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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
dihydrolipoamide dehydrogenase, ferric leghemoglobin reductase, ferric leghemoglobin reductase 2, FLbR-2, FLbR2,
more
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dihydrolipoamide dehydrogenase
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ferric leghemoglobin reductase
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ferric leghemoglobin reductase 2
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NAD(P)H + H+ + 2 ferrileghemoglobin = NAD(P)+ + 2 ferroleghemoglobin
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NAD(P)H:ferrileghemoglobin oxidoreductase
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2 ferricytochrome c + NAD(P)H
2 ferrocytochrome c + NAD(P)+ + H+
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reduced at 53% of leghemoglobin rate
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?
2,6-dichloroindophenol + NADH
reduced 2,6-dichloroindophenol + NAD+
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
NAD(P)H + ferrimyoglobin
NAD(P)+ + ferromyoglobin
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-
-
?
NADH + ferrileghemoglobin
NAD+ + ferroleghemoglobin
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-
-
?
NADH + H+ + ferrileghemoglobin
NAD+ + ferroleghemoglobin
NADH + H+ + oxidized ferric rice non-symbiotic Hb1
NAD+ + + reduced ferric rice non-symbiotic Hb1
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-
-
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?
NADH + lipoamide
NAD+ + ?
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-
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?
NADH + lipoamide
NAD+ + lipoamide
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recombinant enzyme, lipoamide-dependent NADH oxidation
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?
NADPH + H+ + ferrileghemoglobin
NADP+ + ferroleghemoglobin
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?
additional information
?
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reactive nitrogen species are able to react with two inactive forms (in terms of oxygen binding) of leghemoglobin: ferryl-leghemoglobin and nitrosyl-leghemoglobin. In both cases, the product of the reactions is metleghemoglobin. As metleghemoglobin can be reduced by a reductase found in the nodules, reactive nitrogen species could contribute to the recycling of these inactive forms to regenerate deoxyLb, the oxygen-binding form of Lb
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?
2,6-dichloroindophenol + NADH
reduced 2,6-dichloroindophenol + NAD+
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no activity in the absence of
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?
2,6-dichloroindophenol + NADH
reduced 2,6-dichloroindophenol + NAD+
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-
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?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
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proposed to be involved in maintaining leghemoglobin in an active form in legume nodules
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?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
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31% activity with NADPH
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?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
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no activity in the absence of O2, formation of H2O2 or peroxide intermediates during NADH oxidation
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?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
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-
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?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
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-
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?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
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-
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?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
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-
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?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
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-
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?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
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reduces both cowpea ferrihemoglobin and soybean ferrileghemoglobin
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?
NADH + H+ + ferrileghemoglobin
NAD+ + ferroleghemoglobin
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-
-
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?
NADH + H+ + ferrileghemoglobin
NAD+ + ferroleghemoglobin
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r
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NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
NADH + H+ + ferrileghemoglobin
NAD+ + ferroleghemoglobin
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?
NADPH + H+ + ferrileghemoglobin
NADP+ + ferroleghemoglobin
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?
additional information
?
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reactive nitrogen species are able to react with two inactive forms (in terms of oxygen binding) of leghemoglobin: ferryl-leghemoglobin and nitrosyl-leghemoglobin. In both cases, the product of the reactions is metleghemoglobin. As metleghemoglobin can be reduced by a reductase found in the nodules, reactive nitrogen species could contribute to the recycling of these inactive forms to regenerate deoxyLb, the oxygen-binding form of Lb
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-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
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-
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?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
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-
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?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
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-
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
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-
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?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
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proposed to be involved in maintaining leghemoglobin in an active form in legume nodules
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?
