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Literature summary for 1.19.6.1 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
Search for more literature for 1.19.6.1

Inhibitors

Inhibitors Comment Organism Structure
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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Methanococcus maripaludis
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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
a

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at, acetylene reduction Methanococcus maripaludis

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Methanococcus maripaludis
FeMo cofactor
-
 Methanococcus maripaludis