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

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

Abstract

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
Volume6
Issue number3
DOIs
StatePublished - Sep 17 2001

Keywords

  • Lipoxygenase
  • Model compounds
  • Nonheme iron
  • Peroxo complexes

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