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FAD
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FAD
not covalently bound to the protein
NADH
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NADPH
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NADPH
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54-80% of NADH activity
NADPH
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54-80% of NADH activity
NADPH
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54-80% of NADH activity
NADPH
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31% of NADH activity
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5,5'-dithiobis(2-nitrobenzoic acid)
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Amobarbital
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1 mM, 35% after 0.5-1 h, 80% after 4 h
catalase
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possibly H2O2 as reaction intermediate
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p-chloromercuribenzoate
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p-hydroxymercuribenzoate
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0.5 mM, slight inhibition
Quinacrine
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0.5 mM, 30-40% inhibition
iodoacetamide
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iodoacetamide
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1 mM, 95-100% inhibition
nicotinate
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nicotinate
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ferrileghemoglobin-nitrite complex
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0.0063 - 0.088
ferrileghemoglobin
0.0092
ferrileghemoglobin
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native enzyme
0.088
ferrileghemoglobin
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0.029
ferrileghemoglobin
recombinant FLbR-2
0.0133
ferrileghemoglobin
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0.0133
ferrileghemoglobin
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0.0124
ferrileghemoglobin
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soybean ferrileghemoglobin
0.0104
ferrileghemoglobin
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cowpea ferrileghemoglobin
0.0095
ferrileghemoglobin
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0.0063
ferrileghemoglobin
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recombinant enzyme
0.716
Lipoamide
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lipoamide-dependent NADH oxidation
3.381
Lipoamide
recombinant FLbR-2
0.0188
NADH
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0.046
NADH
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lipoamide-dependent NADH oxidation
0.058
NADH
recombinant FLbR-2
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1.6 - 6.2
ferrileghemoglobin
137
NADH
recombinant FLbR-2
1.6
ferrileghemoglobin
recombinant FLbR-2
2.5
ferrileghemoglobin
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soybean ferrileghemoglobin
3.1
ferrileghemoglobin
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cowpea ferrileghemoglobin
6.2
ferrileghemoglobin
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recombinant enzyme
6.2
ferrileghemoglobin
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native enzyme
31
Lipoamide
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recombinant enzyme
392
Lipoamide
recombinant FLbR-2
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0.215
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reduction of ferrileghemoglobin
0.216
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reduction of ferrileghemoglobin
0.218
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reduction of ferrileghemoglobin
0.388
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reduction of ferrileghemoglobin in the presence of O2
0.486
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recombinant enzyme, reduction of ferrileghemoglobin
0.5
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reduction of ferrileghemoglobin
1.85
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oxidation of NADH in the presence of O2, 30fold higher than in the absence of O2
2
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reduction of 2,6-dichlorophenolindophenol
2.565
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reduction of 2,6-dichloroindophenol
4.47
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recombinant enzyme, reduction of 2,6-dichloroindophenol
4.5
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reduction of 2,6-dichloroindophenol in the presence of O2
4.89
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reduction of 2,6-dichlorophenolindophenol
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5.2
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decrease of activity from 100% at pH 5.2, to 30% at pH 6.7, no measurements below 5.2
6.5
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reduction of ferrileghemoglobin
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4.8 - 8.5
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no activity below and above
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5.8
isoelectric focusing, pH-range 4.0-6.5
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bean
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brenda
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SwissProt
brenda
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brenda
soybean
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brenda
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brenda
cowpea
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brenda
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high mRNA level
brenda
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brenda
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brenda
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high mRNA level
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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low mRNA level
brenda
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brenda
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brenda
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LEGRE_SOYBN
523
0
55804
Swiss-Prot
Mitochondrion (Reliability: 1 )
LEGRE_VIGUN
523
0
55780
Swiss-Prot
Mitochondrion (Reliability: 3 )
A0A072V2R0_MEDTR
502
0
53243
TrEMBL
Mitochondrion (Reliability: 2 )
O81413_SOYBN
500
0
53002
TrEMBL
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50030
electrospray mass spectrometry
54000
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2 * 54000, SDS-PAGE
56000
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2 * 56000, deduced from amino acid sequence
83000
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equilibrium ultracentrifugation
110000
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gel filtration
55000
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2 * 55000, SDS-PAGE
55000
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2 * 55000, SDS-PAGE
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dimer
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2 * 55000, SDS-PAGE
dimer
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2 * 54000, SDS-PAGE
dimer
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2 * 55000, SDS-PAGE
dimer
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2 * 56000, deduced from amino acid sequence
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additional information
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heat labile
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0°C, 37 days, 96% activity retains
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ammonium sulfate, hydroxylapatite, ion exchange, gel filtration
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His Trap HP Ni-chelating resin column chromatography
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recombinant enzyme, Sepharose 6B, Probond
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expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
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overexpression in Escherichia coli BL21
production of a recombinant FLbR-2 from Escherichia coli BL21(DE3) by using an overexpression method based on the self-induction of the recombinant Escherichia coli
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cloning of cDNA
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Moran, J.F.; Sun, Z.; Sarath, G.; Arredondo-Peter, R.; James, E.K.; Becana, M.; Klucas, R.V.
