Literature summary for 1.7.7.1 extracted from

Hirasawa, M.; Knaff, D.B.
Interaction of ferredoxin-linked nitrite reductase with ferredoxin (1985), Biochim. Biophys. Acta, 830, 173-180.

No PubMed abstract available

Search for more literature for 1.7.7.1

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
additional information	-	the native enzyme with a MW of 85000 can be split into a modified form of a MW of 61000 that retains activity with the non-physiological electron-donor, methyl viologen but loses most of the ferredoxin-linked activity and an 24000 MW coupling protein fragment in which the ferredoxin-binding domain is located	Spinacia oleracea

Organism

Organism	UniProt	Comment	Textmining
Spinacia oleracea	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Spinacia oleracea

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
nitrite + reduced ferredoxin	-	Spinacia oleracea	ammonia + oxidized ferredoxin	-	?

Subunits

Subunits	Comment	Organism
More	spinach: the native enzyme with a molecular weight of 85000 can be split into a modified form with a MW of 61000 that retains activity with the non-physiological electron-donor methyl viologen, but loses most of the ferredoxin-linked activity and an 24000 MW coupling protein fragment in which the ferredoxin-binding domain is located	Spinacia oleracea

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Release 2023.1 (January 2023)