Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 Fe(II) + NADP+ + H+
2 Fe(III) + NADPH
-
Substrates: -
Products: -
?
2 Fe(II)-cytochrome c + NADP+ + H+
2 Fe(III)-cytochrome c + NADPH
-
Substrates: -
Products: -
?
2 Fe(II)-siderophore + NADP+ + H+
2 Fe(III)-siderophore + NADPH
2 Fe(III)-(1,10-phenanthroline)3 + NADPH
2 Fe(II)-(1,10-phenanthroline)3 + NADP+ + H+
-
Substrates: -
Products: -
?
2 Fe(III)-(catechol)2 + NADPH
2 Fe(II)-(catechol)2 + NADP+ + H+
-
Substrates: -
Products: -
?
2 Fe(III)-(citrate)2 + NADPH
2 Fe(II)-(citrate)2 + NADP+ + H+
-
Substrates: -
Products: -
?
2 Fe(III)-(L-DOPA)2 + NADPH
2 Fe(II)-(L-DOPA)2 + NADP+ + H+
-
Substrates: highest specific activity
Products: -
?
2 Fe(III)-citrate + NADPH
2 Fe(II)-citrate + NADP+ + H+
-
Substrates: -
Products: -
?
2 Fe(III)-cyclam + NADPH
2 Fe(II)-cyclam + NADP+ + H+
-
Substrates: lowest specific activity
Products: -
?
2 Fe(III)-dicitrate + NADPH
2 Fe(II)-dicitrate + NADP+ + H+
-
Substrates: -
Products: -
?
2 Fe(III)-diethylenetriaminepentaacetate + NADPH
2 Fe(II)-diethylenetriaminepentaacetate + NADP+ + H+
-
Substrates: -
Products: -
?
2 Fe(III)-EDTA + NADH
2 Fe(II)-EDTA + NAD+ + H+
-
Substrates: -
Products: ?
?
2 Fe(III)-EDTA + NADPH
2 Fe(II)-EDTA + NADP+ + H+
2 Fe(III)-nitrilotriacetic acid + NADPH
2 Fe(II)-nitrilotriacetic acid + NADP+ + H+
-
Substrates: -
Products: -
?
2 Fe(III)-siderophore + NADPH
2 Fe(II)-siderophore + NADP+ + H+
2 Fe(III)-tris(2-pyridylmethyl)amine + NADPH
2 Fe(II)-tris(2-pyridylmethyl)amine + NADP+ + H+
-
Substrates: -
Products: -
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
Substrates: -
Products: -
?
2 ferrocyanide + NADP+ + H+
2 ferricyanide + NADPH
-
Substrates: -
Products: -
?
2,6-dichloroindophenol + NADPH + H+
?
-
Substrates: best substrate in the presence and absence of FAD
Products: -
?
an Fe(III)-siderophore + NADPH
Fe(II) + an apo-siderophore + NADP+ + H+
-
Substrates: -
Products: -
?
cytochrome c + NADPH + H+
?
-
Substrates: -
Products: -
?
Fe(II) + an apo-siderophore + NADP+ + H+
an Fe(III)-siderophore + NADPH
-
Substrates: -
Products: -
?
Fe(III)-(N-2,3-dihydroxybenzoyl-Gly-Thr)3 + NADPH + H+
Fe(II) + (2,3-dihydroxybenzoyl-Gly-Thr)3 + NADP+
-
Substrates: -
Products: -
?
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3 + NADPH + H+
Fe(II) + (2,3-dihydroxybenzoyl-L-serine)3 + NADP+
-
Substrates: -
Products: -
?
Fe(III)-aerobactin + NADPH + H+
Fe(II) + aerobactin + NADP+
-
Substrates: -
Products: -
?
Fe(III)-bacillibactin + NADPH + H+
Fe(II) + bacillibacitin + NADP+
-
Substrates: -
Products: -
?
Fe(III)-citrate + NADPH + H+
?
-
Substrates: -
Products: -
?
Fe(III)-deferoxamine + NADPH + H+
?
-
Substrates: -
Products: -
?
Fe(III)-dicitrate + NADPH + H+
Fe(II) + citrate + NADP+
-
Substrates: -
Products: -
?
Fe(III)-diethylenetriamine-N,N,N',N'',N''-pentaacetate + NADPH + H+
Fe(II) + diethylenetriamine-N,N,N',N'',N''-pentaacetate + NADP+ + H+
-
Substrates: -
Products: -
?
Fe(III)-EDTA + NADPH + H+
Fe(II) + EDTA + NADP+
Fe(III)-EDTA + NADPH + H+
Fe(II) + EDTA + NADP+ + H+
-
Substrates: -
Products: -
?
Fe(III)-enterobactin + NADPH + H+
Fe(II) + enterobactin + NADP+
-
Substrates: -
Products: -
?
Fe(III)-ferrichrome + NADPH + H+
?
-
Substrates: -
Products: -
?
Fe(III)-nitrilotriacetic acid + NADPH + H+
?
-
Substrates: -
Products: -
?
Fe(III)-o,o-EDDHA I + NADPH
Fe(II)-o,o-EDDHA I + NADP+ + H+
-
Substrates: i.e. ethylenediaminebis(o-hydroxyphenyl)acetic acid
Products: -
?
Fe(III)-vibriobactin + NADPH + H+
Fe(II) + vibriobactin + NADP+
-
Substrates: -
Products: -
?
Fe2+ + NADPH
Fe3+ + NADP+ + H+
-
Substrates: -
Products: -
?
ferric ammonium citrate + NADPH + H+
?
-
Substrates: -
Products: -
?
ferric enterobactin + NADPH + H+
?
ferritin + NADPH + H+
?
-
Substrates: -
Products: -
?
tert-butyl hydroperoxide + NADPH + H+
?
-
Substrates: -
Products: -
?
transferrin + NADPH + H+
?
-
Substrates: -
Products: -
?
additional information
?
-
2 Fe(II)-siderophore + NADP+ + H+

