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Literature summary 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)

EC Number Cloned (Comment) Organism
1.18.6.1
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Azotobacter vinelandii

Protein Variants

EC Number Protein Variants Comment Organism
1.18.6.1 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
1.18.6.1 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

EC Number Organism UniProt Comment Textmining
1.18.6.1 Azotobacter vinelandii
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-
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1.18.6.1 Azotobacter vinelandii DJ995
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-
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.6.1 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 ?
-
?
1.18.6.1 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 ?
-
?