EC Number | Application | Comment | Organism |
---|---|---|---|
1.18.6.1 | energy production | the reaction produces H2 as a by-product and is interesting for production of clean energy | Azotobacter vinelandii |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.18.6.1 | additional information | in vitro synthesis of the iron-molybdenum cofactor of nitrogenase using purified proteins, a minimal in vitro system, containing NifB, NifEN, and NifH proteins, together with Fe2+, S2-, MoO4 2-, R-homocitrate, S-adenosyl methionine, and Mg-ATP, is sufficient for the synthesis of FeMo-co and the activation of apo-dinitrogenase under anaerobic-reducing conditions, modeling, overview | Azotobacter vinelandii |
1.18.6.1 | V70I | the mutant is suitable for analysis of reaction intermediates, since it exhibits the highest concentration of trapped H+-intermediate when turned over under Ar | Azotobacter vinelandii |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.18.6.1 | additional information | - |
additional information | kinetic analysis, overview | Azotobacter vinelandii |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.18.6.1 | Fe2+ | part of the iron-molybdenum and molybdenum-iron cofactors | Azotobacter vinelandii | |
1.18.6.1 | Mg2+ | - |
Azotobacter vinelandii | |
1.18.6.1 | Molybdenum | part of the iron-molybdenum and molybdenum-iron cofactors | Azotobacter vinelandii |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.18.6.1 | N2 + 8 e- + 16 ATP + 8 H+ | Azotobacter vinelandii | the enzyme is responsible for biological nitrogen fixation, the conversion of atmospheric N2 to NH3 | 2 NH3 + H2 + 16 ADP + 16 phosphate | - |
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EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.18.6.1 | Azotobacter vinelandii | - |
- |
- |
1.18.6.1 | Azotobacter vinelandii | - |
recombinant strain DJ1373 expressing mutant V70I | - |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.18.6.1 | 4 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate | reaction mechanism, determination of reaction intermediates, two-step relaxation of the nitrogenase H+/H+ intermediate during step-annealing,both steps show large solvent kinetic isotope effects, step A is the catalytically central state that is activated for N2 binding by the accumulation of 4 electrons, and step B accumulates 2 electrons, overview | Azotobacter vinelandii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.18.6.1 | N2 + 8 e- + 16 ATP + 8 H+ | - |
Azotobacter vinelandii | 2 NH3 + H2 + 16 ADP + 16 phosphate | - |
? | |
1.18.6.1 | N2 + 8 e- + 16 ATP + 8 H+ | the enzyme is responsible for biological nitrogen fixation, the conversion of atmospheric N2 to NH3 | Azotobacter vinelandii | 2 NH3 + H2 + 16 ADP + 16 phosphate | - |
? | |
1.18.6.1 | N2 + 8 e- + 16 ATP + 8 H+ | relaxation of the nitrogenase H+/H+ intermediate during step-annealing | Azotobacter vinelandii | 2 NH3 + H2 + 16 ADP + 16 phosphate | - |
? |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.18.6.1 | ATP | - |
Azotobacter vinelandii | |
1.18.6.1 | FeMo protein | FeMo-co is composed of 7Fe, 9S, Mo, R-homocitrate, and one unidentified light atom, in vitro synthesis of the iron-molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum, and homocitrate using purified Nif proteins, Several nif genes are essential for FeMo-co synthesis in vivo, e.g., nifB, nifU, nifS, nifH, nifN, nifE, and nifV, modeling, overview | Azotobacter vinelandii |