A flavoprotein. The enzyme catalyses the reduction of bound ferric iron in a variety of iron chelators (siderophores), resulting in the release of ferrous iron. The enzyme from the hyperthermophilic archaeon Archaeoglobus fulgidus is not active with uncomplexed Fe(III). cf. EC 1.16.1.7, ferric-chelate reductase (NADH) and EC 1.16.1.9, ferric-chelate reductase (NADPH).
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SYSTEMATIC NAME
IUBMB Comments
Fe(II)-siderophore:NAD(P)+ oxidoreductase
A flavoprotein. The enzyme catalyses the reduction of bound ferric iron in a variety of iron chelators (siderophores), resulting in the release of ferrous iron. The enzyme from the hyperthermophilic archaeon Archaeoglobus fulgidus is not active with uncomplexed Fe(III). cf. EC 1.16.1.7, ferric-chelate reductase (NADH) and EC 1.16.1.9, ferric-chelate reductase (NADPH).
no activity is obtained with uncomplexed Fe3+, i.e. FeCl3 and Fe(OH)3, with the menaquinone analog dimethylnaphthoquinone or with Fe2+-EDTA. The enzyme does not reduce EDTA-chelated Ag+ and Cu2+. With Fe3+-EDTA as the electron acceptor, the purified enzyme exhibits a slightly higher affinity and Vmax for NADH than for NADPH as the electron donor
no activity is obtained with uncomplexed Fe3+, i.e. FeCl3 and Fe(OH)3, with the menaquinone analog dimethylnaphthoquinone or with Fe2+-EDTA. The enzyme does not reduce EDTA-chelated Ag+ and Cu2+. With Fe3+-EDTA as the electron acceptor, the purified enzyme exhibits a slightly higher affinity and Vmax for NADH than for NADPH as the electron donor
reduction of Fe(III)-ethylenediaminetetraacetic acid is monitored spectrophotometrically by the Fe(II)-bathophenanthroline disulfonate complex formation for enzyme activity determination
rates with NADPH as the electron donor are not significantly different from those with NADH as the donor, activity in cell extract, enzyme not purified
with Fe3+-EDTA as the electron acceptor, the purified enzyme exhibits a slightly higher affinity and Vmax for NADH than for NADPH as the electron donor
rates with NADPH as the electron donor are not significantly different from those with NADH as the donor, activity in cell extract, enzyme not purified
with Fe3+-EDTA as the electron acceptor, the purified enzyme exhibits a slightly higher affinity and Vmax for NADH than for NADPH as the electron donor
a protein kinase, required for enzyme activity because CIPK23 helps in iron aquisition. Involvement of calcium-dependent CBL-CIPK23 complexes in the regulation of iron acquisition
FCR activity of inner envelope of chloroplast vesicles isolated from Fe-deficient plants shows clear biphasic kinetics. Using NADPH, biphasic saturation kinetics are measured with the first saturation found at KM = 0.0046 mM Fe(III)-EDTA, and the second saturation found at KM = 0.0557 mM Fe(III)-EDTA. In the presence of NADH, the saturation kinetics is monophasic, the sole saturation reaction rate is significantly lower, and the KM value of the reaction is significantly higher with 0.0834 mM Fe(III)-EDTA compared to the second saturation measured with NADPH. In vesicles isolated from Fe-sufficient plants, the affinity of the enzyme does not change with KM = 0.0042mM Fe(III)-EDTA. The second, low-affinity saturation point, KM = 0.155 mM Fe(III)-EDTA is significantly higher than that in Fe-sufficient plants, with a reaction rate that is also somewhat higher than in the envelope of chloroplast membranes of Fe-sufficient plants
NADH-dependent ferric reductase activity increases approximately 100fold in whole-cell extracts from iron-grown cells relative to those from nitrate-grown cells
NADH-dependent ferric reductase activity increases approximately 100fold in whole-cell extracts from iron-grown cells relative to those from nitrate-grown cells
NADH-dependent ferric reductase activity increases approximately 100fold in whole-cell extracts from iron-grown cells relative to those from nitrate-grown cells
NADH-dependent ferric reductase activity increases approximately 100fold in whole-cell extracts from iron-grown cells relative to those from nitrate-grown cells
