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Literature summary for 1.18.1.2 extracted from
- Ferredoxin:NADP+ oxidoreductase as a target of Cd2+ inhibitory action - biochemical studies (2011), Phytochemistry, 72, 14-20.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 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 |  |
| 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 | |
| iodoacetamide | - |
Spinacia oleracea | |
| iodoacetamide | - |
Triticum aestivum | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| chloroplast | - |
Triticum aestivum | 9507 | - |
| chloroplast | - |
Spinacia oleracea | 9507 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 reduced ferredoxin + NADP+ | Triticum aestivum | - |
2 oxidized ferredoxin + NADPH + H+ | - |
r | |
| 2 reduced ferredoxin + NADP+ | Spinacia oleracea | - |
2 oxidized ferredoxin + NADPH + H+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Spinacia oleracea | - |
- |
- |
| Triticum aestivum | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| leaf | - |
Triticum aestivum | - |
| leaf | - |
Spinacia oleracea | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 reduced ferredoxin + NADP+ | - |
Triticum aestivum | 2 oxidized ferredoxin + NADPH + H+ | - |
r | |
| 2 reduced ferredoxin + NADP+ | - |
Spinacia oleracea | 2 oxidized ferredoxin + NADPH + H+ | - |
r | |
| 2 reduced ferricyanide + NADP+ | - |
Triticum aestivum | 2 oxidized ferricyanide + NADPH | - |
r | |
| 2 reduced ferricyanide + NADP+ | - |
Spinacia oleracea | 2 oxidized ferricyanide + NADPH | - |
r | |
| 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 | ? | - |
? | |
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| ferredoxin:NADP+ oxidoreductase | - |
Triticum aestivum |
| ferredoxin:NADP+ oxidoreductase | - |
Spinacia oleracea |
| FNR | - |
Triticum aestivum |
| FNR | - |
Spinacia oleracea |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.7 | - |
assay at | Triticum aestivum |
| 8.7 | - |
assay at | Spinacia oleracea |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Triticum aestivum | |
| FAD | - |
Spinacia oleracea | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.72 | - |
Cd2+ | pH 8.7, temperature not specified in the publication | Triticum aestivum | |
| 1.72 | - |
Cd2+ | pH 8.7, temperature not specified in the publication | Spinacia oleracea | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
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