Inhibitors | Comment | Organism | Structure |
---|---|---|---|
diazene | inhibits proton reduction | Azotobacter vinelandii | |
H2 | inhibits both N2 and diazene reduction | Azotobacter vinelandii |
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 | 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Azotobacter vinelandii | - |
- |
- |
Azotobacter vinelandii DJ995 | - |
- |
- |
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 | Comment | Organism |
---|---|---|
More | the Mo-based nitrogenase is composed of two component proteins called the Fe protein and the MoFe protein | Azotobacter vinelandii |
Synonyms | Comment | Organism |
---|---|---|
nitrogenase | - |
Azotobacter vinelandii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Azotobacter vinelandii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | - |
assay at | Azotobacter vinelandii |
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 |