Literature summary for 1.7.7.1 extracted from

Hirasawa, M.; Tripathy, J.; Sommer, F.; Somasundaram, R.; Chung, J.; Nestander, M.; Kruthiventi, M.; Zabet-Moghaddam, M.; Johnson, M.; Merchant, S.; Allen, J.; Knaff, D.
Enzymatic properties of the ferredoxin-dependent nitrite reductase from Chlamydomonas reinhardtii. Evidence for hydroxylamine as a late intermediate in ammonia production (2010), Photosynth. Res., 103, 67-77.

Search for more literature for 1.7.7.1

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Chlamydomonas reinhardtii

Crystallization (Commentary)

Crystallization (Comment)	Organism
modeling of structure based on spinach nitrite reductase. Arginine and lysine residues are involved in electrostatically-stabilized binding to ferredoxin	Chlamydomonas reinhardtii

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
63000	-	x * 63000, SDS-PAGE	Chlamydomonas reinhardtii

Organism

Organism	UniProt	Comment	Textmining
Chlamydomonas reinhardtii	A8J4P1	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
hydroxylamine + reduced ferredoxin	hydroxylamine can serve as an electron-accepting substrate for the enzyme and the product of hydroxylamine reduction is ammonia. Hydroxylamine, bound to the enzyme, can serve as a late intermediate during the reduction of nitrite to ammonia catalyzed by the enzyme	Chlamydomonas reinhardtii	ammonia + H2O + oxidized ferredoxin	-	?
additional information	presence of two separate one-electron redox couples with Em values of -255 mV and -390 mV, respcetively	Chlamydomonas reinhardtii	?	-	?

Subunits

Subunits	Comment	Organism
?	x * 63000, SDS-PAGE	Chlamydomonas reinhardtii

Synonyms

Synonyms	Comment	Organism
Nii1	-	Chlamydomonas reinhardtii

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Release 2023.1 (January 2023)