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Literature summary extracted from

  • Mikami, B.; Ida, S.
    Reversible inactivation of ferredoxin-nitrate reductase from the cyanobacterium Plectonema boryanum. The role of superoxide anion and cyanide (1986), Plant Cell Physiol., 27, 1013-1021.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.7.7.2 azide competitive inhibitor Leptolyngbya boryana
1.7.7.2 cyanide competitive inhibitor Leptolyngbya boryana
1.7.7.2 Dithionite inactivation can be suppressed by cyanide and azide and specifically prevented by superoxide dismutase Leptolyngbya boryana
1.7.7.2 EDTA photoactivated EDTA, irreversible inactivation Leptolyngbya boryana
1.7.7.2 FAD photoactivated FAD, irreversible inactivation Leptolyngbya boryana

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.7.2 Molybdenum Mo center Leptolyngbya boryana

Organism

EC Number Organism UniProt Comment Textmining
1.7.7.2 Leptolyngbya boryana
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.7.7.2 reversible inactivation of ferredoxin-linked activity by exposure of dithionite solution of the enzyme to air, but no effect on methyl viologen-linked activity Leptolyngbya boryana

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.7.2 nitrate + reduced ferredoxin
-
 Leptolyngbya boryana nitrite + H2O + oxidized ferredoxin
-
 ?
1.7.7.2 nitrate + reduced methyl viologen enzyme also has methyl viologen-linked activity Leptolyngbya boryana nitrite + oxidized methyl viologen
-
 ?