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Literature summary extracted from

  • Dodsworth, J.A.; Leigh, J.A.
    NIFI1,2 inhibits nitrogenase by competing with Fe protein for binding to the MoFe protein (2007), Biochem. Biophys. Res. Commun., 364, 378-382.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.18.6.1 NIFI1,2 a regulatory protein, inhibits nitrogenase by competing with Fe protein for binding to the MoFe protein, NifI1,2 inhibits ATP- and MoFe protein-dependent oxidation of the Fe protein, and NIFI1,2 binding prevents association of the two nitrogenase components, the inhibition is relieved by 2-oxoglutarate. NIFI1,2 is unable to bind to an AlF4-stabilized Fe protein-MoFe protein complex. Both nifI1 and nifI2 are required for regulation in vivo Methanococcus maripaludis
1.19.6.1 NIFI1,2 a regulatory protein, inhibits nitrogenase by competing with Fe protein for binding to the MoFe protein, NifI1,2 inhibits ATP- and MoFe protein-dependent oxidation of the Fe protein, and NIFI1,2 binding prevents association of the two nitrogenase components, the inhibition is relieved by 2-oxoglutarate. NIFI1,2 is unable to bind to an AlF4- stabilized Fe protein:MoFe protein complex. Both nifI1 and nifI2 are required for regulation in vivo Methanococcus maripaludis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.18.6.1 Fe2+ as part of the Fe protein in the MoFe protein, [4Fe-4S] clusters Methanococcus maripaludis
1.19.6.1 Fe2+ as part of the Fe protein in the MoFe protein, [4Fe-4S] clusters Methanococcus maripaludis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.6.1 additional information Methanococcus maripaludis both nifI1 and nifI2 are required for regulation in vivo ?
-
?
1.18.6.1 reduced ferredoxin + H+ + N2 + ATP + H2O Methanococcus maripaludis
-
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
?
1.19.6.1 6 reduced flavodoxin + N2 + 6 H2O + 6 ATP Methanococcus maripaludis
-
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
?
1.19.6.1 additional information Methanococcus maripaludis both nifI1 and nifI2 are required for regulation in vivo ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.18.6.1 Methanococcus maripaludis
-
-
-
1.19.6.1 Methanococcus maripaludis
-
-
-

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 reaction mechanism, overview Methanococcus maripaludis
1.19.6.1 4 reduced flavodoxin + 2 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized flavodoxin + 2 NH4+ + H2 + 16 ADP + 16 phosphate reaction mechanism, overview Methanococcus maripaludis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.6.1 additional information both nifI1 and nifI2 are required for regulation in vivo Methanococcus maripaludis ?
-
?
1.18.6.1 additional information the enzyme performs acetylene reduction Methanococcus maripaludis ?
-
?
1.18.6.1 reduced ferredoxin + H+ + N2 + ATP + H2O
-
Methanococcus maripaludis oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
?
1.19.6.1 6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
-
Methanococcus maripaludis 6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
?
1.19.6.1 additional information both nifI1 and nifI2 are required for regulation in vivo Methanococcus maripaludis ?
-
?
1.19.6.1 additional information the enzyme performs acetylene reduction Methanococcus maripaludis ?
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.18.6.1 7.5
-
assay at, acetylene reduction Methanococcus maripaludis
1.19.6.1 7.5
-
assay at, acetylene reduction Methanococcus maripaludis

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.6.1 ATP
-
Methanococcus maripaludis
1.18.6.1 FeMo cofactor
-
Methanococcus maripaludis
1.19.6.1 ATP
-
Methanococcus maripaludis
1.19.6.1 FeMo cofactor
-
Methanococcus maripaludis