BRENDA - Enzyme Database
show all sequences of 1.6.5.2

The structural and functional basis of catalysis mediated by NAD(P)Hacceptor oxidoreductase (FerB) of Paracoccus denitrificans

Sedlacek, V.; Klumpler, T.; Marek, J.; Kucera, I.; PLoS ONE 9, e96262 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene ferB, sequence comparisons and phylogenetic tree, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Paracoccus denitrificans
Crystallization (Commentary)
Crystallization
Organism
purified recombinant wild-type andd selenomethionine-labeled His6-tagged wild-type enzyme in complex with NADH, X-ray diffraction structure determination and analysis at 1.4-1.75 A resolution, multiple wavelength anomalous dispersion using selenium anomalous signal, modeling
Paracoccus denitrificans
Engineering
Amino acid exchange
Commentary
Organism
E77A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
E77K
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
E77L
site-directed mutagenesis, almost inactive mutant
Paracoccus denitrificans
E77M
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
G115F
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
G115I
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
G118F
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
G118I
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
N18A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
Paracoccus denitrificans
N79A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
Paracoccus denitrificans
R13A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
Paracoccus denitrificans
R80E
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
R80K
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
R80L
site-directed mutagenesis, almost inactive mutant
Paracoccus denitrificans
R80M
site-directed mutagenesis, almost inactive mutant
Paracoccus denitrificans
R95A
site-directed mutagenesis, replacing the bulky Arg95 in the vicinity of the active site with alanine substantially enhances the activity of the mutant towards external flavins compared to the wild-type; site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
Paracoccus denitrificans
R95E
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
S113A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
S11A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
Paracoccus denitrificans
S16A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
Paracoccus denitrificans
Y46A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
Paracoccus denitrificans
Y78A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type; site-directed mutagenesis, the mutation does not at all affect the enzyme activity
Paracoccus denitrificans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetics, stopped-flow spectrophotometry
Paracoccus denitrificans
0.02
-
NADH
pH 7.4, 25C, recombinant mutant R95A
Paracoccus denitrificans
0.022
-
NADH
pH 7.4, 25C, recombinant wild-type enzyme
Paracoccus denitrificans
0.03
-
NADH
pH 7.4, 25C, recombinant mutant E77K; pH 7.4, 25C, recombinant mutant R80E
Paracoccus denitrificans
0.038
-
NADH
pH 7.4, 25C, recombinant mutant G118I
Paracoccus denitrificans
0.04
-
NADH
pH 7.4, 25C, recombinant mutant Y78A
Paracoccus denitrificans
0.06
-
NADH
pH 7.4, 25C, recombinant mutant S113A
Paracoccus denitrificans
0.07
-
NADH
pH 7.4, 25C, recombinant mutant R95E
Paracoccus denitrificans
0.085
-
NADH
pH 7.4, 25C, recombinant mutant G118F
Paracoccus denitrificans
0.18
-
NADH
pH 7.4, 25C, recombinant mutant E77A
Paracoccus denitrificans
0.25
-
NADH
pH 7.4, 25C, recombinant mutant E77L
Paracoccus denitrificans
0.35
-
NADH
pH 7.4, 25C, recombinant mutant R80K
Paracoccus denitrificans
0.41
-
NADH
pH 7.4, 25C, recombinant mutant G115F
Paracoccus denitrificans
0.42
-
NADH
pH 7.4, 25C, recombinant mutant E77M
Paracoccus denitrificans
0.58
-
NADH
pH 7.4, 25C, recombinant mutant R80L
Paracoccus denitrificans
0.63
-
NADH
pH 7.4, 25C, recombinant mutant G115I
Paracoccus denitrificans
0.78
-
NADH
pH 7.4, 25C, recombinant mutant R80M
Paracoccus denitrificans
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Paracoccus denitrificans
5737
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Paracoccus denitrificans
the flavoprotein ferric reductase B, FerB, from Paracoccus denitrificans is one of two major enzymes able to reduce Fe(III)-ligand complexes when NADH is the electron donor. The protein is also active as a chromate reductase and, to a substantially greater extent, as a quinone reductase
?
-
-
-
additional information
Paracoccus denitrificans Pd 1222
the flavoprotein ferric reductase B, FerB, from Paracoccus denitrificans is one of two major enzymes able to reduce Fe(III)-ligand complexes when NADH is the electron donor. The protein is also active as a chromate reductase and, to a substantially greater extent, as a quinone reductase
?
-
-
-
NADH + H+ + a quinone
Paracoccus denitrificans
hydride transfer occurs from the 4-pro-S position of NADH to the solvent-accessible si side of the flavin ring
NAD+ + a hydroquinone
-
-
r
NADH + H+ + a quinone
Paracoccus denitrificans Pd 1222
hydride transfer occurs from the 4-pro-S position of NADH to the solvent-accessible si side of the flavin ring
NAD+ + a hydroquinone
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Paracoccus denitrificans
A1B9E3
-
-
Paracoccus denitrificans Pd 1222
A1B9E3
-
-
Purification (Commentary)
Commentary
Organism
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)
Paracoccus denitrificans
Reaction
Reaction
Commentary
Organism
NAD(P)H + H+ + a quinone = NAD(P)+ + a hydroquinone
the activity obeys the standard bi-bi ping-pong reaction mechanism
Paracoccus denitrificans
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the flavoprotein ferric reductase B, FerB, from Paracoccus denitrificans is one of two major enzymes able to reduce Fe(III)-ligand complexes when NADH is the electron donor. The protein is also active as a chromate reductase and, to a substantially greater extent, as a quinone reductase
743659
Paracoccus denitrificans
?
-
-
-
-
additional information
low activity with riboflavin instead of FMN
743659
Paracoccus denitrificans
?
-
-
-
-
additional information
the flavoprotein ferric reductase B, FerB, from Paracoccus denitrificans is one of two major enzymes able to reduce Fe(III)-ligand complexes when NADH is the electron donor. The protein is also active as a chromate reductase and, to a substantially greater extent, as a quinone reductase
743659
Paracoccus denitrificans Pd 1222
?