2 Fe(III)-siderophore + NADPH
-
Substrates: -
Products: -
r
2 Fe(II)-siderophore + NADP+ + H+
2 Fe(III)-siderophore + NADPH
-
Substrates: -
Products: -
?
2 Fe(II)-siderophore + NADP+ + H+
2 Fe(III)-siderophore + NADPH
-
Substrates: -
Products: -
?
2 Fe(III)-EDTA + NADPH

2 Fe(II)-EDTA + NADP+ + H+
-
Substrates: -
Products: -
?
2 Fe(III)-EDTA + NADPH
2 Fe(II)-EDTA + NADP+ + H+
-
Substrates: -
Products: -
?
2 Fe(III)-EDTA + NADPH
2 Fe(II)-EDTA + NADP+ + H+
-
Substrates: -
Products: ?
?
2 Fe(III)-siderophore + NADPH

2 Fe(II)-siderophore + NADP+ + H+
-
Substrates: -
Products: -
?
2 Fe(III)-siderophore + NADPH
2 Fe(II)-siderophore + NADP+ + H+
-
Substrates: -
Products: -
?
2 Fe(III)-siderophore + NADPH
2 Fe(II)-siderophore + NADP+ + H+
Substrates: -
Products: -
?
2 Fe(III)-siderophore + NADPH
2 Fe(II)-siderophore + NADP+ + H+
Substrates: -
Products: -
?
Fe(III)-EDTA + NADPH + H+

Fe(II) + EDTA + NADP+
-
Substrates: -
Products: -
?
Fe(III)-EDTA + NADPH + H+
Fe(II) + EDTA + NADP+
-
Substrates: -
Products: -
?
Fe(III)-EDTA + NADPH + H+
Fe(II) + EDTA + NADP+
-
Substrates: -
Products: -
?
ferric enterobactin + NADPH + H+

?
-
Substrates: weak activity
Products: -
?
ferric enterobactin + NADPH + H+
?
-
Substrates: weak activity
Products: -
?
additional information

