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Literature summary for 1.7.7.2 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
Search for more literature for 1.7.7.2

Inhibitors

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

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum Mo center Leptolyngbya boryana

Organism

Organism UniProt Comment Textmining
Leptolyngbya boryana
-
-
-

Oxidation Stability

Oxidation Stability Organism
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)

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