-
-
-
-
additional information
low activity with riboflavin instead of FMN
743659
Paracoccus denitrificans Pd 1222
?
-
-
-
-
NADH + H+ + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
i.e. ubiquinone-10, UQ-10, a quinone electron acceptor
743659
Paracoccus denitrificans
NAD+ + 2,3-dimethoxy-5-methyl-1,4-benzoquinol
-
-
-
r
NADH + H+ + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
i.e. ubiquinone-10, UQ-10, a quinone electron acceptor
743659
Paracoccus denitrificans Pd 1222
NAD+ + 2,3-dimethoxy-5-methyl-1,4-benzoquinol
-
-
-
r
NADH + H+ + 2,3-dimethoxy-5-methyl-2,5-cyclohexadiene-1,4-dione
i.e. ubiquinone-0, UQ-0, a quinone electron acceptor
743659
Paracoccus denitrificans
NAD+ + 2,3-dimethoxy-5-methylbenzene-1,4-diol
-
-
-
r
NADH + H+ + a quinone
hydride transfer occurs from the 4-pro-S position of NADH to the solvent-accessible si side of the flavin ring
743659
Paracoccus denitrificans
NAD+ + a hydroquinone
-
-
-
r
NADH + H+ + a quinone
hydride transfer occurs from the 4-pro-S position of NADH to the solvent-accessible si side of the flavin ring. The first, reductive half-reaction of flavin cofactor is rate-limiting
743659
Paracoccus denitrificans
NAD+ + a hydroquinone
-
-
-
r
NADH + H+ + a quinone
hydride transfer occurs from the 4-pro-S position of NADH to the solvent-accessible si side of the flavin ring
743659
Paracoccus denitrificans Pd 1222
NAD+ + a hydroquinone
-
-
-
r
NADH + H+ + a quinone
hydride transfer occurs from the 4-pro-S position of NADH to the solvent-accessible si side of the flavin ring. The first, reductive half-reaction of flavin cofactor is rate-limiting
743659
Paracoccus denitrificans Pd 1222
NAD+ + a hydroquinone
-
-
-
r
Subunits
Subunits
Commentary
Organism
dimer
a head-to-tail dimer with two flavin mononucleotide groups bound at the opposite sides of the subunit interface. The dimers tend to self-associate to a tetrameric form at higher protein concentrations. Amino acid residues important for the binding of FMN and NADH and for the catalytic activity are identified
Paracoccus denitrificans
More
occurrence of a dimer-tetramer equilibrium
Paracoccus denitrificans
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
additional information
-
stopped-flow spectrophotometry at 10C
Paracoccus denitrificans
25
-
assay at
Paracoccus denitrificans
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.072
-
NADH
pH 7.4, 25C, recombinant mutant E77L
Paracoccus denitrificans
0.142
-
NADH
pH 7.4, 25C, recombinant mutant R80L
Paracoccus denitrificans
0.275
-
NADH
pH 7.4, 25C, recombinant mutant R80E
Paracoccus denitrificans
0.302
-
NADH
pH 7.4, 25C, recombinant mutant R80M
Paracoccus denitrificans
0.75
-
NADH
pH 7.4, 25C, recombinant mutant E77K
Paracoccus denitrificans
1.7
-
NADH
pH 7.4, 25C, recombinant mutant G115I
Paracoccus denitrificans
2.2
-
NADH
pH 7.4, 25C, recombinant mutant G115F
Paracoccus denitrificans
2.5
-
NADH
pH 7.4, 25C, recombinant mutant E77M
Paracoccus denitrificans
9.5
-
NADH
pH 7.4, 25C, recombinant mutant R80K
Paracoccus denitrificans
12
-
NADH
pH 7.4, 25C, recombinant mutant G118I
Paracoccus denitrificans
17.9
-
NADH
pH 7.4, 25C, recombinant mutant E77A
Paracoccus denitrificans
21.1
-
NADH
pH 7.4, 25C, recombinant mutant R95E
Paracoccus denitrificans
76.7
-
NADH
pH 7.4, 25C, recombinant mutant S113A
Paracoccus denitrificans
77
-
NADH
pH 7.4, 25C, recombinant mutant G118F
Paracoccus denitrificans
146
-
NADH
pH 7.4, 25C, recombinant mutant R95A
Paracoccus denitrificans
196
-
NADH
pH 7.4, 25C, recombinant mutant Y78A
Paracoccus denitrificans
258
-
NADH
pH 7.4, 25C, recombinant wild-type enzyme
Paracoccus denitrificans
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Paracoccus denitrificans
Cofactor
Cofactor
Commentary
Organism
Structure
FMN
flavin mononucleotide groups are non-covalently bound at the opposite sides of the subunit interface of the enzyme dimer, binding site structure analysis, overview. The flavin is required for activity, residue Glu77 anchors a conserved water molecule in close proximity to the O2 of FMN, with the probable role of facilitating flavin reduction. interaction of apoenzyme with the FMN phosphate significantly stabilizes the complex with the enzyme. Hydride transfer occurs from the 4-pro-S position of NADH to the solvent-accessible si side of the flavin ring. The first, reductive half-reaction of flavin cofactor is rate-limiting. Importance of residue Ser11, Arg13, Ser16 and Asn18 for FMN binding, and of the tyrosine residues Tyr46 and Tyr78 and possibly also Ser113 for capturing the isoalloxazine ring of FMN
Paracoccus denitrificans
additional information
the enzyme is not NADPH-dependent, but NADH-dependent
Paracoccus denitrificans
NAD+
-
Paracoccus denitrificans
NADH
-
Paracoccus denitrificans
riboflavin
low activity with riboflavin instead of FMN
Paracoccus denitrificans
Cloned(Commentary) (protein specific)
Commentary
Organism
gene ferB, sequence comparisons and phylogenetic tree, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Paracoccus denitrificans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FMN
flavin mononucleotide groups are non-covalently bound at the opposite sides of the subunit interface of the enzyme dimer, binding site structure analysis, overview. The flavin is required for activity, residue Glu77 anchors a conserved water molecule in close proximity to the O2 of FMN, with the probable role of facilitating flavin reduction. interaction of apoenzyme with the FMN phosphate significantly stabilizes the complex with the enzyme. Hydride transfer occurs from the 4-pro-S position of NADH to the solvent-accessible si side of the flavin ring. The first, reductive half-reaction of flavin cofactor is rate-limiting. Importance of residue Ser11, Arg13, Ser16 and Asn18 for FMN binding, and of the tyrosine residues Tyr46 and Tyr78 and possibly also Ser113 for capturing the isoalloxazine ring of FMN
