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Literature summary for 1.18.6.1 extracted from

  • Keable, S.; Vertemara, J.; Zadvornyy, O.; Eilers, B.; Danyal, K.; Rasmussen, A.; De Gioia, L.; Zampella, G.; Seefeldt, L.; Peters, J.
    Structural characterization of the nitrogenase molybdenum-iron protein with the substrate acetylene trapped near the active site (2018), J. Inorg. Biochem., 180, 129-134 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant enzyme R96Q bound to acetylene, capillary batch diffusion method, using 30% (w/v) polyethylene glycol 4000, 0.1 M Tris (pH 8.0), 0.17 M Na2MoO4, and 0.001 M sodium dithionite Azotobacter vinelandii

Protein Variants

Protein Variants Comment Organism
R96Q the substitution of Arg to Gln at position 96 makes the active site pocket environment more hydrophobic than that of the native enzyme Azotobacter vinelandii

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii P07328 and P07329 alpha and beta chains
-
Azotobacter vinelandii DJ1264 P07328 and P07329 alpha and beta chains
-

Synonyms

Synonyms Comment Organism
nitrogenase MoFe protein
-
Azotobacter vinelandii
nitrogenase molybdenum-iron protein
-
Azotobacter vinelandii

Cofactor

Cofactor Comment Organism Structure
iron-molybdenum cofactor the enzyme contains 2 [8Fe-7S] P clusters and 2 active site [7Fe-9S-C-Mo-homocitrate] iron-molybdenum cofactors Azotobacter vinelandii