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Literature summary for 1.18.1.2 extracted from
- Binding energetics of ferredoxin-NADP+ reductase with ferredoxin and its relation to function (2011), ChemBioChem, 12, 2062-2070.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Zea mays |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Zea mays | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| leaf | - |
Zea mays | - |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | ferredoxin-ferredoxin reductase binding is accompanied by endothermic reactions and driven by the entropy gain. Increases in the conformational entropy of the ferredoxin-ferredoxin reductase complex contribute largely to stabilizing the complex. Ferredoxin binding leads to both structural stiffening and softening of ferredoxin reductase. Enhanced ferredoxin reductase backbone fluctuations suggest favorable contributions to the net conformational entropy. Relatively large-scale motions of the C-terminus, a gatekeeper for interactions of NADP(H), are quenched in the closed form, thereby facilitating exit of NADP(H) | Zea mays |
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Release 2023.1 (January 2023)
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