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.

引用

页码：431 / 459

页数：29

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