A nonheme iron(II) complex that models the redox cycle of lipoxygenase

Jinheung Kim, Yan Zang, Miquel Costas, Roger G. Harrison, Elizabeth C. Wilkinson, Lawrence Que

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The air-stable complex [Fe(6-Me3-TPA) (O2CAr)]+ [1; 6-Me3-TPA=tris(6-methyl-2-pyridylmethyl)amine] has been synthesized as a model for the iron(II) site of lipoxygenase. This iron(II) complex reacts with 0.5 equiv ROOH to form a yellow species, which has been formulated as [FeIII(OH)(6-Me3-TPA) (O2CAr)]+ (2) by electrospray mass spectrometry. Addition of more ROOH converts 2 into a purple species, which is characterized by electrospray ionization mass spectrometry and resonance Raman spectroscopy as [FeIII(OOR)(6-Me3-TPA)(O2CAr)]+. The purple species is metastable and decomposes via Fe-O bond homolysis to regenerate the starting iron(II) complex. These metal-centered transformations parallel the changes observed for lipoxygenase in its reaction with its product hydroperoxide.

Original languageEnglish (US)
Pages (from-to)275-284
Number of pages10
JournalJournal of Biological Inorganic Chemistry
Issue number3
StatePublished - 2001

Bibliographical note

Funding Information:
Acknowledgements This work has been supported by a grant from the National Institutes of Health (GM-33162 to L.Q.) and a postdoctoral fellowship from Fundacio “La Caixa” (to M.C.).


  • Lipoxygenase
  • Model compounds
  • Nonheme iron
  • Peroxo complexes


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