Paracoccus denitrificans
additional information
the enzyme is not NADPH-dependent, but NADH-dependent
Paracoccus denitrificans
NAD+
-
Paracoccus denitrificans
NADH
-
Paracoccus denitrificans
riboflavin
low activity with riboflavin instead of FMN
Paracoccus denitrificans
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant wild-type andd selenomethionine-labeled His6-tagged wild-type enzyme in complex with NADH, X-ray diffraction structure determination and analysis at 1.4-1.75 A resolution, multiple wavelength anomalous dispersion using selenium anomalous signal, modeling
Paracoccus denitrificans
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E77A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
E77K
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
E77L
site-directed mutagenesis, almost inactive mutant
Paracoccus denitrificans
E77M
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
G115F
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
G115I
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
G118F
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
G118I
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
N18A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
Paracoccus denitrificans
N79A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
Paracoccus denitrificans
R13A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
Paracoccus denitrificans
R80E
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
R80K
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
R80L
site-directed mutagenesis, almost inactive mutant
Paracoccus denitrificans
R80M
site-directed mutagenesis, almost inactive mutant
Paracoccus denitrificans
R95A
site-directed mutagenesis, replacing the bulky Arg95 in the vicinity of the active site with alanine substantially enhances the activity of the mutant towards external flavins compared to the wild-type; site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
Paracoccus denitrificans
R95E
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
S113A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
Paracoccus denitrificans
S11A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
Paracoccus denitrificans
S16A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
Paracoccus denitrificans
Y46A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
Paracoccus denitrificans
Y78A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type; site-directed mutagenesis, the mutation does not at all affect the enzyme activity
Paracoccus denitrificans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetics, stopped-flow spectrophotometry
Paracoccus denitrificans
0.02
-
NADH
pH 7.4, 25C, recombinant mutant R95A
Paracoccus denitrificans
0.022
-
NADH
pH 7.4, 25C, recombinant wild-type enzyme
Paracoccus denitrificans
0.03
-
NADH
pH 7.4, 25C, recombinant mutant E77K; pH 7.4, 25C, recombinant mutant R80E
Paracoccus denitrificans
0.038
-
NADH
pH 7.4, 25C, recombinant mutant G118I
Paracoccus denitrificans
0.04
-
NADH
pH 7.4, 25C, recombinant mutant Y78A
Paracoccus denitrificans
0.06
-
NADH
pH 7.4, 25C, recombinant mutant S113A
Paracoccus denitrificans
0.07
-
NADH
pH 7.4, 25C, recombinant mutant R95E
Paracoccus denitrificans
0.085
-
NADH
pH 7.4, 25C, recombinant mutant G118F
Paracoccus denitrificans
0.18
-
NADH
pH 7.4, 25C, recombinant mutant E77A
Paracoccus denitrificans
0.25
-
NADH
pH 7.4, 25C, recombinant mutant E77L
Paracoccus denitrificans
0.35
-
NADH
pH 7.4, 25C, recombinant mutant R80K
Paracoccus denitrificans
0.41
-
NADH
pH 7.4, 25C, recombinant mutant G115F
Paracoccus denitrificans
0.42
-
NADH
pH 7.4, 25C, recombinant mutant E77M
Paracoccus denitrificans
0.58
-
NADH
pH 7.4, 25C, recombinant mutant R80L
Paracoccus denitrificans
0.63
-
NADH
pH 7.4, 25C, recombinant mutant G115I
Paracoccus denitrificans
0.78
-
NADH
pH 7.4, 25C, recombinant mutant R80M
Paracoccus denitrificans
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Paracoccus denitrificans
5737
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Paracoccus denitrificans
the flavoprotein ferric reductase B, FerB, from Paracoccus denitrificans is one of two major enzymes able to reduce Fe(III)-ligand complexes when NADH is the electron donor. The protein is also active as a chromate reductase and, to a substantially greater extent, as a quinone reductase
?
-
-
-
additional information
Paracoccus denitrificans Pd 1222
the flavoprotein ferric reductase B, FerB, from Paracoccus denitrificans is one of two major enzymes able to reduce Fe(III)-ligand complexes when NADH is the electron donor. The protein is also active as a chromate reductase and, to a substantially greater extent, as a quinone reductase
?
-
-
-
NADH + H+ + a quinone
Paracoccus denitrificans
hydride transfer occurs from the 4-pro-S position of NADH to the solvent-accessible si side of the flavin ring
NAD+ + a hydroquinone
-
-
r
NADH + H+ + a quinone
Paracoccus denitrificans Pd 1222
hydride transfer occurs from the 4-pro-S position of NADH to the solvent-accessible si side of the flavin ring
NAD+ + a hydroquinone
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)
Paracoccus denitrificans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the flavoprotein ferric reductase B, FerB, from Paracoccus denitrificans is one of two major enzymes able to reduce Fe(III)-ligand complexes when NADH is the electron donor. The protein is also active as a chromate reductase and, to a substantially greater extent, as a quinone reductase
743659
Paracoccus denitrificans
?
-
-
-
-
additional information
low activity with riboflavin instead of FMN
743659
Paracoccus denitrificans
?
