4.8 Article

Three-dimensional structure of a purple lipoxygenase

Journal

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 123, Issue 44, Pages 10814-10820

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/ja011759t

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Funding

  1. NIGMS NIH HHS [GM 62140] Funding Source: Medline

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Polyunsaturated fatty acid metabolism is governed primarily by two enzymes, prostaglandin H synthase and lipoxygenase. The crystal structure of the metastable product-oxidized purple form of soybean lipoxygenase-3 was determined at 2.0 Angstrom resolution. The data reveal that the chromophore corresponds to an iron-peroxide complex, a potential intermediate in the catalyzed reaction. A significant alteration of the iron site accompanies the formation of the complex. The structure, the first for a fatty acid-lipoxygenase complex, also reveals an unexpected mode of binding, and identifies amino acid residues that may play significant roles in catalysis, regio- and stereoselectivity.

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