ACONITASE, A 2-FACED PROTEIN - ENZYME AND IRON REGULATORY FACTOR

被引:227
作者
BEINERT, H [1 ]
KENNEDY, MC [1 ]
机构
[1] MED COLL WISCONSIN,BIOPHYS RES INST,MILWAUKEE,WI 53226
关键词
IRON-SULFUR PROTEIN; IRON-SULFUR CLUSTER LABILITY; IRON-SULFUR CLUSTER INTERCONVERSIONS; APO-ACONITASE;
D O I
10.1096/fasebj.7.15.8262329
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
In this brief survey, the path of development of our knowledge of the iron-sulfur enzyme aconitase [citrate(isocitrate)hydrolyase EC4.2.1.3.] is traced from its discovery in 1937. Particular emphasis is on developments in the past decade, when EPR, Mossbauer and electron nuclear double resonance spectroscopies, X-ray crystallography, and mutational analysis were applied to the problem. More recently discovered was the significant amino acid sequence identity between mitochondrial aconitase and the iron regulatory factor or iron-responsive element binding protein (IRE-BP). This has led to the realization that IRE-BP is an alternative form of cytosolic (not of mitochondrial) aconitase that is devoid of its cubane Fe-S cluster.
引用
收藏
页码:1442 / 1449
页数:8
相关论文
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