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Literature summary extracted from

  • Barney, B.M.; McClead, J.; Lukoyanov, D.; Laryukhin, M.; Yang, T.C.; Dean, D.R.; Hoffman, B.M.; Seefeldt, L.C.
    Diazene (HN=NH) is a substrate for nitrogenase: insights into the pathway of N2 reduction (2007), Biochemistry, 46, 6784-6794.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.19.6.1 diazene inhibits proton reduction Azotobacter vinelandii
1.19.6.1 H2 inhibits both N2 and diazene reduction Azotobacter vinelandii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.19.6.1 additional information
-
 additional information steady-state turnover analysis with diazene and hydrazine bound to the FeMo cofactor, overview Azotobacter vinelandii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.19.6.1 Fe2+ in the the active site metal cluster FeMo-cofactor, the Fe protein contains a single [4Fe-4S] cluster plus two MgATP binding sites Azotobacter vinelandii
1.19.6.1 Mg2+ the Fe protein contains a single [4Fe-4S] cluster plus two MgATP binding sites Azotobacter vinelandii
1.19.6.1 Molybdenum in the the active site metal cluster FeMo-cofactor Azotobacter vinelandii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.19.6.1 reduced ferredoxin + H+ + N2 + ATP Azotobacter vinelandii
-
 oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
 ?
1.19.6.1 reduced ferredoxin + H+ + N2 + ATP Azotobacter vinelandii DJ995
-
 oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.19.6.1 Azotobacter vinelandii
-
-
-
1.19.6.1 Azotobacter vinelandii DJ995
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.19.6.1 additional information diazene is a substrate for the wild-type nitrogenase and is reduced to NH3, hydrazine in reduced in absence of H2. Diazene joins the normal N2-reduction pathway, and diazene- and hydrazine-trapped turnover states represent the same intermediate in the normal reduction of N2 by nitrogenase, implications for the N2 reductionmechanism, overview Azotobacter vinelandii ?
-
 ?
1.19.6.1 additional information diazene is a substrate for the wild-type nitrogenase and is reduced to NH3, hydrazine in reduced in absence of H2. Diazene joins the normal N2-reduction pathway, and diazene- and hydrazine-trapped turnover states represent the same intermediate in the normal reduction of N2 by nitrogenase, implications for the N2 reductionmechanism, overview Azotobacter vinelandii DJ995 ?
-
 ?
1.19.6.1 N2H2 + H+ diazene is a substrate for the wild-type nitrogenase and is reduced to NH3, cofactor binding structure and kinetic mechanism, overview Azotobacter vinelandii NH3
-
 ?
1.19.6.1 N2H2 + H+ diazene is a substrate for the wild-type nitrogenase and is reduced to NH3, cofactor binding structure and kinetic mechanism, overview Azotobacter vinelandii DJ995 NH3
-
 ?
1.19.6.1 reduced ferredoxin + H+ + N2 + ATP
-
 Azotobacter vinelandii oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
 ?
1.19.6.1 reduced ferredoxin + H+ + N2 + ATP nitrogenase catalyzes the sequential addition of six electrons and six protons to a N2 that is bound to the active site metal cluster FeMo-cofactor, yielding two ammonia molecules Azotobacter vinelandii oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
 ?
1.19.6.1 reduced ferredoxin + H+ + N2 + ATP
-
 Azotobacter vinelandii DJ995 oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
 ?
1.19.6.1 reduced ferredoxin + H+ + N2 + ATP nitrogenase catalyzes the sequential addition of six electrons and six protons to a N2 that is bound to the active site metal cluster FeMo-cofactor, yielding two ammonia molecules Azotobacter vinelandii DJ995 oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
1.19.6.1 More the Mo-based nitrogenase is composed of two component proteins called the Fe protein and the MoFe protein Azotobacter vinelandii

Synonyms

EC Number Synonyms Comment Organism
1.19.6.1 nitrogenase
-
 Azotobacter vinelandii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.19.6.1 30
-
 assay at Azotobacter vinelandii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.19.6.1 7.2
-
 assay at Azotobacter vinelandii

Cofactor

EC Number Cofactor Comment Organism Structure
1.19.6.1 ATP the Fe protein contains a single [4Fe-4S] cluster plus two MgATP binding sites Azotobacter vinelandii
1.19.6.1 FeMo cofactor the active site metal cluster FeMo-cofactor Azotobacter vinelandii