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Literature summary extracted from

  • Petersen, J.; Mitchell, C.J.; Fisher, K.; Lowe, D.J.
    Structural basis for VO(2+)-inhibition of nitrogenase activity: (B) pH-sensitive inner-sphere rearrangements in the 1H-environment of the metal coordination site of the nitrogenase Fe-protein identified by ENDOR spectroscopy (2008), J. Biol. Inorg. Chem., 13, 637-650.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.18.6.1 Fe2+ different VO2+-nucleotide coordination environments exist for the Fe-protein Kp2 that depend on pH and are distinguishable by EPR spectroscopy, Kp2 structure, overview Klebsiella pneumoniae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.6.1 reduced ferredoxin + H+ + N2 + ATP Klebsiella pneumoniae
-
 oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.18.6.1 Klebsiella pneumoniae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.6.1 reduced ferredoxin + H+ + N2 + ATP
-
 Klebsiella pneumoniae oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
1.18.6.1 More Kp2 structure analysis bound to Vo2+ and at different pH, overview Klebsiella pneumoniae

Synonyms

EC Number Synonyms Comment Organism
1.18.6.1 Kp2
-
 Klebsiella pneumoniae
1.18.6.1 nitrogenase Fe-protein
-
 Klebsiella pneumoniae
1.18.6.1 nitrogenase iron-protein
-
 Klebsiella pneumoniae

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.6.1 ATP
-
 Klebsiella pneumoniae