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Literature summary extracted from

  • Grzyb, J.; Bojko, M.; Waloszek, A.; Strzalka, K.
    Ferredoxin:NADP+ oxidoreductase as a target of Cd2+ inhibitory action - biochemical studies (2011), Phytochemistry, 72, 14-20.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.18.1.2 Cd2+ noncompetitive type of inhibition, effect of cadmium binding is significant disturbance in the electron transfer process from FAD to dibromothymoqinone, but less interference with the reduction of ferricyanide. It causes a strong inhibition of ferredoxin reduction, indicating that Cd-induced changes in the FNR structure disrupt ferredoxin binding. Iodoacetamide blocks the sensitivity to Cd2+ inhibition. pH-Dependent inhibition: to interact with cadmium in a mode which leads to inhibition, the cysteine residues of FNR have to be charged. Almost no inhibition in pH lower than pH 7.7, while in pH higher than pH 8.1 the reduction of activity caused by cadmium ions increases, FNR cysteine-peptide mapping, overview. Triticum aestivum FNR is more sensitive to lower cadmium concentrations than the Spinacia oleracea enzyme Spinacia oleracea
1.18.1.2 Cd2+ noncompetitive type of inhibition, effect of cadmium binding is significant disturbance in the electron transfer process from FAD to dibromothymoqinone, but less interference with the reduction of ferricyanide. It causes a strong inhibition of ferredoxin reduction, indicating that Cd-induced changes in the FNR structure disrupt ferredoxin binding. Iodoacetamide blocks the sensitivity to Cd2+ inhibition. pH-Dependent inhibition: to interact with cadmium in a mode which leads to inhibition, the cysteine residues of FNR have to be charged. Almost no inhibition in pH lower than pH 7.7, while in pH higher than pH 8.1 the reduction of activity caused by cadmium ions increases, FNR cysteine-peptide mapping, overview. Triticum aestivum FNR is more sensitive to lower cadmium concentrations than the Spinacia oleracea enzyme Triticum aestivum
1.18.1.2 iodoacetamide
-
Spinacia oleracea
1.18.1.2 iodoacetamide
-
Triticum aestivum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.18.1.2 chloroplast
-
Triticum aestivum 9507
-
1.18.1.2 chloroplast
-
Spinacia oleracea 9507
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.1.2 2 reduced ferredoxin + NADP+ Triticum aestivum
-
2 oxidized ferredoxin + NADPH + H+
-
r
1.18.1.2 2 reduced ferredoxin + NADP+ Spinacia oleracea
-
2 oxidized ferredoxin + NADPH + H+
-
r

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Spinacia oleracea
-
-
-
1.18.1.2 Triticum aestivum
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.18.1.2 leaf
-
Triticum aestivum
-
1.18.1.2 leaf
-
Spinacia oleracea
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 2 reduced ferredoxin + NADP+
-
Triticum aestivum 2 oxidized ferredoxin + NADPH + H+
-
r
1.18.1.2 2 reduced ferredoxin + NADP+
-
Spinacia oleracea 2 oxidized ferredoxin + NADPH + H+
-
r
1.18.1.2 2 reduced ferricyanide + NADP+
-
Triticum aestivum 2 oxidized ferricyanide + NADPH
-
r
1.18.1.2 2 reduced ferricyanide + NADP+
-
Spinacia oleracea 2 oxidized ferricyanide + NADPH
-
r
1.18.1.2 additional information in vitro, the enzyme catalyses the NADPH-dependent reduction of various substrates, including ferredoxin, the analogue of its redox centre-ferricyanide, and the analogue of quinones, which is dibromothymoquinone Triticum aestivum ?
-
?
1.18.1.2 additional information in vitro, the enzyme catalyses the NADPH-dependent reduction of various substrates, including ferredoxin, the analogue of its redox centre-ferricyanide, and the analogue of quinones, which is dibromothymoquinone Spinacia oleracea ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.18.1.2 ferredoxin:NADP+ oxidoreductase
-
Triticum aestivum
1.18.1.2 ferredoxin:NADP+ oxidoreductase
-
Spinacia oleracea
1.18.1.2 FNR
-
Triticum aestivum
1.18.1.2 FNR
-
Spinacia oleracea

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.18.1.2 8.7
-
assay at Triticum aestivum
1.18.1.2 8.7
-
assay at Spinacia oleracea

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD
-
Triticum aestivum
1.18.1.2 FAD
-
Spinacia oleracea

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.18.1.2 1.72
-
Cd2+ pH 8.7, temperature not specified in the publication Triticum aestivum
1.18.1.2 1.72
-
Cd2+ pH 8.7, temperature not specified in the publication Spinacia oleracea

General Information

EC Number General Information Comment Organism
1.18.1.2 physiological function FNR catalyses the ferredoxin-dependent reduction of NADP+ to NADPH in linear photosynthetic electron transport. The enzyme also transfers electrons from reduced ferredoxin or NADPH to the cytochrome b6f complex in cyclic electron transport Triticum aestivum
1.18.1.2 physiological function FNR catalyses the ferredoxin-dependent reduction of NADP+ to NADPH in linear photosynthetic electron transport. The enzyme also transfers electrons from reduced ferredoxin or NADPH to the cytochrome b6f complex in cyclic electron transport Spinacia oleracea