1.16.1.7: ferric-chelate reductase (NADH)
This is an abbreviated version!
For detailed information about ferric-chelate reductase (NADH), go to the full flat file.
Word Map on EC 1.16.1.7
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1.16.1.7
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feiii
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fe-deficient
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feiii-chelate
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chlorosis
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iron-deficiency
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agriculture
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fe-sufficient
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phytosiderophores
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feiii-reducing
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lefro1
- 1.16.1.7
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feiii
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fe-deficient
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feiii-chelate
- chlorosis
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iron-deficiency
- agriculture
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fe-sufficient
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phytosiderophores
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feiii-reducing
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lefro1
Reaction
2 Fe(II)-siderophore + + = 2 Fe(III)-siderophore +
Synonyms
AhFRO1, EC 1.6.99.13, FC-R, FCR, Fe deficiency-induced ferric chelate reductase, Fe(III) chelate reductase, Fe(III) reductase, Fe(III)-chelate reductase, Fe(III)-ethylenediaminetetraacetic complex reductase, Fe(III)EDTA reductase, Fe3+-chelate reductase, ferric chelate reductase, ferric reductase oxidase, ferric-chelate reductase, FRO1, FRO2, FRO6, FRO7, iron chelate reductase, NADH-linked FeEDTA reductase, NADH-linked ferric chelate (turbo) reductase, NADH:Fe3+ oxidoreductase, reductase, iron chelate, root Fe(III) reductase, [Fe(III)-EDTA] reductase
ECTree
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General Information
General Information on EC 1.16.1.7 - ferric-chelate reductase (NADH)
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malfunction
Fragaria sp.
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plants grown in the absence of iron show Fe deficiency symptoms with smaller chlorotic leaves, less biomass, acidification of the nutrient solution, and roots that are smaller and less ramified and that contain a higher content of Cu2+
physiological function
additional information
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in response to iron deficiency, dicots employ a reduction-based mechanism by inducing FCR at the root plasma membrane to enhance iron uptake
physiological function
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biological reduction of Fe(III)EDTA is one of the key steps in nitrogen oxides removal in the integrated approach of metal chelate absorption combined with microbial reduction. Simultaneous reduction of NO chelated by Fe(II)EDTA (Fe(II)EDTA-NO) and Fe(III)EDTA
physiological function
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ferric-chelate reductase is a key enzyme in Fe uptake
physiological function
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ferric-chelate reductase is a key enzyme in Fe uptake
physiological function
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ferric-chelate reductase which functions in the reduction of ferric to ferrous iron on root surface is a critical protein for iron homeostasis in strategy I plants. LeFRO1 is a major ferric-chelate reductase involved in iron uptake in tomato
physiological function
Fragaria sp.
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root ferric chelate reductase is regulated by iron and copper in strawberry plants, overview
physiological function
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iron (Fe) is abundant in soils but generally poorly soluble. Plants, with the exception of Graminaceae, take up Fe using an Fe(III)-chelate reductase coupled to an Fe(II) transporter. Beta vulgaris roots secrete flavins upon Fe deficiency, that are involved in Fe acquisition. Root-secretion of flavins improves Fe nutrition involving the reduction of soluble Fe(III) to Fe(II) by an Fe(III) chelate reductase (FCR). Flavin depletion does not affect the root proton extrusion and Fe(III)-chelate reductase activities of Fe-deficient plants. Plants respond to Fe deficiency by lowering the pH of the growth media and increasing the root Fe(III) reductase activity. Flavins allow Beta vulgaris plants to mine Fe from Fe(III)-oxides
physiological function
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biological reduction of Fe(III)EDTA is one of the key steps in nitrogen oxides removal in the integrated approach of metal chelate absorption combined with microbial reduction. Simultaneous reduction of NO chelated by Fe(II)EDTA (Fe(II)EDTA-NO) and Fe(III)EDTA
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ferric reductase activity in leaves of transgenic plants grown under iron-sufficient or iron-deficient conditions is 2.13 and 1.26fold higher than in control plants, respectively. The enhanced ferric reductase activity leads to increased concentrations of ferrous iron and chlorophyll, and reduces the iron deficiency chlorosis in the transgenic plants, compared to the control plants. In roots, the concentration of ferrous iron and ferric reductase activity are not significantly different in the transgenic plants compared to the control plants, phenotype, overview
additional information
relationship between the protection of photosynthesis and the light-dependent FCR activity on plasma membranes and chloroplast envelopes, overview. FCR activities in barley chloroplasts are not severely damaged by Fe deficiency, enzyme activities under iron deficient conditions, overview
additional information
relationship between the protection of photosynthesis and the light-dependent FCR activity on plasma membranes and chloroplast envelopes, overview. FCR activities in barley chloroplasts are not severely damaged by Fe deficiency, enzyme activities under iron deficient conditions, overview
additional information
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relationship between the protection of photosynthesis and the light-dependent FCR activity on plasma membranes and chloroplast envelopes, overview. FCR activities in sorghum chloroplasts are not severely damaged by Fe deficiency, enzyme activities under iron deficient conditions, overview
additional information
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Ala112 of LeFRO1 is critical for maintaining the high activity of ferric-chelate reductase, modification of this amino acid results in a significant reduction of enzyme activity. The combination of the amino acid residue Ile at the site 24 with Lys at the site 582 plays a positive role in the enzyme activity of LeFRO1, genotyping, overview
additional information
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relationship between the protection of photosynthesis and the light-dependent FCR activity on plasma membranes and chloroplast envelopes, overview. FCR activities in sorghum chloroplasts are not severely damaged by Fe deficiency, enzyme activities under iron deficient conditions, overview
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additional information
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relationship between the protection of photosynthesis and the light-dependent FCR activity on plasma membranes and chloroplast envelopes, overview. FCR activities in barley chloroplasts are not severely damaged by Fe deficiency, enzyme activities under iron deficient conditions, overview
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