Activating Compound | Comment | Organism | Structure |
---|---|---|---|
light | light-driven activation of the molybdenum-iron-protein, MoFeP, of nitrogenase for substrate reduction is independent of ATP hydrolysis and the iron-protein, FeP, binding structure and mechanism, overview | Azotobacter vinelandii |
Protein Variants | Comment | Organism |
---|---|---|
additional information | a MoFeP variant labeled on its surface with a Ru-photosensitizer is shown to photocatalytically reduce protons and acetylene, most likely at its active site, FeMoco. The uncoupling of nitrogenase catalysis from ATP hydrolysis enables the study of redox dynamics within MoFeP and the population of discrete reaction intermediates, overview | Azotobacter vinelandii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Azotobacter vinelandii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
N2 + 8 e- + 8 H+ + 16 ATP | Azotobacter vinelandii | - |
2 NH3 + H2 + 16 ADP + 16 phosphate | - |
ir |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Azotobacter vinelandii | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
N2 + 8 e- + 8 H+ + 16 ATP | - |
Azotobacter vinelandii | 2 NH3 + H2 + 16 ADP + 16 phosphate | - |
ir | |
N2 + 8 e- + 8 H+ + 16 ATP | cofactor binding structure analysis, Fe protein-MoFe protein complex structure in the presence of ATP analogue AMPPCP, overview | Azotobacter vinelandii | 2 NH3 + H2 + 16 ADP + 16 phosphate | - |
ir |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Azotobacter vinelandii | |
FeMo cofactor | binding structure and mechanism, overview | Azotobacter vinelandii |