Molecular cloning, functional characterization, and subcellular localization of soybean nodule dihydrolipoamide reductase
Plant Physiol.
128
300-313
2002
Glycine max (O81413), Glycine max
brenda
Saari, L.L.; Klucas, R.V.
Ferric leghemoglobin reductase from soybean root nodules
Arch. Biochem. Biophys.
231
102-113
1984
Glycine max
brenda
Becana, M.; Klucas, R.V.
Enzymatic and nonenzymatic mechanisms for ferric leghemoglobin reduction in legume root nodules
Proc. Natl. Acad. Sci. USA
87
7295-7299
1990
Glycine max, Phaseolus vulgaris, Vigna unguiculata
brenda
Ji, L.; Wood, S.; Becana, M.; Klucas, R.V.
Purification and characterization of soybean root nodule ferric leghemoglobin reductase
Plant Physiol.
96
32-37
1991
Glycine max
brenda
Ji, L.; Becana, M.; Klucas, R.V.
Involvement of molecular oxygen in the enzyme-catalyzed NADH oxidation and ferric leghemoglobin reduction
Plant Physiol.
100
33-39
1992
Glycine max
brenda
Ji, L.; Becana, M.; Sarath, G.; Klucas, R.V.
Cloning and sequence analysis of a cDNA encoding ferric leghemoglobin reductase from soybean nodules
Plant Physiol.
104
453-459
1994
Glycine max
brenda
Ji, L.; Becana, M.; Sarath, G.; Shearman, L.; Klucas, R.V.
Overproduction in Escherichia coli and characterization of a soybean ferric leghemoglobin reductase
Plant Physiol.
106
203-209
1994
Glycine max
brenda
Kim, H.M.
Redox potential of a soybean ferric leghemoglobin reductase
J. Biochem. Mol. Biol.
31
444-452
1998
Glycine max
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brenda
Luan, P.; Arechaga-Ocampo, E.; Sarath, G.; Arredondo-Peter, R.; Klucas, R.V.
Analysis of a ferric leghemoglobin reductase from cowpea (Vigna unguiculata) root nodules
Plant Sci.
154
161-170
2000
Vigna unguiculata
brenda
Herold, S.; Puppo, A.
Kinetics and mechanistic studies of the reactions of metleghemoglobin, ferrylleghemoglobin, and nitrosylleghemoglobin with reactive nitrogen species
J. Biol. Inorg. Chem.
10
946-957
2005
Glycine max
brenda
Urarte, E.; Auzmendi, I.; Rol, S.; Ariz, I.; Aparicio-Tejo, P.; Arredondo-Peter, R.; Moran, J.F.
A self-induction method to produce high quantities of recombinant functional flavo-leghemoglobin reductase
Methods Enzymol.
436
411-423
2008
Glycine max
brenda
Gopalasubramaniam, S.K.; Kondapalli, K.C.; Millan-Pacheco, C.; Pastor, N.; Stemmler, T.L.; Moran, J.F.; Arredondo-Peter, R.
Soybean dihydrolipoamide dehydrogenase (ferric leghemoglobin reductase 2) interacts with and reduces ferric rice non-symbiotic hemoglobin 1
Sciencejet
2
33
2013
Glycine max
brenda
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