Mode of substrate carboxyl binding to the [4Fe-4S]+ cluster of reduced aconitase as studied by 17O and 13C electron-nuclear double resonance spectroscopy.

Lignende værker

• Mössbauer and EPR studies of activated aconitase: development of a localized valence state at a subsite of the [4Fe-4S] cluster on binding of citrate.
  af: Emptage, M H, et al.
  Udgivet: (1983)
• Mössbauer study of the inactive Fe3S4 and Fe3Se4 and the active Fe4Se4 forms of beef heart aconitase.
  af: Surerus, K K, et al.
  Udgivet: (1989)
• The reaction of fluorocitrate with aconitase and the crystal structure of the enzyme-inhibitor complex
  af: Lauble, H., et al.
  Udgivet: (1996)
• Magnetic circular dichroism study of the selenium-substituted form (Fe3Se4) of bovine heart aconitase.
  af: Breton, J L, et al.
  Udgivet: (1995)
• Mössbauer studies of beef heart aconitase: evidence for facile interconversions of iron-sulfur clusters.
  af: Kent, T A, et al.
  Udgivet: (1982)