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Literature summary extracted from

  • Burns, R.C.; Hardy, R.W.F.
    Purification of nitrogenase and crystallization of its Mo-Fe protein (1972), Methods Enzymol., 24, 480-496.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.18.6.1 MoFe protein Azotobacter vinelandii
1.18.6.1 purified enzyme is diluted at room temperature with 3 volumes of Tris-HCl 0.01 M, pH 7.2, immediate crystal formation Azotobacter vinelandii

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.18.6.1 1,10-phenanthroline
-
 Azotobacter vinelandii
1.18.6.1 1,2-Dihydroxybenzene 3,5-disulfonate
-
 Azotobacter vinelandii
1.18.6.1 2,2'-dipyridyl
-
 Azotobacter vinelandii
1.18.6.1 2,3-Dimercaptopropanol
-
 Azotobacter vinelandii
1.18.6.1 ADP
-
 Azotobacter vinelandii
1.18.6.1 CO
-
 Azotobacter vinelandii
1.18.6.1 Cu2+
-
 Azotobacter vinelandii
1.18.6.1 H2
-
 Azotobacter vinelandii
1.18.6.1 additional information high ionic strength inhibits Azotobacter vinelandii
1.18.6.1 NO
-
 Azotobacter vinelandii
1.18.6.1 O2
-
 Azotobacter vinelandii
1.18.6.1 Zn2+
-
 Azotobacter vinelandii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.18.6.1 additional information
-
 additional information
-
 Azotobacter vinelandii
1.18.6.1 0.1
-
 N2
-
 Azotobacter vinelandii
1.18.6.1 0.3
-
 ATP
-
 Azotobacter vinelandii
1.18.6.1 0.4 1.2 C2H2
-
 Azotobacter vinelandii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.18.6.1 Co2+ divalent cation requirement is satisfied by Co2+, is best supported by concentrations of divalent cation one-half the concentration of ATP Azotobacter vinelandii
1.18.6.1 Fe2+ divalent cation requirement is satisfied by Fe2+, is best supported by concentrations of divalent cation one-half the concentration of ATP Azotobacter vinelandii
1.18.6.1 Mg2+ divalent metal requirement is satisfied by Mg2+, reaction is best supported by concentration of divalent cation one-half the concentration of ATP Azotobacter vinelandii
1.18.6.1 Mn2+ divalent cation requirement is satisfied by Mn2+, is best supported by concentrations of divalent cation one-half the concentration of ATP Azotobacter vinelandii
1.18.6.1 Ni2+ divalent cation requirement is satisfied by Ni2+, is best supported by concentrations of divalent cation one-half the concentration of ATP 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
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.18.6.1
-
 Azotobacter vinelandii

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
-
-
 Azotobacter vinelandii

Storage Stability

EC Number Storage Stability Organism
1.18.6.1 -15°C, anaerobic storage, overnight, complete loss of activity Azotobacter vinelandii
1.18.6.1 22°C, O2-free atmosphere, pH 7-8, stable Azotobacter vinelandii
1.18.6.1 5°C, O2-free atmosphere, overnight, 80% loss of activity 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 1-propyne, 1-butyne and allene are reduced to the corresponding alkenes Azotobacter vinelandii 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 reduced ferredoxin + H+ + CH3NC + ATP
-
 Azotobacter vinelandii oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
 ?
1.18.6.1 reduced ferredoxin + H+ + N3- + ATP
-
 Azotobacter vinelandii oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
 ?