Reduction of the active-site iron by potent inhibitors of lipoxygenases

J Biol Chem. 1991 May 5;266(13):8225-9.

Abstract

Lipoxygenases are non-heme iron dioxygenases that catalyze the oxygenation of polyunsaturated fatty acids. Using soybean lipoxygenase-1 as a model, we have shown that two classes of lipoxygenase inhibitors currently in development as potential antiinflammatory agents obtain a significant amount of their potency by reducing the lipoxygenase active-site iron from the active ferric state to the inactive ferrous state. It is not surprising that the members of the first of these classes, the 2-benzyl-1-naphthols, are reducing agents. The members of the second class, the N-alkyl-hydroxamic acids, were not anticipated to be sufficiently strong reducing agents to be oxidized by the lipoxygenase ferric center; that they are provides additional evidence for that iron having a high reduction potential. This brings to (at least) five the number of classes of lipoxygenase inhibitors that are capable of reducing the active-site ferric ion and suggests the generality of this approach in the rational design of lipoxygenase inhibitors.

MeSH terms

  • Binding Sites
  • Electron Spin Resonance Spectroscopy
  • Glycine max / enzymology
  • Hydroxamic Acids / pharmacology*
  • Iron / metabolism*
  • Lipoxygenase Inhibitors*
  • Naphthols / pharmacology*
  • Oxidation-Reduction

Substances

  • Hydroxamic Acids
  • Lipoxygenase Inhibitors
  • Naphthols
  • Iron