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Literature summary for 1.18.6.1 extracted from

  • Yang, K.Y.; Haynes, C.A.; Spatzal, T.; Rees, D.C.; Howard, J.B.
    Turnover-dependent inactivation of the nitrogenase MoFe-protein at high pH (2014), Biochemistry, 53, 333-343 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.18.6.1

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion method, using 150 mM ACES, 75 mM Tris, 75 mM ethanolamine (pH 9.8), 17-18% (w/v) PEG 3350, 0.8 M NaCl, and 1 mM sodium dithionite Azotobacter vinelandii

Metals/Ions

Metals/Ions Comment Organism Structure
Iron contains iron Azotobacter vinelandii
Molybdenum contains molybdenum Azotobacter vinelandii

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii P07328
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylene + dithionite + H+ + ATP + H2O
-
 Azotobacter vinelandii ethylene + ?
-
 ?

Subunits

Subunits Comment Organism
? x * 233000, SDS-PAGE Azotobacter vinelandii

Synonyms

Synonyms Comment Organism
nitrogenase MoFe-protein
-
 Azotobacter vinelandii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
-
 Azotobacter vinelandii

pH Stability

pH Stability pH Stability Maximum Comment Organism
9.5
-
 the enzyme is stable when incubated at pH 9.5. At higher pH values and under turnover conditions, the enzyme is slowly inactivated. Initially the enzyme is reversibly inhibited (about 90%) for substrate reduction at pH 9.5, yet in a second, slower process, the enzyme becomes irreversibly inactivated as measured by substrate reduction at the optimal pH of 7.8. Incubation of the enzyme alone at pH 9.5 shows only minimal activity loss even after 4 h Azotobacter vinelandii