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Literature summary for 1.18.6.1 extracted from

  • Petersen, J.; Fisher, K.; Lowe, D.J.
    Structural basis for VO2+ inhibition of nitrogenase activity (A): 31P and 23Na interactions with the metal at the nucleotide binding site of the nitrogenase Fe protein identified by ENDOR spectroscopy (2008), J. Biol. Inorg. Chem., 13, 623-635.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
VO2+ structural basis for VO2+ inhibition of nitrogenase activity, 31P and 23Na interactions with the metal at the nucleotide binding site of the nitrogenase Fe protein identified by ENDOR spectroscopy, vanadyl hyperfine couplings of VO2+-ATP and VO2+-ADP complexes in the presence of the nitrogenase Fe protein, overview Klebsiella pneumoniae

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ nitrogenase Fe protein, the FeS cluster exhibits very little change upon MgATP binding, two bound nucleotides are believed to mediate the diverse, functionally essential structural rearrangements in the Fe protein Klebsiella pneumoniae
Mg2+ required, the FeS cluster exhibits very little change upon MgATP binding Klebsiella pneumoniae

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Klebsiella pneumoniae
-
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
More Kp2 structure analysis bound to Vo2+, ATP, and ADP, characterization of the metal-nucleotide coordination environment, overview Klebsiella pneumoniae

Synonyms

Synonyms Comment Organism
Kp2
-
Klebsiella pneumoniae
nitrogenase Fe protein
-
Klebsiella pneumoniae

Cofactor

Cofactor Comment Organism Structure
ATP the FeS cluster exhibits very little change upon MgATP binding Klebsiella pneumoniae