The lipoate synthase from Escherichia coli is an iron-sulfur protein

被引：50

作者：

Ollagnier-de Choudens, S ^{[1
]}

Fontecave, M ^{[1
]}

机构：

[1] Univ Grenoble 1, CNRS, CEA, DBMSCB,Lab Chim & Biochim,Ctr Redox Biol, F-38054 Grenoble 09, France

来源：

FEBS LETTERS | 1999年 / 453卷 / 1-2期

关键词：

lipoate synthase; iron-sulfur protein; C-S bond formation; electron paramagnetic resonance;

D O I：

10.1016/S0014-5793(99)00694-8

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：

Lipoate synthase catalyzes the last step of the biosynthesis of lipoic acid in microorganisms and plants. The protein isolated from an overexpressing Escherichia coli strain was purified from inclusion bodies. Spectroscopic (UV-visible and electron paramagnetic resonance) properties of the reconstituted protein demonstrate the presence of a (2Fe-2S) center per protein. As observed in biotin synthase, these clusters are converted to (4Fe-4S) centers during reduction under anaerobic conditions, The possible involvement of the cluster in the insertion of sulfur atoms into the octanoic acid backbone is discussed. (C) 1999 Federation of European Biochemical Societies.

引用

页码：25 / 28

页数：4

共 21 条

[1] SEMI-MICRO METHODS FOR ANALYSIS OF LABILE SULFIDE AND OF LABILE SULFIDE PLUS SULFANE SULFUR IN UNUSUALLY STABLE IRON SULFUR PROTEINS [J].