古老的铁硫簇组装蛋白IscA中铁结合的特性分析
Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein.
作者信息
Ding Huangen, Clark Robert J
机构信息
Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA.
出版信息
Biochem J. 2004 Apr 15;379(Pt 2):433-40. doi: 10.1042/BJ20031702.
Abstract
Iron-sulphur clusters are one of the most common types of redox centre in biology. At least six proteins (IscS, IscU, IscA, HscB, HscA and ferredoxin) have been identified as being essential for the biogenesis of iron-sulphur proteins in bacteria. It has been shown that IscS is a cysteine desulphurase that provides sulphur for iron-sulphur clusters, and that IscU is a scaffold for the IscS-mediated assembly of iron-sulphur clusters. The iron donor for iron-sulphur clusters, however, remains elusive. Here we show that IscA is an iron binding protein with an apparent iron association constant of 3.0x10(19) M(-1), and that iron-loaded IscA can provide iron for the assembly of transient iron-sulphur clusters in IscU in the presence of IscS and L-cysteine in vitro. The results suggest that IscA is capable of recruiting intracellular iron and delivering iron for iron-sulphur clusters in proteins.
摘要
铁硫簇是生物学中最常见的氧化还原中心类型之一。至少六种蛋白质（IscS、IscU、IscA、HscB、HscA和铁氧还蛋白）已被确定为细菌中铁硫蛋白生物合成所必需的。研究表明，IscS是一种半胱氨酸脱硫酶，为铁硫簇提供硫，而IscU是IscS介导的铁硫簇组装的支架。然而，铁硫簇的铁供体仍然不清楚。在这里，我们表明IscA是一种铁结合蛋白，其表观铁结合常数为3.0×10¹⁹ M⁻¹，并且在体外存在IscS和L-半胱氨酸的情况下，负载铁的IscA可以为IscU中瞬时铁硫簇的组装提供铁。结果表明，IscA能够募集细胞内的铁并为蛋白质中的铁硫簇提供铁。
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