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Literature summary extracted from

  • Miller, R.; Eady, R.
    Molybdenum and vanadium nitrogenases of Azotobacter chroococcum. Low temperature favours N2 reduction by vanadium nitrogenase (1988), Biochem. J., 256, 429-432 .
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.18.6.2 Iron enhanced low-temperature activity of vanadium-dependent nitrogenase is associated with the Fe protein of V nitrogenase Azotobacter chroococcum

Organism

EC Number Organism UniProt Comment Textmining
1.18.6.2 Azotobacter chroococcum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.6.2 12 reduced ferredoxin + 12 H+ + N2 + 40 ATP + 40 H2O
-
Azotobacter chroococcum 12 oxidized ferredoxin + 3 H2 + 2 NH3 + 40 ADP + 40 phosphate
-
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Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.18.6.2 30
-
-
Azotobacter chroococcum

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.18.6.2 5
-
2.4% of maximum activity, NH3-assay Azotobacter chroococcum
1.18.6.2 10
-
9.1% of maximum activity, NH3-assay Azotobacter chroococcum
1.18.6.2 16
-
30% of maximum activity, NH3-assay Azotobacter chroococcum