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Literature summary 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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.7.7.1 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

EC Number Organism UniProt Comment Textmining
1.7.7.1 Spinacia oleracea
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.7.1
-
 Spinacia oleracea

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
1.7.7.1 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