Literature summary 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 .

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.18.6.1	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

EC Number	Protein Variants	Comment	Organism
1.18.6.1	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

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

Synonyms

EC Number	Synonyms	Comment	Organism
1.18.6.1	nitrogenase MoFe protein	-	Azotobacter vinelandii
1.18.6.1	nitrogenase molybdenum-iron protein	-	Azotobacter vinelandii

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.18.6.1	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

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Release 2023.1 (January 2023)