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Literature summary for 1.19.6.1 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

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

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
-
-
Azotobacter vinelandii DJ995
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
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 ?
-
?
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
-
?
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
-
?
reduced ferredoxin + H+ + N2 + ATP
-
Azotobacter vinelandii oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
?
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
-
?
reduced ferredoxin + H+ + N2 + ATP
-
Azotobacter vinelandii DJ995 oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
?
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

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

Synonyms

Synonyms Comment Organism
nitrogenase
-
Azotobacter vinelandii

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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