Structural Models of the [Fe4S4] Clusters of Homologous Nitrogenase Fe Proteins
Structural Models of the [Fe4S4] Clusters of Homologous Nitrogenase Fe Proteins
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DOI：
10.1021/ic200636k
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发表时间：
2011-08-01
影响因子：
4.6
通讯作者：
Ribbe, Markus W.
中科院分区：
文献类型：
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作者：
Blank, Michael A.;Lee, Chi Chung;Ribbe, Markus W.
钼（Mo）-、钒（V）-和铁（Fe）-固氮酶的铁（Fe）蛋白分别由nifH、vnfH和anfH编码。虽然nifH编码的Fe蛋白近年来已被广泛研究，但关于vnfH和anfH编码的Fe蛋白的性质的信息仍然很少。在这里，我们提出了一个组合的生化，电子顺磁共振（EPR）和X射线吸收光谱（XAS）分析的[Fe 4S 4]集群的NifH，VnfH，和AnfH的棕色固氮菌。我们的数据表明，所有三个Fe蛋白质包含[Fe 4S 4]簇非常相似的光谱和几何结构特性，虽然NifH不同更多的VnfH和AnfH的电子结构。这些意见有一个有趣的影响的理论的合理序列的进化固氮酶铁蛋白。更重要的是，本文提出的结果提供了一个平台，为未来的调查的差异活动的三个铁蛋白在固氮酶的生物合成和催化。
The iron (Fe) proteins of molybdenum (Mo)-, vanadium (V)-, and iron (Fe)-only nitrogenases are encoded by nifH, vnfH, and anfH, respectively. While the nifH-encoded Fe protein has been extensively studied over recent years, information regarding the properties of the vnfH- and anfH-encoded Fe proteins has remained scarce. Here, we present a combined biochemical, electron paramagnetic resonance (EPR) and X-ray absorption spectroscopy (XAS) analysis of the [Fe4S4] clusters of NifH, VnfH, and AnfH of Azotobacter vinelandii. Our data show that all three Fe proteins contain [Fe4S4] clusters of very similar spectroscopic and geometric structural properties, although NifH differs more from VnfH and AnfH with regard to the electronic structure. These observations have an interesting impact on the theory of the plausible sequence of evolution of nitrogenase Fe proteins. More importantly, the results presented herein provide a platform for future investigations of the differential activities of the three Fe proteins in nitrogenase biosynthesis and catalysis.