Lipoxygenases: Structural Principles and Spectroscopy

作者：Betty Jean Gaffney · 发表于：Annual Review of Biophysics and Biomolecular Structure · 年份：1996 · DOI：10.1146/annurev.bb.25.060196.002243 · 被引用次数：92 · 研究领域：Insect-Plant Interactions and Control、Synthesis and Biological Evaluation、Plant Gene Expression Analysis

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.