Recent Advances in the Chemical Synthesis of Nitrogenase Model Clusters
Recent Advances in the Chemical Synthesis of Nitrogenase Model Clusters
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DOI：
10.1007/430_2018_26
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发表时间：
2018
影响因子：
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通讯作者：
Kazuki Tanifuji;Y. Ohki
中科院分区：
文献类型：
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作者：
Kazuki Tanifuji;Y. Ohki
唯一能够固定氮的酶，固氮酶，在环境条件下将惰性的和丰富的氮素(N2)还原为生物可利用的氨(NH3)。研究最多的变体MoFe固氮酶使用三种金属辅因子：电子载体组分(Fe蛋白质)中的[Fe4S4]簇，以及催化组分(MoFe蛋白质)中的[Fe8S7](P-簇)和[MoFe7S9C](M-簇)簇。为了更好地了解这些辅因子的物理性质，人们发展了各种方法来合成模型金属硫簇合物。在这篇综述中，我们着重讨论了以下主题的最新进展：(A)全铁[Fe4S4]0团簇的合成，它是铁蛋白质中团簇的超还原状态，(B)P-团簇独特的[Fe8S7]无机核心的复制，以及(C)与M-团簇相关的金属-硫团簇的合成及其包含一个轻原子的变体。尽管M-团簇的复制仍然难以捉摸，但最近的一些进展似乎朝着满足M-团簇的关键结构特征的新的金属硫团簇的方向发展。
The only enzyme that is able to fix nitrogen, nitrogenase, reduces inert and abundant dinitrogen (N2) into bioavailable ammonia (NH3) under ambient conditions. The most investigated variant, the MoFe nitrogenase, uses three metallo-cofactors: the [Fe4S4] cluster in the electron-carrier component (Fe protein), as well as the [Fe8S7] (P-cluster) and [MoFe7S9C] (M-cluster) clusters in the catalytic component (MoFe protein). To better understand the physical properties of these cofactors, various methods have been developed for the chemical synthesis of model metal-sulfur clusters. In this review, we address the following topics with emphasis on recent developments: (a) the synthesis of all-ferrous [Fe4S4]0clusters, which are isoelectronic to thesuper-reducedstate of the cluster in the Fe protein, (b) the reproduction of the unique [Fe8S7] inorganic core of the P-cluster, and (c) the synthesis of metal-sulfur clusters relevant to the M-cluster and their variants that incorporate a light atom. Even though reproduction of the M-cluster remains elusive, some recent advances seem promising toward new classes of metal-sulfur clusters that satisfy the key structural features of the M-cluster.