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Information on EC 1.16.1.9 - ferric-chelate reductase (NADPH)
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1.16.1.9 ferric-chelate reductase (NADPH)IUBMB Comments
Contains FAD. The enzyme, which is widespread among bacteria, catalyses the reduction of ferric iron bound to a variety of iron chelators (siderophores), including ferric triscatecholates and ferric dicitrate, resulting in the release of ferrous iron. The enzyme from the bacterium Escherichia coli has the highest efficiency with the hydrolysed ferric enterobactin complex ferric N-(2,3-dihydroxybenzoyl)-L-serine . cf. EC 1.16.1.7, ferric-chelate reductase (NADH) and EC 1.16.1.10, ferric-chelate reductase [NAD(P)H].
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Word Map
- 1.16.1.9
-
ferredoxin-nadp+
- ferredoxins
- cyanobacterium
- thylakoids
-
photosystems
-
phycobilisome
-
fad-binding
- phycocyanin
-
1.18.1.2
-
nadph-thioredoxin
-
chloroplast-targeted
- isoalloxazine
- flavodoxin
-
ferredoxin-dependent
-
leaf-type
-
re-face
- tic62
- thermosynechococcus
The enzyme appears in viruses and cellular organisms
Reaction Schemes
2
Fe(II)-siderophore
+
+
=
2
Fe(III)-siderophore
+
Synonyms
ferredoxin-nadp(+) oxidoreductase, fnr(s), fcr-lm, fcr-os, ferric siderophore reductase, ferri-siderophore reductase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FCR-LM
ferric chelate reductase
ferric reductase
ferric-chelate reductase
FRO2
YqjH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 Fe(II)-siderophore + NADP+ + H+ = 2 Fe(III)-siderophore + NADPH
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
Fe(II)-siderophore:NADP+ oxidoreductase
Contains FAD. The enzyme, which is widespread among bacteria, catalyses the reduction of ferric iron bound to a variety of iron chelators (siderophores), including ferric triscatecholates and ferric dicitrate, resulting in the release of ferrous iron. The enzyme from the bacterium Escherichia coli has the highest efficiency with the hydrolysed ferric enterobactin complex ferric N-(2,3-dihydroxybenzoyl)-L-serine [3]. cf. EC 1.16.1.7, ferric-chelate reductase (NADH) and EC 1.16.1.10, ferric-chelate reductase [NAD(P)H].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 Fe(II)-cytochrome c + NADP+ + H+
2 Fe(III)-cytochrome c + NADPH
-
-
-
-
?
2,6-dichloroindophenol + NADPH + H+
?
-
best substrate in the presence and absence of FAD
-
-
?
an Fe(III)-siderophore + NADPH
Fe(II) + an apo-siderophore + NADP+ + H+
-
-
-
-
?
Fe(II) + an apo-siderophore + NADP+ + H+
an Fe(III)-siderophore + NADPH
-
-
-
-
?
Fe(III)-(N-2,3-dihydroxybenzoyl-Gly-Thr)3 + NADPH + H+
Fe(II) + (2,3-dihydroxybenzoyl-Gly-Thr)3 + NADP+
-
-
-
-
?
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3 + NADPH + H+
Fe(II) + (2,3-dihydroxybenzoyl-L-serine)3 + NADP+
-
-
-
-
?
Fe(III)-bacillibactin + NADPH + H+
Fe(II) + bacillibacitin + NADP+
-
-
-
-
?
Fe(III)-diethylenetriamine-N,N,N',N'',N''-pentaacetate + NADPH + H+
Fe(II) + diethylenetriamine-N,N,N',N'',N''-pentaacetate + NADP+ + H+
-
-
-
-
?
Fe(III)-o,o-EDDHA I + NADPH
Fe(II)-o,o-EDDHA I + NADP+ + H+
-
i.e. ethylenediaminebis(o-hydroxyphenyl)acetic acid
-
-
?
2 Fe(III)-siderophore + NADPH
2 Fe(II)-siderophore + NADP+ + H+
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme shows no ferric reductase activity toward ferric chloride
-
-
?
additional information
?
-
-
the enzyme shows no ferric reductase activity toward ferric chloride
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
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
-
-
?
