MgATP-induced conformational changes in the iron protein from Azotobacter vinelandii, as studied by small-angle x-ray scattering.

This publication has 19 references indexed in Scilit:

• Crystallographic Structure of the Nitrogenase Iron Protein from Azotobacter vinelandii
  Science, 1992
• Electrochemical titration of the S = 3/2 and S = ½ states of the iron protein of nitrogenase
  FEBS Letters, 1986
• Identification of possible adenine nucleotide‐binding sites in nitrogenase Fe‐ and MoFe‐proteins by amino acid sequence comparison
  FEBS Letters, 1984
• Electron‐Paramagnetic‐Resonance Studies on Nitrogenase
  European Journal of Biochemistry, 1974
• Effect of magnesium adenosine 5'-triphosphate on the accessibility of the iron of clostridial azoferredoxin, a component of nitrogenase
  Biochemistry, 1974
• Studies by electron paramagnetic resonance on the catalytic mechanism of nitrogenase of Klebsiella pneumoniae
  Biochemical Journal, 1973
• An effect of magnesium adenosine 5′-triphosphate on the structure of azoferredoxin from Clostridiumpasteurianum
  Biochemical and Biophysical Research Communications, 1973
• The binding of ATP and ADP by nitrogenase components from Clostridium pasteurianum
  Biochimica et Biophysica Acta (BBA) - Enzymology, 1973
• Electron Paramagnetic Resonance of Nitrogenase and Nitrogenase Components from Clostridium pasteurianum W5 and Azotobacter vinelandii OP
  Proceedings of the National Academy of Sciences, 1972
• On the structure and function of nitrogenase from Clostridium pasteurianum W5
  Biochemical and Biophysical Research Communications, 1972