-
-
-
-
additional information
the flavoprotein ferric reductase B, FerB, from Paracoccus denitrificans is one of two major enzymes able to reduce Fe(III)-ligand complexes when NADH is the electron donor. The protein is also active as a chromate reductase and, to a substantially greater extent, as a quinone reductase
743659
Paracoccus denitrificans Pd 1222
?
-
-
-
-
additional information
low activity with riboflavin instead of FMN
743659
Paracoccus denitrificans Pd 1222
?
-
-
-
-
NADH + H+ + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
i.e. ubiquinone-10, UQ-10, a quinone electron acceptor
743659
Paracoccus denitrificans
NAD+ + 2,3-dimethoxy-5-methyl-1,4-benzoquinol
-
-
-
r
NADH + H+ + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
i.e. ubiquinone-10, UQ-10, a quinone electron acceptor
743659
Paracoccus denitrificans Pd 1222
NAD+ + 2,3-dimethoxy-5-methyl-1,4-benzoquinol
-
-
-
r
NADH + H+ + 2,3-dimethoxy-5-methyl-2,5-cyclohexadiene-1,4-dione
i.e. ubiquinone-0, UQ-0, a quinone electron acceptor
743659
Paracoccus denitrificans
NAD+ + 2,3-dimethoxy-5-methylbenzene-1,4-diol
-
-
-
r
NADH + H+ + a quinone
hydride transfer occurs from the 4-pro-S position of NADH to the solvent-accessible si side of the flavin ring
743659
Paracoccus denitrificans
NAD+ + a hydroquinone
-
-
-
r
NADH + H+ + a quinone
hydride transfer occurs from the 4-pro-S position of NADH to the solvent-accessible si side of the flavin ring. The first, reductive half-reaction of flavin cofactor is rate-limiting
743659
Paracoccus denitrificans
NAD+ + a hydroquinone
-
-
-
r
NADH + H+ + a quinone
hydride transfer occurs from the 4-pro-S position of NADH to the solvent-accessible si side of the flavin ring
743659
Paracoccus denitrificans Pd 1222
NAD+ + a hydroquinone
-
-
-
r
NADH + H+ + a quinone
hydride transfer occurs from the 4-pro-S position of NADH to the solvent-accessible si side of the flavin ring. The first, reductive half-reaction of flavin cofactor is rate-limiting
743659
Paracoccus denitrificans Pd 1222
NAD+ + a hydroquinone
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
a head-to-tail dimer with two flavin mononucleotide groups bound at the opposite sides of the subunit interface. The dimers tend to self-associate to a tetrameric form at higher protein concentrations. Amino acid residues important for the binding of FMN and NADH and for the catalytic activity are identified
Paracoccus denitrificans
More
occurrence of a dimer-tetramer equilibrium
Paracoccus denitrificans
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
additional information
-
stopped-flow spectrophotometry at 10C
Paracoccus denitrificans
25
-
assay at
Paracoccus denitrificans
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.072
-
NADH
pH 7.4, 25C, recombinant mutant E77L
Paracoccus denitrificans
0.142
-
NADH
pH 7.4, 25C, recombinant mutant R80L
Paracoccus denitrificans
0.275
-
NADH
pH 7.4, 25C, recombinant mutant R80E
Paracoccus denitrificans
0.302
-
NADH
pH 7.4, 25C, recombinant mutant R80M
Paracoccus denitrificans
0.75
-
NADH
pH 7.4, 25C, recombinant mutant E77K
Paracoccus denitrificans
1.7
-
NADH
pH 7.4, 25C, recombinant mutant G115I
Paracoccus denitrificans
2.2
-
NADH
pH 7.4, 25C, recombinant mutant G115F
Paracoccus denitrificans
2.5
-
NADH
pH 7.4, 25C, recombinant mutant E77M
Paracoccus denitrificans
9.5
-
NADH
pH 7.4, 25C, recombinant mutant R80K
Paracoccus denitrificans
12
-
NADH
pH 7.4, 25C, recombinant mutant G118I
Paracoccus denitrificans
17.9
-
NADH
pH 7.4, 25C, recombinant mutant E77A
Paracoccus denitrificans
21.1
-
NADH
pH 7.4, 25C, recombinant mutant R95E
Paracoccus denitrificans
76.7
-
NADH
pH 7.4, 25C, recombinant mutant S113A
Paracoccus denitrificans
77
-
NADH
pH 7.4, 25C, recombinant mutant G118F
Paracoccus denitrificans
146
-
NADH
pH 7.4, 25C, recombinant mutant R95A
Paracoccus denitrificans
196
-
NADH
pH 7.4, 25C, recombinant mutant Y78A
Paracoccus denitrificans
258
-
NADH
pH 7.4, 25C, recombinant wild-type enzyme
Paracoccus denitrificans
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Paracoccus denitrificans
General Information
General Information
Commentary
Organism
evolution
enzyme FerB is listed in the NADPH-dependent FMN reductase family, PF03358
Paracoccus denitrificans
additional information
importance of residue Ser11, Arg13, Ser16 and Asn18 for FMN binding, and of the tyrosine residues Tyr46 and Tyr78 and possibly also Ser113 for capturing the isoalloxazine ring of FMN. FMN and NADH docking, overview
Paracoccus denitrificans
physiological function
FerB from Paracoccus denitrificans is a soluble cytoplasmic flavoprotein that accepts redox equivalents from NADH or NADPH and transfers them to various acceptors such as quinones, ferric complexes and chromate
Paracoccus denitrificans
General Information (protein specific)
General Information
Commentary
Organism
evolution
enzyme FerB is listed in the NADPH-dependent FMN reductase family, PF03358
Paracoccus denitrificans
additional information
importance of residue Ser11, Arg13, Ser16 and Asn18 for FMN binding, and of the tyrosine residues Tyr46 and Tyr78 and possibly also Ser113 for capturing the isoalloxazine ring of FMN. FMN and NADH docking, overview
Paracoccus denitrificans
physiological function
FerB from Paracoccus denitrificans is a soluble cytoplasmic flavoprotein that accepts redox equivalents from NADH or NADPH and transfers them to various acceptors such as quinones, ferric complexes and chromate
Paracoccus denitrificans
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.24
-
NADH
pH 7.4, 25C, recombinant mutant R80L
Paracoccus denitrificans
0.29
-
NADH
pH 7.4, 25C, recombinant mutant E77L
Paracoccus denitrificans
0.39
-
NADH
pH 7.4, 25C, recombinant mutant R80M
Paracoccus denitrificans
2.7
-
NADH
pH 7.4, 25C, recombinant mutant G115I
Paracoccus denitrificans
5.4
-
NADH
pH 7.4, 25C, recombinant mutant G115F
Paracoccus denitrificans
6
-
NADH
pH 7.4, 25C, recombinant mutant E77M
