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Literature summary for 1.18.6.1 extracted from

  • Lukoyanov, D.; Yang, Z.Y.; Barney, B.M.; Dean, D.R.; Seefeldt, L.C.; Hoffman, B.M.
    Unification of reaction pathway and kinetic scheme for N2 reduction catalyzed by nitrogenase (2012), Proc. Natl. Acad. Sci. USA, 109, 5583-5587.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
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Azotobacter vinelandii DJ1260
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diazene + ? modified nitrogenase variant V70A/H195Q under turnover conditions using diazene, methyldiazene, or hydrazine as substrate traps a common S = 1/2 intermediate. Such samples also contain a common intermediate with FeMo-co in an integer-spin state having a ground-state non-Kramers doublet. This species, designated H, has NH2 bound to FeMo-co and corresponds to the penultimate intermediate of N2 hydrogenation, the state formed after the accumulation of seven electrons/protons and the release of the first NH3, the S = 1/2 species corresponds to the final intermediate in N2 reduction, the state formed after accumulation of eight electrons/protons, with NH3 still bound to FeMo-co prior to release and regeneration of resting-state FeMo-co Azotobacter vinelandii ?
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?
diazene + ? modified nitrogenase variant V70A/H195Q under turnover conditions using diazene, methyldiazene, or hydrazine as substrate traps a common S = 1/2 intermediate. Such samples also contain a common intermediate with FeMo-co in an integer-spin state having a ground-state non-Kramers doublet. This species, designated H, has NH2 bound to FeMo-co and corresponds to the penultimate intermediate of N2 hydrogenation, the state formed after the accumulation of seven electrons/protons and the release of the first NH3, the S = 1/2 species corresponds to the final intermediate in N2 reduction, the state formed after accumulation of eight electrons/protons, with NH3 still bound to FeMo-co prior to release and regeneration of resting-state FeMo-co Azotobacter vinelandii DJ1260 ?
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?
hydrazine + ?
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Azotobacter vinelandii ?
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?
hydrazine + ?
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Azotobacter vinelandii DJ1260 ?
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?
methyldiazene + ?
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Azotobacter vinelandii ?
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?
methyldiazene + ?
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Azotobacter vinelandii DJ1260 ?
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?
additional information draft mechanism for N2 reduction by nitrogenase. Diazene binds to the one-electron reduced intermediate with the release of H2, and enters the N2 pathway as the final form of the four-electron reduced state. In contrast, N2H4 instead binds to one-electron reduced intermediate, as is proposed for another two-electron substrate, C2H2, and joins the N2 pathway at a stage corresponding to the seven-electron reduced intermediate in the N2 reduction scheme Azotobacter vinelandii ?
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additional information draft mechanism for N2 reduction by nitrogenase. Diazene binds to the one-electron reduced intermediate with the release of H2, and enters the N2 pathway as the final form of the four-electron reduced state. In contrast, N2H4 instead binds to one-electron reduced intermediate, as is proposed for another two-electron substrate, C2H2, and joins the N2 pathway at a stage corresponding to the seven-electron reduced intermediate in the N2 reduction scheme Azotobacter vinelandii DJ1260 ?
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