Literature summary extracted from

Lee, Y.H.; Ikegami, T.; Standley, D.M.; Sakurai, K.; Hase, T.; Goto, Y.
Binding energetics of ferredoxin-NADP+ reductase with ferredoxin and its relation to function (2011), ChemBioChem, 12, 2062-2070.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.18.1.2	expression in Escherichia coli	Zea mays

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.18.1.2	Zea mays	-	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
1.18.1.2	leaf	-	Zea mays	-

General Information

EC Number	General Information	Comment	Organism
1.18.1.2	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)