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

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JBIC Journal of Biological Inorganic Chemistry Aims and scope Submit manuscript

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.

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Authors and Affiliations

  1. Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, 207 Pleasant St. S.E., Minneapolis, MN 55455, USA, , , , ,

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

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  1. Jinheung Kim
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  2. Yan Zang
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  3. Miquel Costas
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  4. Roger G. Harrison
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  5. Elizabeth C. Wilkinson
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  6. Lawrence Que Jr
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Kim, J., Zang, Y., Costas, M. et al. A nonheme iron(II) complex that models the redox cycle of lipoxygenase. J. Biol. Inorg. Chem. 6, 275–284 (2001). https://doi.org/10.1007/s007750000198

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  • DOI: https://doi.org/10.1007/s007750000198

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