ferric chelate reductase 1 like protein (FRRS1L) mutations in human lead to epilepsy, choreoathetosis, and cognitive deficits. Overexpression of enzyme FRRS1L in hippocampal neurons does not change glutamatergic synaptic transmission, but single-cell knockout of FRRS1L strongly reduces the surface and total expression levels of GluA1 in cultured hippocampal neurons, and significantly decreases AMPAR-mediated synaptic transmission in mouse hippocampal pyramidal neurons
lesion of CIPK23 renders Arabidopsis mutants hypersensitive to iron deficiency by downregulating ferric chelate reductase activity, leading to chlorosis in young leaves and lower iron concentration than wild-type plants under iron-deficient conditions, phenotype, overview
lesion of CIPK23 renders Arabidopsis mutants hypersensitive to iron deficiency by downregulating ferric chelate reductase activity, leading to chlorosis in young leaves and lower iron concentration than wild-type plants under iron-deficient conditions, phenotype, overview
ferric chelate reductase 1 like protein (FRRS1L) mutations in human lead to epilepsy, choreoathetosis, and cognitive deficits. Overexpression of enzyme FRRS1L in hippocampal neurons does not change glutamatergic synaptic transmission, but single-cell knockout of FRRS1L strongly reduces the surface and total expression levels of GluA1 in cultured hippocampal neurons, and significantly decreases AMPAR-mediated synaptic transmission in mouse hippocampal pyramidal neurons
the protein kinase CIPK23 is involved in iron acquisition. Lesion of CIPK23 renders Arabidopsis mutants hypersensitive to iron deficiency, as evidenced by stronger chlorosis in young leaves and lower iron concentration than wild-type plants under iron-deficient conditions by downregulating ferric chelate reductase activity. Iron deficiency evokes an increase in cytosolic Ca2+ concentration, and the elevated Ca2+ binds to CBL1/CBL9, leading to activation of CIPK23, CBL-CIPK23complexes might be as nutritional sensors to sense and regulate the mineral homeostasis in Arabisopsis thaliana. Regulation of FCR activity by CIPK23 may not be achieved by modulation of genes FRO2, FRO3 and FRO5 at transcriptional level
the protein kinase CIPK23 is involved in iron acquisition. Lesion of CIPK23 renders Arabidopsis mutants hypersensitive to iron deficiency, as evidenced by stronger chlorosis in young leaves and lower iron concentration than wild-type plants under iron-deficient conditions by downregulating ferric chelate reductase activity. Iron deficiency evokes an increase in cytosolic Ca2+ concentration, and the elevated Ca2+ binds to CBL1/CBL9, leading to activation of CIPK23, CBL-CIPK23complexes might be as nutritional sensors to sense and regulate the mineral homeostasis in Arabisopsis thaliana. Regulation of FCR activity by CIPK23 may not be achieved by modulation of genes FRO2, FRO3 and FRO5 at transcriptional level
iron has an essential role in the biosynthesis of chlorophylls and redox cofactors, and thus chloroplast iron uptake is a process of special importance. The chloroplast ferric chelate oxidoreductase (cFRO) has a crucial role in this process
recombinant FRRS1L interacts with both GluA1 and GluA2 subunits of AMPA receptors, AMPARs, but does not form dimers/oligomers, in HEK293 cells. Important role of FRRS1L in the regulation of excitatory synaptic strength. FRRS1L is a component of native AMPAR complexes in the brain
recombinant FRRS1L interacts with both GluA1 and GluA2 subunits of AMPA receptors, AMPARs, but does not form dimers/oligomers, in HEK293 cells. Important role of FRRS1L in the regulation of excitatory synaptic strength. FRRS1L is a component of native AMPAR complexes in the brain
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of the homodimeric enzyme are grown at 4°C by the hanging drop vapor diffusion technique, with protein solution at a concentration of 25 mg/ml in 0.1 M Tris-HCl (pH 7.5) and a reservoir consisting of 21%22% w/v PEG4000, 0.1 M sodium acetate, and 0.1 M Tris-HCl (pH 8.4). The crystallization drops are microseeded after 2024 hr. Crystal structure of recombinant enzyme containing a bound FMN solved at 1.5 A resolution. The NADP+-bound enzyme complex is determined at 1.65 A resolution
isolation of chloroplasts and chloroplast envelope membranes from leaves. Before isolating chloroplasts, the chlorophyll content and photosynthetic activity of Fe-sufficient and Fe-deficient leaves are measured, as indicators of the iron nutrition status