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首页> 外文期刊>Biochemistry >Frataxin Accelerates [2Fe-2S] Cluster Formation on the Human Fe-S Assembly Complex
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Frataxin Accelerates [2Fe-2S] Cluster Formation on the Human Fe-S Assembly Complex

机译：Frataxin促进人类Fe-S组装复合体上的[2Fe-2S]团簇形成。

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Iron-sulfur (Fe-S) clusters function as protein cofactors for a wide variety of critical cellular reactions. In human mitochondria, a core Fe-S assembly complex [called SDUF and composed of NFS1, ISD11, ISCU2, and frataxin (FXN) proteins] synthesizes Fe-S clusters from iron, cysteine sulfur, and reducing equivalents and then transfers these intact clusters to target proteins. In vitro assays have relied on reducing the complexity of thiS complicated Fe-S assembly process by using, surrogate electron donor molecules and monitoring simplified reactions. Recent studies have concluded that FXN promotes the synthesis of [4Fe-4S] clusters on the mammalian Fe-S assembly complex. Here the kinetics of Fe-S synthesis reactions were determined using different electron donation systems and by monitoring the products with circular dichroism and absorbance spectroscopies. We discovered that common surrogate electron donor molecules intercepted Fe-S cluster intermediates and formed high-molecular Weight species (HMWS). The HMWS are associated with iron, sulfide, and thiol-containing proteins and have properties of a heterogeneous solubilized mineral with spectroscopic properties remarkably reminiscent of those of [4Fe-4S] clusters. In contrast, reactions using physiological reagents revealed that FXN accelerates the formation of [2Fe-2S] clusters rather than [4Fe-4S] clusters as previously reported. In the preceding paper [Fox, N. G., et al. (2015) Biochemistry 54, DOT: 10.1021/bi5014485], [2Fe-2S] intermediates on the SDUF complex were shown to readily transfer to uncomplexed ISCU2 or apo acceptor proteins, depending on the reaction conditions. Our results indicate that FXN accelerates a rate-limiting sulfur transfer step in the synthesis of [2Fe-2S] clusters on the human Fe-S assembly complex.
机译：铁-硫（Fe-S）簇可作为多种关键细胞反应的蛋白质辅因子。在人类线粒体中，核心的Fe-S组装复合物（称为SDUF，由NFS1，ISD11，ISCU2和frataxin（FXN）蛋白组成）从铁，半胱氨酸硫和还原的等价物合成Fe-S簇，然后转移这些完整簇靶向蛋白质。体外测定依赖于通过使用，替代电子给体分子并监测简化的反应来降低这种复杂的Fe-S组装过程的复杂性。最近的研究得出结论，FXN促进了哺乳动物Fe-S组装复合物上[4Fe-4S]团簇的合成。在这里，Fe-S合成反应的动力学是通过使用不同的电子给体系统并通过圆二色性和吸收光谱法监测产物来确定的。我们发现常见的替代电子给体分子拦截Fe-S簇中间体并形成高分子量物种（HMWS）。 HMWS与含铁，硫化物和硫醇的蛋白质有关，并具有异质可溶矿物的特性，其光谱学特性明显让人联想到[4Fe-4S]团簇。相反，使用生理试剂的反应表明，FXN会加速[2Fe-2S]团簇的形成，而不是先前报道的[4Fe-4S]团簇。在之前的论文中[Fox，N. G.，et al。 （2015）Biochemistry 54，DOT：10.1021 / bi5014485]，SDUF复合物上的[2Fe-2S]中间体根据反应条件容易转移至未复合的ISCU2或载脂蛋白受体蛋白。我们的结果表明，FXN加速了人类Fe-S组装复合物上[2Fe-2S]团簇的合成中的限速硫转移步骤。

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