Inhibitors | Comment | Organism | Structure |
---|---|---|---|
O2 | irreversibly inactivated | Cyanobacterium sp. |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Molybdenum | - |
Trichormus variabilis | |
Molybdenum | enzyme consists of 2 proteins: a molybdenum and iron-containing protein (MoFe protein, component I, dinitrogenase) and an iron containing protein (Fe protein, component II, dinitrogenase reductase), together they form the active nitrogenase complex | Cyanobacterium sp. |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
60000 | - |
Fe protein | Cyanobacterium sp. |
216000 | - |
nitrogenase complex | Cyanobacterium sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O | Trichormus variabilis | - |
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate | - |
? | |
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O | Cyanobacterium sp. | ferredoxin normally functions as immediate electron donor to nitrogenase, during iron starvation it is replaced by flavodoxin | 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate | - |
? | |
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O | Cyanobacterium sp. | regulation | 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate | - |
? | |
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O | Cyanobacterium sp. | biological N2 fixation | 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cyanobacterium sp. | - |
- |
- |
Trichormus variabilis | - |
- |
- |
Oxidation Stability | Organism |
---|---|
extreme sensitivity to O2 | Cyanobacterium sp. |
stable to O2, no loss in nitrogen fixation activity | Trichormus variabilis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 | Trichormus variabilis | |
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 | Cyanobacterium sp. |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
heterocyst | in heterocysteous cyanobacteria exclusive site of N2 fixation during aerobic growth | Cyanobacterium sp. | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O | - |
Cyanobacterium sp. | 2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate | - |
? | |
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O | - |
Trichormus variabilis | 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate | - |
? | |
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O | - |
Cyanobacterium sp. | 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate | - |
? | |
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O | ferredoxin normally functions as immediate electron donor to nitrogenase, during iron starvation it is replaced by flavodoxin | Cyanobacterium sp. | 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate | - |
? | |
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O | regulation | Cyanobacterium sp. | 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate | - |
? | |
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O | biological N2 fixation | Cyanobacterium sp. | 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | - |
Cyanobacterium sp. |