure which correlates well with the optical absorption spectrum of the bound flavin. 4,6-dinitro-o-cresol 145-151 formin 1 Homo sapiens 35-38 1137985-2 1975 A peptide-bound flavin as the prosthetic group of L-gulono-gamma-lactone oxidase. 4,6-dinitro-o-cresol 16-22 gulonolactone (L-) oxidase Rattus norvegicus 50-80 1112779-4 1975 This complex is then reversibly converted to a different Complex II in a slow first order reaction (k2 equals 40 min--1; k-2 equals 0.07 min--1), which is accompanied by major spectral perturbations of the flavin spectrum. 4,6-dinitro-o-cresol 206-212 CD59 molecule (CD59 blood group) Homo sapiens 113-119 1112779-4 1975 This complex is then reversibly converted to a different Complex II in a slow first order reaction (k2 equals 40 min--1; k-2 equals 0.07 min--1), which is accompanied by major spectral perturbations of the flavin spectrum. 4,6-dinitro-o-cresol 206-212 CD59 molecule (CD59 blood group) Homo sapiens 137-143 1168573-2 1975 The time dependence of the fluorescence of tryptophanyl and flavin residues in lipoamide dehydrogenase has been investigated with single-photon decay spectroscopy. 4,6-dinitro-o-cresol 60-66 dihydrolipoamide dehydrogenase Homo sapiens 79-102 4375038-0 1974 The covalently bound flavin of Chromatium cytochrome c552. 4,6-dinitro-o-cresol 21-27 cytochrome c, somatic Homo sapiens 42-54 4448180-0 1974 The covalently bound flavin of Chromatium cytochrome c552. 4,6-dinitro-o-cresol 21-27 cytochrome c, somatic Homo sapiens 42-54 4592986-0 1973 Relation of phospholipase D activity to the decay of succinate dehydrogenase and of covalently bound flavin in yeast cells undergoing glucose repression. 4,6-dinitro-o-cresol 101-107 phospholipase D Saccharomyces cerevisiae S288C 12-27 4462563-1 1974 Turkey liver xanthine dehydrogenase containing the full complement of molybdenum, flavin and iron-sulphur prosthetic groups is, as normally isolated, a mixture of functional and non-functional enzyme. 4,6-dinitro-o-cresol 82-88 xanthine dehydrogenase/oxidase Meleagris gallopavo 13-35 16658941-12 1974 Finally, the nitrate reductase will exhibit a diaphorase activity and reduce the artificial electron acceptor mammalian cytochrome c in flavin-adeninedinucleotide-dependent reaction.Inhibition studies with potassium cyanide, sodium azide, and o-phenanthroline have yielded indirect evidence for metal component (s) of the enzyme.The inhibition of the NADH-requiring enzyme activities by p-hydroxymercuribenzoate has shown that an essential sulfhydryl group is involved in the initial portion of the electron transport. 4,6-dinitro-o-cresol 136-142 cytochrome c, somatic Homo sapiens 120-132 4334973-0 1972 Properties of the covalently bound flavin of chromatium cytochrome c-552 and its conversion to 8-carboxy-riboflavin. 4,6-dinitro-o-cresol 35-41 cytochrome c, somatic Homo sapiens 56-68 4749271-26 1973 It is postulated that in addition to the well-known flavin reaction, formation of H(2)O(2) may be due to interaction with an energy-dependent component of the respiratory chain at the cytochrome b level. 4,6-dinitro-o-cresol 52-58 cytochrome b, mitochondrial Rattus norvegicus 184-196 4692264-0 1973 Evidence for the involvement of a reduced flavin isomerization catalyst in the regeneration of bleached rhodopsin. 4,6-dinitro-o-cresol 42-48 rhodopsin Homo sapiens 104-113 5495148-13 1970 The photobleaching of rhodopsin sensitized by flavin is also demonstrated. 4,6-dinitro-o-cresol 46-52 rhodopsin Homo sapiens 22-31 5159777-0 1971 The flavin of chromatium cytochrome C-552. 