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Literature summary extracted from

  • Barney, B.M.; Laryukhin, M.; Igarashi, R.Y.; Lee, H.I.; Dos Santos, P.C.; Yang, T.C.; Hoffman, B.M.; Dean, D.R.; Seefeldt, L.C.
    Trapping a hydrazine reduction intermediate on the nitrogenase active site (2005), Biochemistry, 44, 8030-8037.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.18.6.1 V70A/H195Q mutant used for freeze-trapping the FeMo-cofactor in a S=1/2 state with hydrazine as substrate. The trapped intermediate incorporates a hydrazine-derived species bound to the FeMo-cofactor. EPR and ENDOR analysis of the adduct Azotobacter vinelandii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.18.6.1 Iron freeze-trapping the FeMo-cofactor in a S=1/2 state with hydrazine as substrate in mutant V70A/H195Q. The trapped intermediate incorporates a hydrazine-derived species bound to the FeMo-cofactor Azotobacter vinelandii
1.18.6.1 Molybdenum freeze-trapping the FeMo-cofactor in a S=1/2 state with hydrazine as substrate in mutant V70A/H195Q. The trapped intermediate incorporates a hydrazine-derived species bound to the FeMo-cofactor Azotobacter vinelandii

Organism

EC Number Organism UniProt Comment Textmining
1.18.6.1 Azotobacter vinelandii
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