Paracoccus denitrificans
9.2
-
NADH
pH 7.4, 25C, recombinant mutant R80E
Paracoccus denitrificans
25
-
NADH
pH 7.4, 25C, recombinant mutant E77K
Paracoccus denitrificans
99
-
NADH
pH 7.4, 25C, recombinant mutant E77A
Paracoccus denitrificans
302
-
NADH
pH 7.4, 25C, recombinant mutant R95E
Paracoccus denitrificans
316
-
NADH
pH 7.4, 25C, recombinant mutant G118I
Paracoccus denitrificans
906
-
NADH
pH 7.4, 25C, recombinant mutant G118F
Paracoccus denitrificans
1278
-
NADH
pH 7.4, 25C, recombinant mutant S113A
Paracoccus denitrificans
2767
-
NADH
pH 7.4, 25C, recombinant mutant R80K
Paracoccus denitrificans
4900
-
NADH
pH 7.4, 25C, recombinant mutant Y78A
Paracoccus denitrificans
7292
-
NADH
pH 7.4, 25C, recombinant mutant R95A
Paracoccus denitrificans
11727
-
NADH
pH 7.4, 25C, recombinant wild-type enzyme
Paracoccus denitrificans
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.24
-
NADH
pH 7.4, 25C, recombinant mutant R80L
Paracoccus denitrificans
0.29
-
NADH
pH 7.4, 25C, recombinant mutant E77L
Paracoccus denitrificans
0.39
-
NADH
pH 7.4, 25C, recombinant mutant R80M
Paracoccus denitrificans
2.7
-
NADH
pH 7.4, 25C, recombinant mutant G115I
Paracoccus denitrificans
5.4
-
NADH
pH 7.4, 25C, recombinant mutant G115F
Paracoccus denitrificans
6
-
NADH
pH 7.4, 25C, recombinant mutant E77M
Paracoccus denitrificans
9.2
-
NADH
pH 7.4, 25C, recombinant mutant R80E
Paracoccus denitrificans
25
-
NADH
pH 7.4, 25C, recombinant mutant E77K
Paracoccus denitrificans
99
-
NADH
pH 7.4, 25C, recombinant mutant E77A
Paracoccus denitrificans
302
-
NADH
pH 7.4, 25C, recombinant mutant R95E
Paracoccus denitrificans
316
-
NADH
pH 7.4, 25C, recombinant mutant G118I
Paracoccus denitrificans
906
-
NADH
pH 7.4, 25C, recombinant mutant G118F
Paracoccus denitrificans
1278
-
NADH
pH 7.4, 25C, recombinant mutant S113A
Paracoccus denitrificans
2767
-
NADH
pH 7.4, 25C, recombinant mutant R80K
Paracoccus denitrificans
4900
-
NADH
pH 7.4, 25C, recombinant mutant Y78A
Paracoccus denitrificans
7292
-
NADH
pH 7.4, 25C, recombinant mutant R95A
Paracoccus denitrificans
11727
-
NADH
pH 7.4, 25C, recombinant wild-type enzyme
Paracoccus denitrificans
Other publictions for EC 1.6.5.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
744242
Shrestha
Leflunomide induces NAD(P)H q ...
Mus musculus
Biochem. Biophys. Res. Commun.
485
195-200
2017
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1
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-
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-
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1
-
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1
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744765
Zhang
Overexpression of NAD(P)H qui ...
Homo sapiens
DNA Cell Biol.
36
256-263
2017
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1
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-
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-
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-
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2
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1
1
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744842
Bian
Affinity-based small fluoresc ...
Homo sapiens
Eur. J. Med. Chem.
127
828-839
2017
-
1
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1
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744882
Lienhart
Catalytic competence, structu ...
Homo sapiens
FEBS J.
284
1233-1245
2017
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-
1
1
1
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4
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2
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2
4
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1
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1
1
1
1
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-
4
-
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-
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-
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2
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2
4
-
-
-
-
-
-
-
-
4
4
744951
Roubalova
Flavonolignan 2,3-dehydrosily ...
Mus musculus
Fitoterapia
119
115-120
2017
-
-
-
-
-
-
-
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-
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-
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5
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1
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1
-
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-
-
-
-
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-
1
-
-
1
-
-
745826
Bang
Docosahexaenoic acid induces ...
Homo sapiens
Molecules
22
E969
2017
-
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3
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2
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-
-
-
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-
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-
1
-
-
1
-
-
746160
Biniek
Role of the NAD(P)H quinone o ...
Arabidopsis thaliana
Planta
245
807-817
2017
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
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-
-
1
1
-
-
-
746536
Zhang
Human glutathione S-transfera ...
Homo sapiens
Toxicol. Lett.
275
83-91
2017
-
1
1
-
-
-
-
-
-
-
-
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3
-
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-
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-
2
1
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5
-
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-
1
1
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-
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2
1
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5
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-
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-
-
-
-
-
-
742353
Rougee
The ontogeny and population v ...
Homo sapiens
Drug Metab. Dispos.
