PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
8429016-4	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
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
1328233-5	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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
2016263-0	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
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
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
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
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
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
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
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
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
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
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
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
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
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	26-58
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
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
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
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
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	protein kinase cAMP-activated catalytic subunit alpha	Sus scrofa	12-15
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
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
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
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
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
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 c, somatic	Homo sapiens	109-121
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
7196439-6	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
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
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
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
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
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
7400118-0	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
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
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
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
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	proteasome 26S subunit, non-ATPase 1	Homo sapiens	47-50
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
5159777-0	1971	The flavin of chromatium cytochrome C-552.	4,6-dinitro-o-cresol	4-10	cytochrome c, somatic	Homo sapiens	25-37
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
31033286-3	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
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
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
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
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
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
30615965-0	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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
28821425-0	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
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
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
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
28970799-5	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
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
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
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
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	42-61
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
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
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
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
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
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
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
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
27461959-0	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
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
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
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
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
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
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 1	Arabidopsis thaliana	27-31
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
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
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
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
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
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
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
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
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
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	118-146
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
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
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
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
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
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
25809265-2	2015	Using small-angle x-ray scattering and nuclear magnetic resonance data, we describe the conformational free-energy landscape of the NADPH-cytochrome P450 reductase (CPR), a typical bidomain redox enzyme composed of two covalently-bound flavin domains, under various experimental conditions.	4,6-dinitro-o-cresol	236-242	cytochrome p450 oxidoreductase	Homo sapiens	132-163
25809265-2	2015	Using small-angle x-ray scattering and nuclear magnetic resonance data, we describe the conformational free-energy landscape of the NADPH-cytochrome P450 reductase (CPR), a typical bidomain redox enzyme composed of two covalently-bound flavin domains, under various experimental conditions.	4,6-dinitro-o-cresol	236-242	cytochrome p450 oxidoreductase	Homo sapiens	165-168
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
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
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
26313597-2	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
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
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
25220264-2	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
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
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 1	Arabidopsis thaliana	20-24
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
23019356-0	2012	Folate binding site of flavin-dependent thymidylate synthase.	4,6-dinitro-o-cresol	23-29	thymidylate synthetase	Homo sapiens	40-60
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
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
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
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
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
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	29-34
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
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
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
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
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
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	75-78
22205878-7	2011	Specifically, we provide evidence that reduction of the flavin moieties in CPR induces CPR opening, whereas ligand binding induces CPR closing.	4,6-dinitro-o-cresol	56-62	cytochrome p450 oxidoreductase	Homo sapiens	87-90
22205878-7	2011	Specifically, we provide evidence that reduction of the flavin moieties in CPR induces CPR opening, whereas ligand binding induces CPR closing.	4,6-dinitro-o-cresol	56-62	cytochrome p450 oxidoreductase	Homo sapiens	87-90
22205878-8	2011	A dynamic reaction cycle was created in which CPR optimizes internal electron transfer between flavin cofactors by adopting closed states and signals "ready and waiting" conformations to partner CYP enzymes by adopting more open states.	4,6-dinitro-o-cresol	95-101	cytochrome p450 oxidoreductase	Homo sapiens	46-49
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
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
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
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
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
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	nitric oxide synthase 2	Rattus norvegicus	16-20
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
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
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	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	20-25
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
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
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
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
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
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
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
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
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
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
20093143-0	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
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
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	lysine demethylase 1B	Homo sapiens	35-39
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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	18-24	glutathione-disulfide reductase	Homo sapiens	50-52
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
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	4-57
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
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
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
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
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
18086551-0	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
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
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
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
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
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	92-127
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
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	159-165	lysine demethylase 1A	Homo sapiens	39-43
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
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
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
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	0-3
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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	0-35
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
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
15811342-0	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
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
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
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
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
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
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
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
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
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
15301527-0	2004	Mechanistic studies of a flavin-dependent thymidylate synthase.	4,6-dinitro-o-cresol	25-31	thymidylate synthetase	Homo sapiens	42-62
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
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	22-28	myoglobin	Homo sapiens	48-57
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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	121-127	monoamine oxidase B	Homo sapiens	14-19
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
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
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
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
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
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
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
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
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
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
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	44-79
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
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
11872165-7	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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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	4-28
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
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
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
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
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
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
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
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
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
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
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
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
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
10716694-0	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
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
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
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
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
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
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	63-69	monoamine oxidase A	Homo sapiens	0-5
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
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
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
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
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
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
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
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
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
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
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
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
9535883-9	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
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
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
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
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
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
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
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
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	131-137	peroxiredoxin 5	Homo sapiens	13-34
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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	6-12	nuclear receptor subfamily 4 group A member 1	Homo sapiens	67-71
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	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
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
8690726-6	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
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
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
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