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Literature summary extracted from

  • Bursey, E.H.; Burgess, B.K.
    Characterization of a variant iron protein of nitrogenase that is impaired in its ability to adopt the MgATP-induced conformational change (1998), J. Biol. Chem., 273, 16927-16934.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.18.6.1 A175G shows in vivo 55% of enzyme activity compared to wild-type, in vitro 20% activity remaining with purified enzyme, slowlier conformational change upon binding of MgATP, model of steric interactions using x-ray crystal structures Azotobacter vinelandii
1.18.6.1 A175S unable to support substrate reduction because of an inability to undergo a required MgATP-induced conformational change Azotobacter vinelandii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.18.6.1 Iron
-
 Azotobacter vinelandii
1.18.6.1 Mg2+ Mg2+ required for MgATP complex Azotobacter vinelandii
1.18.6.1 Molybdenum
-
 Azotobacter vinelandii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O Azotobacter vinelandii
-
 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.18.6.1 Azotobacter vinelandii
-
 nitrogen fixation complex is encoded on nif gene cluster
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.18.6.1 4 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein Azotobacter vinelandii
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.18.6.1 additional information
-
 assay in anaerobic atmosphere required Azotobacter vinelandii
1.18.6.1 0.27
-
 mutant A175G, purified enzyme, substrate C2H2 Azotobacter vinelandii
1.18.6.1 1.52
-
 wild-type, purified enzyme, substrate C2H2 Azotobacter vinelandii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.6.1 2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
-
 Azotobacter vinelandii 2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
-
 Azotobacter vinelandii 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O MgATP-dependent Azotobacter vinelandii 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.18.6.1 30
-
 assay at Azotobacter vinelandii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.18.6.1 7.4
-
 assay at Azotobacter vinelandii