?
-
-
Substrates: the enzyme is able to effectively reduce synthetic ferric chelates, which are octahedral Fe(III) complexes derived from polyaminocarboxylic acids, the process requires the generation of a coordination vacancy in the Fe(III)L6 complex I and the incorporation of a water molecule, photometric titration, overview
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows no ferric reductase activity toward ferric chloride
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows no ferric reductase activity toward ferric chloride
Products: -
?
additional information
?
-
-
Substrates: no activity with NADH. In the absence of FAD, the enzyme shows no activity towards ferric citrate, Fe(III)-ferrichrome, Fe(III)-deferoxamine, Fe(III)-nitrilotriacetic acid, and transferrin
Products: -
?
additional information
?
-
-
Substrates: DNA degradation occurring in the presence of NADPH, Fe(III)-EDTA and hydrogen peroxide is potently enhanced by the purified enzyme, indicating that the enzyme may drive the Fenton reaction, reducing ferric iron to ferrous iron when it evokes the Fenton reaction
Products: -
?
additional information
?
-
-
Substrates: the purified enzyme reacts with cytochrome c, ferricyanide and 2,6-dichloroindophenol, the flavin-independent NADPH oxidoreductase elicites NADPH oxidation activity during reduction of t-butyl hydroperoxide in the presence of Fe(III)-EDTA
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0042
Fe(III)-(N-2,3-dihydroxybenzoyl-Gly-Thr)3
-
wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.0018 - 0.04
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3
0.048
Fe(III)-aerobactin
-
wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.0276 - 0.16
Fe(III)-citrate
0.0134 - 0.066
Fe(III)-dicitrate
0.0168 - 0.5762
Fe(III)-EDTA
0.0004 - 0.0078
Fe(III)-enterobactin
0.0014
Fe(III)-vibriobactin
-
wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.043
NADPH
-
at pH 7.5 and 37°C
0.0018
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3

-
wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.036
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3
-
mutant enzyme R130A in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.04
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3
-
mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.0276
Fe(III)-citrate

-
in the presence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C
0.03022
Fe(III)-citrate
-
at suboptimal iron nutrition, pH and temperature not specified in the publication
0.04637
Fe(III)-citrate
-
at iron deficiency, pH and temperature not specified in the publication
0.047
Fe(III)-citrate
-
at optimal iron nutrition, pH and temperature not specified in the publication
0.16
Fe(III)-citrate
-
in the absence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C
0.0134
Fe(III)-dicitrate

-
wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.051
Fe(III)-dicitrate
-
mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.066
Fe(III)-dicitrate
-
mutant enzyme R130A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.0168
Fe(III)-EDTA

-
in the presence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C
0.02207
Fe(III)-EDTA
-
at optimal iron nutrition, pH and temperature not specified in the publication
0.02346
Fe(III)-EDTA
-
at iron deficiency, pH and temperature not specified in the publication
0.033
Fe(III)-EDTA
-
at pH 7.5 and 37°C
0.05252
Fe(III)-EDTA
-
at suboptimal iron nutrition, pH and temperature not specified in the publication
0.5762
Fe(III)-EDTA
-
in the absence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C
0.0004
Fe(III)-enterobactin

-
wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.0059
Fe(III)-enterobactin
-
mutant enzyme R130A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.0078
Fe(III)-enterobactin
-
mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
9.193
Fe(III)-(N-2,3-dihydroxybenzoyl-Gly-Thr)3
-
wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.091 - 23.35
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3
0.02
Fe(III)-aerobactin
-
wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
1.59 - 41
Fe(III)-citrate
0.139 - 5.427
Fe(III)-dicitrate
0.032 - 8.211
Fe(III)-enterobactin
1.268
Fe(III)-vibriobactin
-
wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.091
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3

-
mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.132
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3
-
mutant enzyme R130A in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
23.35
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3
-
wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
1.59
Fe(III)-citrate

-
in the absence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C
41
Fe(III)-citrate
-
in the presence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C
0.139
Fe(III)-dicitrate

-
mutant enzyme R130A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.271
Fe(III)-dicitrate
-
mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
5.427
Fe(III)-dicitrate
-
wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.12
Fe(III)-EDTA

-
in the absence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C
122
Fe(III)-EDTA
-
in the presence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C
0.032
Fe(III)-enterobactin