2 Fe(III)-siderophore + NADPH
2 Fe(II)-siderophore + NADP+ + H+
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
the enzyme uses FADH2/FAD as a covalently bound cofactor rather than a substrate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
flavin
-
the enzyme is able to reduce iron compounds in the absence of free flavin, but the ferric reduction by the enzyme is enhanced by the addition of free flavin n the presence of natural chelate iron compounds but also synthetic chelate iron compounds
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.048
Fe(III)-aerobactin
-
wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
0.0014
Fe(III)-vibriobactin
-
wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°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
0.16
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
0.5762
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.24
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
1.11
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
0.95
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
2
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.02
Fe(III)-aerobactin
-
wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C
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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.02
-
crude extract, using tert-butyl hydroperoxide as substrate, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C
0.91
-
after 45.5fold purification, using tert-butyl hydroperoxide as substrate, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
detected throughout the root, but most abundant in the outer epidermal cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
metabolism
-
YqjH represents a redox factor that enhances the efficiency of ferric iron assimilation during siderophore-dependent iron homeostasis and enhances siderophore utilization in different iron acquisition pathways, including assimilation of low-potential ferric substrates that are not reduced by common cellular cofactors
physiological function
-
the enzyme is required for iron homeostasis in Escherichia coli
physiological function
-
the process known as Strategy I, occurs in the rhizosphere and is mediated by the FRO2, a ferric chelate reductase enzyme. Once reduced, the Fe(II) is taken up into the cells by the IRT1, a specific transport system
physiological function
-
the enzyme is required for iron homeostasis in Escherichia coli
-
additional information
enzyme molecular dynamics simulation, overview
Show AA Sequence and Transmembrane Helices (642 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
three-dimensional structure, generated through threading-based method, and domain analysis, comparison with X-ray and NMR structures, and structure comparison with the enzyme from Panicum sumatrense
additional information
three-dimensional structure, generated through threading-based method, and domain analysis. The enzyme contains an N-terminal domain (residues 1-51), a ferric reductase domain (residues 52-136), a linker helix (residues 137-165), a Nox_Duox_Like_FAD domain (165-355) and a helix+ C-terminal domain, analysis of secondary structure. Structure comparison with the enzyme from Oryza sativa
additional information
Panicum sumatrense RLM-37
-
three-dimensional structure, generated through threading-based method, and domain analysis. The enzyme contains an N-terminal domain (residues 1-51), a ferric reductase domain (residues 52-136), a linker helix (residues 137-165), a Nox_Duox_Like_FAD domain (165-355) and a helix+ C-terminal domain, analysis of secondary structure. Structure comparison with the enzyme from Oryza sativa
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M succinic acid-sodium phosphate dibasic-glycine buffer pH 4.0 and 18% (w/v) PEG 1500
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K55A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
R130A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
R246A
-
the variant is rather unstable, showing precipitate formation and cofactor release during protein concentration
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, butyl Toyopearl column chromatography, DEAE Sepharose column chromatography, POROS HQ-H column chromatography, and Red Sepharose column chromatography
-
Ni-NTA-Sepharose column chromatography and DEAE Sepharose column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene FRO2, DNA and amino acid sequence determination and analysis, sequence comparison, the predicted gene structure shows the presence of 6 exons and 5 introns and its protein sequence contains ferric reductase and NOX_Duox_Like_FAD_NADP domains
gene FRO2, sequence comparison, the predicted gene structure shows the presence of 6 exons and 5 introns and its protein sequence contains ferric reductase and NOX_Duox_Like_FAD_NADP domains
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
addition of Fe2+ decreases yqjH expression starting at 100 nM, with a maximum repression of 4fold occurring at 0.01 mM Fe2+. Addition of CoCl2 concentrations of more than 500 nM also repress yqjH expression by about 50%
FRO2 transcript shows abundance under iron deficiency. The addition of 300 mM bathocuproine disulfonic acid further reduces FRO2 transcript abundance in plants grown under high-iron conditions for 3 days
-
YqjI-dependent transcriptional repression is reduced when cells are exposed to elevated nickel levels, resulting in increased expression of yqjH. Upon addition of NiCl2, yqjH expression increases starting at 100 nM NiCl2, with maximum induction by 0.001 mM NiCl2 (42%). Deletion of yqjI leads to constitutive expression levels of yqjH that are 30fold higher than wild type basal expression levels
addition of Fe2+ decreases yqjH expression starting at 100 nM, with a maximum repression of 4fold occurring at 0.01 mM Fe2+. Addition of CoCl2 concentrations of more than 500 nM also repress yqjH expression by about 50%
-
addition of Fe2+ decreases yqjH expression starting at 100 nM, with a maximum repression of 4fold occurring at 0.01 mM Fe2+. Addition of CoCl2 concentrations of more than 500 nM also repress yqjH expression by about 50%
-
-
YqjI-dependent transcriptional repression is reduced when cells are exposed to elevated nickel levels, resulting in increased expression of yqjH. Upon addition of NiCl2, yqjH expression increases starting at 100 nM NiCl2, with maximum induction by 0.001 mM NiCl2 (42%). Deletion of yqjI leads to constitutive expression levels of yqjH that are 30fold higher than wild type basal expression levels
-
YqjI-dependent transcriptional repression is reduced when cells are exposed to elevated nickel levels, resulting in increased expression of yqjH. Upon addition of NiCl2, yqjH expression increases starting at 100 nM NiCl2, with maximum induction by 0.001 mM NiCl2 (42%). Deletion of yqjI leads to constitutive expression levels of yqjH that are 30fold higher than wild type basal expression levels
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Pisum sativum
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,