单分子力谱表明，Fe-N键促成了米托奈德单体中2Fe2S簇的多种断裂途径。
Single-Molecule Force Spectroscopy Reveals that the Fe-N Bond Enables Multiple Rupture Pathways of the 2Fe2S Cluster in a MitoNEET Monomer.
作者信息
Song Guobin, Ding Xuan, Liu Huaxing, Yuan Guodong, Tian Fang, Shi Shengchao, Yang Yang, Li Guoqiang, Zheng Peng
机构信息
State Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, Jiangsu 210023, P. R. China.
State Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, Jiangsu 210023, P. R. China.
出版信息
Anal Chem. 2020 Nov 3;92(21):14783-14789. doi: 10.1021/acs.analchem.0c03536. Epub 2020 Oct 13.
The mitochondrial outer membrane protein, mitoNEET (mNT), is an iron-sulfur protein containing an FeS(His)(Cys) cluster with a unique single Fe-N bond. Previous studies have shown that this Fe(III)-N(His) bond is essential for metal cluster transfer and protein function. To further understand the effect of this unique Fe-N bond on the metal cluster and protein, we used atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) to investigate the mechanical unfolding mechanism of an mNT monomer, focusing on the rupture pathway and kinetic stability of the cluster. We found that the Fe-N bond was the weakest point of the cluster, the rupture of which occurred first, and could be independent of the cluster break. Moreover, this Fe-N bond enabled a dynamic and labile iron-sulfur cluster, as multiple unfolding pathways of mNT with a unique FeS(Cys) intermediate were observed accordingly.
线粒体外膜蛋白mitoNEET（mNT）是一种铁硫蛋白，含有一个具有独特单铁氮键的FeS(His)(Cys)簇。先前的研究表明，这种Fe(III)-N(His)键对于金属簇转移和蛋白质功能至关重要。为了进一步了解这种独特的铁氮键对金属簇和蛋白质的影响，我们使用基于原子力显微镜的单分子力谱（AFM-SMFS）来研究mNT单体的机械展开机制，重点关注簇的断裂途径和动力学稳定性。我们发现铁氮键是簇的最薄弱点，它首先发生断裂，并且可能独立于簇的断裂。此外，这种铁氮键使得铁硫簇具有动态和不稳定的特性，相应地观察到mNT具有独特的FeS(Cys)中间体的多种展开途径。
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