44
967-974
2016
-
1
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-
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1
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4
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2
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1
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2
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3
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1
1
-
-
-
743497
Saroussi
The type II NADPH dehydrogena ...
Chlamydomonas reinhardtii
Plant Physiol.
170
1975-1988
2016
-
-
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1
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1
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1
1
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744232
Maeda
NAD(P)H quinone oxidoreductas ...
Mus musculus
Biochem. Biophys. Res. Commun.
473
1276-1280
2016
-
-
-
-
-
-
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2
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1
1
-
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-
745193
Atia
-
Tocotrienol-rich palm oil ext ...
Mus musculus
J. Appl. Pharm. Sci.
6
127-134
2016
-
-
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1
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1
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1
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1
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1
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745530
Jackson
Phytonutrients differentially ...
Mus musculus
J. Med. Food
19
47-53
2016
-
-
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-
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1
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1
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1
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1
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1
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745663
Glorieux
Overexpression of NAD(P)Hquin ...
Homo sapiens
Life Sci.
145
57-65
2016
-
1
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-
-
-
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3
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2
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1
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2
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745830
Gayam
An NAD(P)Hquinone oxidoreduct ...
Homo sapiens
Nanoscale
8
12307-12317
2016
-
-
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1
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1
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2
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-
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-
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746007
Okubo
NAD(P)H dehydrogenase, quinon ...
Homo sapiens, Mus musculus
Pigment cell Melanoma Res.
29
309-316
2016
-
-
-
-
-
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2
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4
-
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2
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2
2
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746204
Kasai
NAD(P)H quinone oxidoreductas ...
Homo sapiens
PLoS ONE
11
e0153181
2016
-
1
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-
-
-
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-
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2
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2
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1
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2
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-
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746535
Gray
NAD(P)H-dependent quinone oxi ...
Rattus norvegicus
Toxicol. Lett.
262
1-11
2016
-
-
-
-
-
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1
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2
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1
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1
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2
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2
1
1
2
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-
742382
Ramos
The FlxABCD-HdrABC proteins c ...
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2
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2
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2
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4
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1
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2
1
1
1
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2
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2
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4
-
-
-
-
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-
-
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-
-
-
-
688795
Wolfova
-
Crystallographic study of Esch ...
Escherichia coli
Mater. Struct. Chem. Biol. Phys. Technol.
15
55-57
2008
-
1
1
1
-
-
-
-
-
-
1
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1
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1
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1
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1
1
1
1
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1
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
688840
Hong
The NADPH quinone reductase Md ...
Helicobacter hepaticus, Helicobacter hepaticus ATCC 51449
Microb. Pathog.
44
169-174
2008
-
-
1
-
1
-
-
-
-
-
-
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4
-
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-
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2
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12
1
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2
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1
2
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1
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2
-
12
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
689130
Fagerholm
NAD(P)H:quinone oxidoreductase ...
Homo sapiens
Nat. Genet.
40
844-853
2008
-
1
-
-
1
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2
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4
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1
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1
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4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
689279
Tijhuis
The influence of fruit and veg ...
Homo sapiens
Nutr. Cancer
60
204-215
2008
1
1
-
-
-
-
1
-
-
-
-
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3
-
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3
4
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1
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1
2
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1
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5
4
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
689700
Ahn
Induction of NAD(P)H:Quinone R ...
Mus musculus
Planta Med.
74
1387-1390
2008
1
-
-
-
-
-
-
-
-
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3
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7
-
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1
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7
-
-
-
-
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-
-
-
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-
-
-
-
-
-
691553
Jia
Potent induction of total cell ...
Homo sapiens
Brain Res.
1197
159-169
2008
1
1
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2
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2
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1
1
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2
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
691669
Isbir
The effect of NQO1 polymorphis ...
Homo sapiens
Cell Biochem. Funct.
26
534-538
2008
-
1
-
-
1
-
-
-
-
-
-
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2
-
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1
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
691776
Diaz-Veliz
Copper neurotoxicity in rat su ...
Rattus norvegicus
Chem. Res. Toxicol.
21
1180-1185
2008
-
1
-
-
-
-
1
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3
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3
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1
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1
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3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
692674
Song
Anti-cancer effect of bio-redu ...
Homo sapiens, Mus musculus, Mus musculus C3H
Int. J. Hyperthermia
24
161-169
2008
2
2
-
-
-
-
-
-
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5
-
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3
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2
2
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3
-
-
-
-
-
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-
-
-
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-
-
-
-
-
-
-
-
692722
Chen
In vitro activity of almond sk ...
Mus musculus
J. Agric. Food Chem.
56
4427-4434
2008
4
1
-
-
-
-
2
-
-
-
-
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-
2
-
-
-
-
-
2
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-
1
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4
1
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2
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-
-
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-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
692844
Belchik
Functions of flavin reductase ...
Cupriavidus pinatubonensis JMP134
J. Bacteriol.
190
1615-1619
2008
-
1
1
-
-
-
-
3
-
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1
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3
-
-
1
-
-
-
5
1
7
1
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-
-
1
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-
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3
-
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-
1
1
3
-
-
-
-
-
-
3
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1
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1
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-
5
1
7
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
692928
Augustine
Gender divergent expression of ...
Rattus norvegicus
J. Biochem. Mol. Toxicol.
22
93-100
2008
2
1
-
-
-
-
-
-
1
-
1
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-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
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2
1
-
-
-
-
-
-
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1
-
1
-
-
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-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
693895
Kim
Association of the NQO1, MPO, ...
Homo sapiens
J. Toxicol. Environ. Health A
71
333-341
2008
-
1
-
-
-
-
-
-
-
-
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1
-
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1
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-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
693945
Begleiter
Investigation of an NQO1 polym ...
Homo sapiens
Leuk. Res.
33
74-81
2008
-
1
-
-
-
-
2
-
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-
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2
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-
1
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-
1
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2
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1
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
694497
Sripathy
hPMC2 is required for recruiti ...
