Lipoxygenases: Structural principles and spectroscopy

被引：81
作者：
Gaffney, BJ
机构：
[1] Chemistry Department, Johns Hopkins University, Baltimore
来源：
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 1996年 / 25卷
关键词：
lipoxygenase; X-ray structure; pi-helix; non-heme iron; metalloprotein; c-terminus; EMR; EPR; XAS; NIR CD; MCD;
D O I：
10.1146/annurev.bb.25.060196.002243
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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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收藏
页码：431 / 459
页数：29
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