Lipoxygenases: structural principles and spectroscopy.
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.
Gaffney
B J
BJ
Chemistry Department, Johns Hopkins University, Baltimore, Maryland 21218-2685, USA.
D000818:Animals; D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D004578:Electron Spin Resonance Spectroscopy; D007501:Iron / Q000737:chemistry; D008084:Lipoxygenase / Q000737:chemistry*; D008958:Models, Molecular; D010940:Plant Proteins / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D010940:Plant Proteins; D007501:Iron; D008084:Lipoxygenase