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Literature summary extracted from

  • Kim, J.; Rees, D.C.
    Nitrogenase and biological nitrogen fixation (1994), Biochemistry, 33, 389-397.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.18.6.1 homocitrate plays role in electron transfer at the [4Fe-4S] cluster to the MoFe-cofactor of the MoFe protein, can be substituted by erythro-fluorohomocitrate but not by threo-fluorohomocitrate Clostridium pasteurianum
1.18.6.1 homocitrate plays role in electron transfer at the [4Fe-4S] cluster to the MoFe-cofactor of the MoFe protein, can be substituted by erythro-fluorohomocitrate but not by threo-fluorohomocitrate Azotobacter vinelandii
1.18.6.1 homocitrate plays role in electron transfer at the [4Fe-4S] cluster to the MoFe-cofactor of the MoFe protein, can be substituted by erythro-fluorohomocitrate but not by threo-fluorohomocitrate Azotobacter chroococcum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.18.6.1 Iron contains [4Fe4S] cluster Clostridium pasteurianum
1.18.6.1 Iron contains [4Fe4S] cluster Azotobacter vinelandii
1.18.6.1 Iron contains [4Fe4S] cluster Azotobacter chroococcum
1.18.6.1 Mg2+ Mg2+ required for MgATP complex Clostridium pasteurianum
1.18.6.1 Mg2+ Mg2+ required for MgATP complex Azotobacter vinelandii
1.18.6.1 Mg2+ Mg2+ required for MgATP complex Azotobacter chroococcum
1.18.6.1 Molybdenum MoFe-cofactor contains 2 clusters of composition [4Fe-3S] and [1Mo-3Fe-3S] that are brigded by 3 nonprotein ligands Clostridium pasteurianum
1.18.6.1 Molybdenum MoFe-cofactor contains 2 clusters of composition [4Fe-3S] and [1Mo-3Fe-3S] that are brigded by 3 nonprotein ligands Azotobacter vinelandii
1.18.6.1 Molybdenum MoFe-cofactor contains 2 clusters of composition [4Fe-3S] and [1Mo-3Fe-3S] that are brigded by 3 nonprotein ligands Azotobacter chroococcum
1.18.6.1 additional information structure and organization of metal clusters Clostridium pasteurianum
1.18.6.1 additional information structure and organization of metal clusters Azotobacter vinelandii
1.18.6.1 additional information structure and organization of metal clusters Azotobacter chroococcum
1.18.6.1 Vanadium characterization of the metal clusters in the nitrogenase vanadium-iron protein Clostridium pasteurianum
1.18.6.1 Vanadium characterization of the metal clusters in the nitrogenase vanadium-iron protein Azotobacter vinelandii
1.18.6.1 Vanadium characterization of the metal clusters in the nitrogenase vanadium-iron protein Azotobacter chroococcum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.18.6.1 60000
-
 Fe protein Clostridium pasteurianum
1.18.6.1 60000
-
 Fe protein Azotobacter vinelandii
1.18.6.1 60000
-
 Fe protein Azotobacter chroococcum
1.18.6.1 60000
-
 about Clostridium pasteurianum
1.18.6.1 60000
-
 about Azotobacter vinelandii
1.18.6.1 60000
-
 about Azotobacter chroococcum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O Clostridium pasteurianum biological N2 fixation 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O Azotobacter vinelandii biological N2 fixation 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O Azotobacter chroococcum biological N2 fixation 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.18.6.1 Azotobacter chroococcum
-
 nitrogen fixation complex is encoded on nif gene cluster
-
1.18.6.1 Azotobacter vinelandii
-
 nitrogen fixation complex is encoded on nif gene cluster
-
1.18.6.1 Azotobacter vinelandii
-
 2 forms of VFe protein
-
1.18.6.1 Clostridium pasteurianum
-
 nitrogen fixation complex is encoded on nif gene cluster
-

Reaction

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 enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein Clostridium pasteurianum
a
1.18.6.1 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 Azotobacter vinelandii
a
1.18.6.1 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 Azotobacter chroococcum
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.6.1 2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
-
 Clostridium pasteurianum 2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
 ?
1.18.6.1 2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
-
 Azotobacter vinelandii 2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
 ?
1.18.6.1 2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
-
 Azotobacter chroococcum 2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O MgATP-dependent Clostridium pasteurianum 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O MgATP-dependent Azotobacter vinelandii 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O MgATP-dependent Azotobacter chroococcum 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O biological N2 fixation Clostridium pasteurianum 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O biological N2 fixation Azotobacter vinelandii 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O biological N2 fixation Azotobacter chroococcum 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
 ?
1.18.6.1 reduced ferredoxin + H+ + CN- + ATP
-
 Clostridium pasteurianum oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
 ?
1.18.6.1 reduced ferredoxin + H+ + CN- + ATP
-
 Azotobacter vinelandii oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
 ?
1.18.6.1 reduced ferredoxin + H+ + CN- + ATP
-
 Azotobacter chroococcum oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
 ?
1.18.6.1 reduced ferredoxin + H+ + N3- + ATP
-
 Clostridium pasteurianum oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
 ?
1.18.6.1 reduced ferredoxin + H+ + N3- + ATP
-
 Azotobacter vinelandii oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
 ?
1.18.6.1 reduced ferredoxin + H+ + N3- + ATP
-
 Azotobacter chroococcum oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.6.1 additional information structure models of Fe protein, MoFe protein, and MoFe-cofactor, and their metal centers, e.g. the [4Fe-4S] cluster based on crystallographic data, substrate binding and electron transfer Clostridium pasteurianum
1.18.6.1 additional information structure models of Fe protein, MoFe protein, and MoFe-cofactor, and their metal centers, e.g. the [4Fe-4S] cluster based on crystallographic data, substrate binding and electron transfer Azotobacter vinelandii
1.18.6.1 additional information structure models of Fe protein, MoFe protein, and MoFe-cofactor, and their metal centers, e.g. the [4Fe-4S] cluster based on crystallographic data, substrate binding and electron transfer Azotobacter chroococcum