-
mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.076
Fe(III)-enterobactin
-
mutant enzyme R130A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
8.211
Fe(III)-enterobactin
-
wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Schagerloef, U.; Wilson, G.; Hebert, H.; Al-Karadaghi, S.; Haegerhaell, C.
Transmembrane topology of FRO2, a ferric chelate reductase from Arabidopsis thaliana
Plant Mol. Biol.
62
215-221
2006
Arabidopsis thaliana
brenda
Bamford, V.; Armour, M.; Mitchell, S.; Cartron, M.; Andrews, S.; Watson, K.
Preliminary X-ray diffraction analysis of YqjH from Escherichia coli: A putative cytoplasmic ferri-siderophore reductase
Acta Crystallogr. Sect. F
64
792-796
2008
Escherichia coli
brenda
Miethke, M.; Hou, J.; Marahiel, M.
The siderophore-interacting protein YqjH acts as a ferric reductase in different iron assimilation pathways of Escherichia coli
Biochemistry
50
10951-10964
2011
Escherichia coli
brenda
Sato, J.; Takeda, K.; Nishiyama, R.; Watanabe, T.; Abo, M.; Yoshimura, E.; Nakagawa, J.; Abe, A.; Kawasaki, S.; Niimura, Y.
Synechocystis ferredoxin-NADP+ oxidoreductase is capable of functioning as ferric reductase and of driving the Fenton reaction in the absence or presence of free flavin
Biometals
24
311-321
2011
Synechocystis sp.
brenda
Wang, S.; Wu, Y.; Outten, F.
Fur and the novel regulator Yqji control transcription of the ferric reductase gene yqjh in Escherichia coli
J. Bacteriol.
193
563-574
2011
Escherichia coli, Escherichia coli MG1655
brenda
Robinson, N.; Procter, C.; Connolly, E.; Guerinot, M.
A ferric-chelate reductase for iron uptake from soils
Nature
397
694-697
1999
Arabidopsis thaliana
brenda
Waters, B.; Blevins, D.; Eide, D.
Characterization of FRO1, a pea ferric-chelate reductase involved in root iron acquisition
Plant Physiol.
129
85-94
2002
Lathyrus oleraceus
brenda
Escudero, R.; Gomez-Gallego, M.; Romano, S.; Fernandez, I.; Gutierrez-Alonso, A.; Sierra, M.A.; Lopez-Rayo, S.; Nadal, P.; Lucena, J.J.
Biological activity of Fe(III) aquo-complexes towards ferric chelate reductase (FCR)
Org. Biomol. Chem.
10
2272-2281
2012
Cucumis sativus
brenda
Chandel, G.; Dubey, M.; Gupta, S.; Patil, A.H.; Rao, A.R.
Identification and characterization of a grain micronutrient-related OsFRO2 rice gene ortholog from micronutrient-rich little millet (Panicum sumatrense)
3 Biotech
7
80
2017
Oryza sativa, Panicum sumatrense (A0A1U9W5F0), Panicum sumatrense RLM-37 (A0A1U9W5F0)
brenda
Umezawa, S.; Konishi, S.; Kino, K.
Development of a synthesis method for odor sesquiterpenoid, (-)-rotundone, using non-heme Fe2+-chelate catalyst and ferric-chelate reductase
Biosci. Biotechnol. Biochem.
83
1875-1883
2019
Escherichia coli
brenda
Umezawa, S.; Akao, H.; Kubota, M.; Kino, K.
Chemoenzymatic oxygenation method for sesquiterpenoid synthesis based on Fe-chelate and ferric-chelate reductase
Biosci. Biotechnol. Biochem.
84
780-788
2020
Escherichia coli
brenda
Li, L.; Ye, L.; Kong, Q.; Shou, H.
A vacuolar membrane ferric-chelate reductase, OsFRO1, alleviates Fe toxicity in rice (Oryza sativa L.)
Front. Plant Sci.
10
700
2019
Oryza sativa Japonica Group
brenda
Sagi-Kazar, M.; Zelenyanszki, H.; Mueller, B.; Cseh, B.; Gyuris, B.; Farkas, S.Z.; Fodor, F.; Toth, B.; Kovacs, B.; Koncz, A.; Visnovitz, T.; Buzas, E.I.; Bankuti, B.; Banati, F.; Szenthe, K.; Solti, A.
Supraoptimal iron nutrition of Brassica napus plants suppresses the iron uptake of chloroplasts by down-regulating chloroplast ferric chelate reductase
Front. Plant Sci.
12
658987
2021
Brassica napus
brenda