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Literature summary for 1.18.6.1 extracted from

  • Curatti, L.; Hernandez, J.A.; Igarashi, R.Y.; Soboh, B.; Zhao, D.; Rubio, L.M.
    In vitro synthesis of the iron-molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum, and homocitrate using purified proteins (2007), Proc. Natl. Acad. Sci. USA, 104, 17626-17631.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.18.6.1

Application

Application Comment Organism
energy production the reaction produces H2 as a by-product and is interesting for production of clean energy Azotobacter vinelandii

Protein Variants

Protein Variants Comment Organism
additional information in vitro synthesis of the iron-molybdenum cofactor of nitrogenase using purified proteins, a minimal in vitro system, containing NifB, NifEN, and NifH proteins, together with Fe2+, S2-, MoO4 2-, R-homocitrate, S-adenosyl methionine, and Mg-ATP, is sufficient for the synthesis of FeMo-co and the activation of apo-dinitrogenase under anaerobic-reducing conditions, modeling, overview Azotobacter vinelandii
V70I the mutant is suitable for analysis of reaction intermediates, since it exhibits the highest concentration of trapped H+-intermediate when turned over under Ar Azotobacter vinelandii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic analysis, overview Azotobacter vinelandii

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ part of the iron-molybdenum and molybdenum-iron cofactors Azotobacter vinelandii
Mg2+
-
 Azotobacter vinelandii
Molybdenum part of the iron-molybdenum and molybdenum-iron cofactors Azotobacter vinelandii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N2 + 8 e- + 16 ATP + 8 H+ Azotobacter vinelandii the enzyme is responsible for biological nitrogen fixation, the conversion of atmospheric N2 to NH3 2 NH3 + H2 + 16 ADP + 16 phosphate
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 ?

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
-
-
Azotobacter vinelandii
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 recombinant strain DJ1373 expressing mutant V70I
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Reaction

Reaction Comment Organism Reaction ID
4 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate reaction mechanism, determination of reaction intermediates, two-step relaxation of the nitrogenase H+/H+ intermediate during step-annealing,both steps show large solvent kinetic isotope effects, step A is the catalytically central state that is activated for N2 binding by the accumulation of 4 electrons, and step B accumulates 2 electrons, overview Azotobacter vinelandii
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N2 + 8 e- + 16 ATP + 8 H+
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 Azotobacter vinelandii 2 NH3 + H2 + 16 ADP + 16 phosphate
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 ?
N2 + 8 e- + 16 ATP + 8 H+ the enzyme is responsible for biological nitrogen fixation, the conversion of atmospheric N2 to NH3 Azotobacter vinelandii 2 NH3 + H2 + 16 ADP + 16 phosphate
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 ?
N2 + 8 e- + 16 ATP + 8 H+ relaxation of the nitrogenase H+/H+ intermediate during step-annealing Azotobacter vinelandii 2 NH3 + H2 + 16 ADP + 16 phosphate
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 ?

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Azotobacter vinelandii
FeMo protein FeMo-co is composed of 7Fe, 9S, Mo, R-homocitrate, and one unidentified light atom, in vitro synthesis of the iron-molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum, and homocitrate using purified Nif proteins, Several nif genes are essential for FeMo-co synthesis in vivo, e.g., nifB, nifU, nifS, nifH, nifN, nifE, and nifV, modeling, overview Azotobacter vinelandii