Homo sapiens
Oncogene
27
6376-6384
2008
-
1
-
-
-
-
-
-
-
-
-
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1
-
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2
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1
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1
-
1
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2
-
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-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
694519
Colucci
Natural and synthetic quinones ...
Homo sapiens, Mus musculus, Rattus norvegicus
Org. Biomol. Chem.
6
637-656
2008
5
1
1
3
-
-
3
-
-
-
1
-
-
4
-
-
2
-
-
4
-
-
18
1
-
-
-
-
-
-
-
5
-
-
-
5
1
1
5
3
-
-
-
3
-
-
-
-
1
-
-
-
-
2
-
4
-
-
18
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
694562
Munday
Structure-activity relationshi ...
Rattus norvegicus
Pharm. Res.
25
2164-2170
2008
2
1
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
6
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
694566
Lim
Bromocriptine activates NQO1 v ...
Rattus norvegicus
Pharmacol. Res.
57
325-331
2008
1
1
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
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-
1
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-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
695203
Stiborova
The environmental pollutant an ...
Rattus norvegicus
Toxicology
247
11-22
2008
1
1
-
-
-
-
1
-
1
-
-
-
-
4
-
-
-
-
-
4
5
-
1
-
-
-
-
-
-
-
-
1
-
-
-
1
1
-
1
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
4
5
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
695265
Bianchet
Structure, function, and mecha ...
Homo sapiens, Mesocricetus auratus, Mus musculus, Rattus norvegicus
Vitam. Horm.
78
63-84
2008
3
4
-
2
1
-
4
-
4
-
-
-
-
4
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
9
-
-
-
3
4
-
9
2
1
-
-
4
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
697473
Bafana
Lateral gene transfer in phylo ...
Cavia porcellus, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae
Comput. Biol. Chem.
32
191-197
2008
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
12
-
-
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
715903
Kim
Crystal structure of a new typ ...
Escherichia coli
J. Mol. Biol.
379
372-384
2008
-
-
-
1
8
-
-
7
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
1
8
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
7
-
-
-
-
-
-
-
-
7
7
672892
Elbekai
Ascorbic acid differentially m ...
Mus musculus
Cancer Lett.
246
54-62
2007
1
1
-
-
-
-
1
-
-
2
-
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-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
-
-
2
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
673704
Han
Eugenol inhibit 7,12-dimethylb ...
Homo sapiens
FEBS Lett.
581
749-756
2007
1
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
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-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
677217
Moffit
Role of NAD(P)H:quinone oxidor ...
Homo sapiens, Mus musculus, Mus musculus CD-1
Toxicology
230
197-206
2007
2
2
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684502
Joung
Capsaicin induces heme oxygena ...
Homo sapiens
Antioxid. Redox Signal.
9
2087-2098
2007
-
-
-
-
-
-
3
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
688259
Colucci
Synthesis and evaluation of 3- ...
Homo sapiens
J. Med. Chem.
50
5780-5789
2007
-
1
1
-
-
-
26
-
-
-
-
-
-
2
-
-
1
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
23
-
1
1
-
-
-
-
23
26
-
-
-
-
-
-
-
-
-
1
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
690145
Casalino
The Nrf2 transcription factor ...
Rattus norvegicus
Toxicology
237
24-34
2007
-
1
-
-
-
-
-
-
1
2
-
-
-
3
-
-
-
-
-
2
8
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
2
-
-
-
-
-
-
-
2
8
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
690894
Reigan
Development of indolequinone m ...
Homo sapiens
Biochemistry
46
5941-5950
2007
-
-
1
-
-
-
6
-
-
-
-
-
-
2
-
-
1
-
-
2
1
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
6
-
-
-
-
-
-
-
-
-
1
-
2
1
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
691592
Korashy
Induction of the NAD(P)H:quino ...
Mus musculus
Cancer Lett.
258
135-143
2007
5
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
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1
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1
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5
1
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1
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-
1
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691774
Fuentes
Inhibition of VMAT-2 and DT-di ...
Rattus norvegicus
Chem. Res. Toxicol.
20
776-783
2007
-
1
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2
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3
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1
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1
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692171
Zhang
Quinone reductase induction ac ...
Mus musculus
Eur. J. Med. Chem.
42
841-850
2007
7
1
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7
1
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1
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693536
Nolan
Coumarin-based inhibitors of h ...
Homo sapiens
J. Med. Chem.
50
6316-6325
2007
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1
1
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26
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2
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1
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2
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1
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1
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52
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1
1
1
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-
52
26
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1
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2
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1
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694350
Choi
Upregulation of NAD(P)H:quinon ...
Homo sapiens
Neoplasia
9
634-642
2007
1
1
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2
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3
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1
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1
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2
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1
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-
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694511
Newsome
Benzimidazole- and benzothiazo ...
Homo sapiens
Org. Biomol. Chem.
5
3665-3673
2007
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1
1
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2
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8
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1
1
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8
-
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694708
Wang
A novel nucleus-encoded chloro ...
Arabidopsis thaliana
Plant Physiol.
144
1742-1752
2007
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1
1
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1
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3
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4
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1
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1
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-
695000
Carey
WrbA bridges bacterial flavodo ...
Escherichia coli
Protein Sci.
16
2301-2305
2007
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1
-
1
-
-
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-
-
-
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1
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1
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3
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1
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3
1
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-
1
-
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-
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-
-
-
-
-
-
-
-
695280
Nivinskas
Prooxidant cytotoxicity of chr ...
Ovis aries, Rattus norvegicus
Z. Naturforsch. C
61
889-895
2007
1
1
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2
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4
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2
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2
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1
1
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2
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-
3
-
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-
2
-
-
-
-
-
-
-
-
-
-
671034
Miseviciene
Reduction of nitroaromatic com ...
Rattus norvegicus
Acta Biochim. Pol.
53
569-576
2006
-
-
-
-
-
-
10
-
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1
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1
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10
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9
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10
9
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1
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-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
671220
Merker
Influence of pulmonary arteria ...
