Polyunsaturated fatty acid metabolism is governed primarily by two enzymes,
prostaglandin H synthase and lipoxygenase. The crystal structure of the me
tastable product-oxidized purple form of soybean lipoxygenase-3 was determi
ned at 2.0 Angstrom resolution. The data reveal that the chromophore corres
ponds to an iron-peroxide complex, a potential intermediate in the catalyze
d reaction. A significant alteration of the iron site accompanies the forma
tion 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 ster
eoselectivity.