4,6-dinitro-o-cresol 4-10 cytochrome c, somatic Homo sapiens 25-37 5822598-0 1969 Effect of flavin compounds on glutathione reductase activity: in vivo and in vitro studies. 4,6-dinitro-o-cresol 10-16 glutathione-disulfide reductase Homo sapiens 30-51 33450351-8 2021 ETF recognizes its dehydrogenase partners via a recognition loop that anchors the protein on its partner followed by dynamic movements of the ETF flavin domain that bring redox cofactors in close proximity, thus promoting electron transfer. 4,6-dinitro-o-cresol 146-152 TEA domain transcription factor 2 Homo sapiens 0-3 33450351-8 2021 ETF recognizes its dehydrogenase partners via a recognition loop that anchors the protein on its partner followed by dynamic movements of the ETF flavin domain that bring redox cofactors in close proximity, thus promoting electron transfer. 4,6-dinitro-o-cresol 146-152 TEA domain transcription factor 2 Homo sapiens 142-145 5497681-0 1970 [Activating effect of flavin coenzymes on cytochrome C transformations photosensitized by chlorophyll]. 4,6-dinitro-o-cresol 22-28 cytochrome c, somatic Homo sapiens 42-54 4233804-0 1967 Partial purification and flavin requirement of chick liver glutathione reductase. 4,6-dinitro-o-cresol 25-31 glutathione-disulfide reductase Gallus gallus 59-80 4379503-0 1965 Coenzyme specificity of D-amino acid oxidase for the flavin moiety of FAD. 4,6-dinitro-o-cresol 53-59 D-amino acid oxidase Homo sapiens 24-44 14017468-0 1963 The flavin requirement and some inhibition characteristics of rat tissue glutathione reductase. 4,6-dinitro-o-cresol 4-10 glutathione-disulfide reductase Rattus norvegicus 73-94 33637846-1 2021 Light-induction of an anionic semiquinone (SQ) flavin radical in Drosophila cryptochrome (dCRY) alters the dCRY conformation to promote binding and degradation of the circadian clock protein Timeless (TIM). 4,6-dinitro-o-cresol 47-53 timeless Drosophila melanogaster 191-199 33637846-1 2021 Light-induction of an anionic semiquinone (SQ) flavin radical in Drosophila cryptochrome (dCRY) alters the dCRY conformation to promote binding and degradation of the circadian clock protein Timeless (TIM). 4,6-dinitro-o-cresol 47-53 timeless Drosophila melanogaster 201-204 33637846-5 2021 Substitutions of flavin-proximal His378 promote CTT undocking in the dark or diminish undocking in the light, consistent with molecular dynamics simulations and TIM degradation activity. 4,6-dinitro-o-cresol 17-23 timeless Drosophila melanogaster 161-164 33245912-7 2021 Flavin-dependent enzymes have been shown to catalyze oxidative dehalogenation reactions utilizing the C4a-hydroperoxyflavin intermediate. 4,6-dinitro-o-cresol 0-6 complement C4A (Rodgers blood group) Homo sapiens 102-105 32790228-3 2020 We report synthetic flavin catalysts that contain C-6 amino modifications at the isoalloxazine core and are consequently capable of mediating halogenations outside the peptide surrounding. 4,6-dinitro-o-cresol 20-26 complement C6 Homo sapiens 50-53 33138244-7 2020 Retinal flavin levels were reduced in RhoP23H/+/Rtbdn-/- and Prph2Y141C/+/Rtbdn-/- retinas. 4,6-dinitro-o-cresol 8-14 retbindin Homo sapiens 48-53 33138244-7 2020 Retinal flavin levels were reduced in RhoP23H/+/Rtbdn-/- and Prph2Y141C/+/Rtbdn-/- retinas. 4,6-dinitro-o-cresol 8-14 peripherin 2 Homo sapiens 61-66 33138244-7 2020 Retinal flavin levels were reduced in RhoP23H/+/Rtbdn-/- and Prph2Y141C/+/Rtbdn-/- retinas. 4,6-dinitro-o-cresol 8-14 retbindin Homo sapiens 74-79