Bos taurus
Am. J. Physiol.
290
L607-619
2006
-
-
-
-
-
-
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4
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2
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1
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2
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1
-
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-
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-
-
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-
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-
672174
Asher
The crystal structure of NAD(P ...
Homo sapiens
Biochemistry
45
6372-6378
2006
-
-
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1
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-
1
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3
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1
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-
-
-
-
-
-
-
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672967
Lyn-Cook
Increased levels of NAD(P)H: q ...
Homo sapiens
Cell Biol. Toxicol.
22
73-80
2006
-
1
-
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-
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2
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2
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1
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2
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-
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-
-
-
-
-
-
-
-
673294
Korashy
Transcriptional regulation of ...
Mus musculus
Drug Metab. Dispos.
34
152-165
2006
-
-
-
-
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-
1
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2
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1
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1
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1
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-
-
-
-
-
-
-
-
673798
van Horssen
NAD(P)H:quinone oxidoreductase ...
Homo sapiens
Free Radic. Biol. Med.
41
311-317
2006
-
1
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1
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2
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2
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1
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1
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2
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-
1
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-
-
-
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-
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-
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674276
Patridge
WrbA from Escherichia coli and ...
Archaeoglobus fulgidus, Escherichia coli
J. Bacteriol.
188
3498-3506
2006
-
-
-
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1
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6
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5
2
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7
-
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-
-
-
-
11
-
14
3
-
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6
-
2
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4
-
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4
-
1
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6
-
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5
2
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-
11
-
14
3
-
-
-
6
-
2
-
-
-
-
-
-
-
-
676097
Guo
The bioreduction of a series o ...
Homo sapiens
Mol. Pharmacol.
70
1194-1203
2006
-
-
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-
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1
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3
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5
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1
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5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
676114
van der Logt
Role of epoxide hydrolase, NAD ...
Homo sapiens
Mutat. Res.
593
39-49
2006
-
1
-
-
-
-
-
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2
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1
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-
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-
-
-
-
-
-
-
-
-
-
-
-
677204
Covarrubias
Higher activity of polymorphic ...
Homo sapiens
Toxicol. Lett.
164
249-258
2006
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1
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-
-
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2
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3
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3
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1
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2
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3
-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
677256
Aleksunes
Up-regulation of NAD(P)H quino ...
Homo sapiens
World J. Gastroenterol.
12
1937-1940
2006
-
1
-
-
-
-
-
-
-
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2
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3
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1
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-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
657888
Vella
NRH:quinone reductase 2: an en ...
Homo sapiens
Biochem. Pharmacol.
71
1-12
2005
-
-
-
-
-
-
-
-
-
-
-
1
-
1
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2
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1
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1
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1
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1
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2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
671033
Nemeikaite-Ceniene
Role of NAD(P)H:quinone oxidor ...
Ovis aries
Acta Biochim. Pol.
52
937-941
2005
-
1
-
-
-
-
-
-
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1
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1
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2
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1
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-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
672897
Guo
Formation of 17-allylamino-dem ...
Homo sapiens
Cancer Res.
65
10006-10015
2005
-
-
-
-
-
-
1
-
-
-
-
-
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3
-
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-
-
1
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1
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1
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1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
673789
Lee
Human NAD(P)H:quinone oxidored ...
Homo sapiens
Free Radic. Biol. Med.
39
257-265
2005
-
1
-
-
-
-
6
-
-
-
-
-
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3
-
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-
-
-
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-
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6
-
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1
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6
6
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
674023
Foppoli
Biological response of human d ...
Homo sapiens
Int. J. Biochem. Cell Biol.
37
852-863
2005
2
-
-
-
-
-
-
-
-
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1
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2
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2
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1
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2
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-
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1
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-
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2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
675291
AbuKhader
Binding of the anticancer prod ...
Homo sapiens
J. Med. Chem.
48
7714-7719
2005
-
-
-
1
-
-
-
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1
-
-
-
-
-
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1
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1
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-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
676693
Greenshields
Differential regulation of whe ...
Triticum monococcum
Planta
222
867-875
2005
-
-
1
-
-
-
1
1
-
-
-
1
-
7
-
-
-
-
-
1
-
-
3
-
1
-
-
-
1
-
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2
-
-
-
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1
2
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-
1
-
1
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1
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1
-
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
676790
Tsvetkov
Inhibition of NAD(P)H:quinone ...
Mus musculus
Proc. Natl. Acad. Sci. USA
102
5535-5540
2005
-
-
-
-
-
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1
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3
-
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
680629
Gonzalez
ChrR, a soluble quinone reduct ...
Pseudomonas putida, Pseudomonas putida KT 2240
J. Biol. Chem.
280
22590-22595
2005
1
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1
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1
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1
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2
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44
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-
1
-
1
1
-
12
-
1
-
-
5
2
-
-
2
-
-
-
1
-
1
2
-
1
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-
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6
1
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2
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-
-
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1
1
-
12
-
1
-
-
5
2
-
-
-
-
-
-
-
-
-
660005
SantaCruz
Regional NAD(P)H:quinone oxido ...
Homo sapiens
Neurobiol. Aging
25
63-69
2004
-
-
-
-
-
-
-
-
-
-
-
1
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2
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-
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3
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1
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1
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3
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
655164
Bauer
Genetic susceptibility to benz ...
Mus musculus
Cancer Res.
63
929-935
2003
-
-
-
-
-
-
-
-
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1
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3
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1
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DT-diaphorase [NAD(P)H: (quino ...
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Stiborova
Human cytosolic enzymes involv ...
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Kinetics of NAD(P)H:quinone ox ...
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Regeneration of lipophilic ant ...
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2003
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Two-electron reduction of quin ...
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Purification and characterizat ...
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Matsushita
NADH dehydrogenase of Coryneba ...
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Characterization of a mechanis ...
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Deng
Photodependent inhibition of r ...
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