Lipoxygenases: structural principles and spectroscopy.

B J Gaffney

doi:10.1146/annurev.bb.25.060196.002243

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Lipoxygenases: structural principles and spectroscopy.

B J Gaffney

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Abstract

Lipoxygenases catalyze the formation of fatty acid hydroperoxides, products used in further biochemical reactions leading to normal and pathological cell functions. X-ray structure analysis and spectroscopy have been applied to elucidate the mechanism of lipoxygenases. Two X-ray structures of soybean lipoxygenase-1 reveal the side chains of three histidines and the COO- of the carboxy terminus as ligands to the catalytically important iron atom. The enzyme contains a novel three-turn pi-helix near the iron center. Spectroscopic studies, including electron magnetic resonance, X-ray absorption spectroscopy, infrared circular dichroism, and magnetic circular dichroism, have been applied to compare lipoxygenases from varied sources and with different substrate positional specificity.

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Animals Circular Dichroism Crystallography, X-Ray Electron Spin Resonance Spectroscopy Iron Lipoxygenase Models, Molecular Plant Proteins Protein Conformation Protein Structure, Secondary Journal Article Research Support, U.S. Gov't, P.H.S.Review

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B J Gaffney. 1996. Lipoxygenases: structural principles and spectroscopy.. https://doi.org/10.1146/annurev.bb.25.060196.002243

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