Literature summary for 1.8.7.1 extracted from

Kim, J.Y.; Kinoshita, M.; Kume, S.; Gt, H.; Sugiki, T.; Ladbury, J.E.; Kojima, C.; Ikegami, T.; Kurisu, G.; Goto, Y.; Hase, T.; Lee, Y.H.
Non-covalent forces tune the electron transfer complex between ferredoxin and sulfite reductase to optimize enzymatic activity (2016), Biochem. J., 473, 3837-3854 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Zea mays

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
chloroplast	-	Zea mays	9507	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
NaCl	at 40-70 mM NaCl in 50 mM Tris/HCl buffer, close to the physiological conditions in plant chloroplasts, delicate interprotein regulation optimizes SiR activity. At NaCl concentrations above several hundred millimolar, collision and diffusion may limit the formation of the stable electron-transfer competent complex	Zea mays

Organism

Organism	UniProt	Comment	Textmining
Zea mays	O23813	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Zea mays	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	ferredoxin:SiR complex formation and interprotein affinity are thermodynamically adjusted by both enthalpy and entropy through electrostatic and non-electrostatic interactions. A combination of electrostatic and non-electrostatic forces stabilizes the complex with similar interfaces and modulates the binding affinity and mode	Zea mays	?	-	?

Synonyms

Synonyms	Comment	Organism
SIR	-	Zea mays

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Release 2023.1 (January 2023)