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Literature summary for 1.18.6.1 extracted from

  • Danyal, K.; Dean, D.R.; Hoffman, B.M.; Seefeldt, L.C.
    Electron transfer within nitrogenase: evidence for a deficit-spending mechanism (2011), Biochemistry, 50, 9255-9263.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Azotobacter vinelandii

Protein Variants

Protein Variants Comment Organism
DELTAC153 mutation in the MoFe protein of nitrogenase. The rate of oxidation of Fe-protein F1+ to this MoFe protein variant is unchanged from the rate to the wild-type MoFe protein, providing further evidence against a gated hopping electron tansfer model Azotobacter vinelandii
S188C mutation in the MoFe protein of nitrogenase. Electron transfer to the MoFe state that contains P-cluster PN and FeMo-cofactor MN is conformationally gated in both wild-type MoFe and S188C mutant MoFe protein and the amino acid substitution S188C does not alter the conformational gate Azotobacter vinelandii

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
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Azotobacter vinelandii DJ995
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information data support a deficit-spending model of electron transfer where the first event is electron tranfer from the P-cluster to FeMo-cofactor and the second, backfill, event is fast electron tranfer from the Fe protein [4Fe-4S] cluster to the oxidized P-cluster. The first electron transfer is conformationally gated, whereas the second is not Azotobacter vinelandii ?
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?
additional information data support a deficit-spending model of electron transfer where the first event is electron tranfer from the P-cluster to FeMo-cofactor and the second, backfill, event is fast electron tranfer from the Fe protein [4Fe-4S] cluster to the oxidized P-cluster. The first electron transfer is conformationally gated, whereas the second is not Azotobacter vinelandii DJ995 ?
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?