The oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-cluster
The oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-cluster
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DOI：
10.1038/nchem.1892
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发表时间：
2014-04-01
期刊：
影响因子：
21.8
通讯作者：
Leger, Christophe
中科院分区：
文献类型：
--
作者：
Fourmond, Vincent;Greco, Claudio;Leger, Christophe
自然是设计催化剂的宝贵灵感来源，各种方法被用来阐明氢化酶的机制，氧化或产生H-2的酶。在FeFe氢化酶中，H-2氧化发生在H-簇上，催化作用涉及H-2结合在铁中心的空配位位点上。在这里，我们表明，这种酶的可逆的氧化失活的结果从H-2的结合，通常是由固有的CO配体阻止的协调位置。活性铁中心周围配位球的这种灵活性赋予酶在氧化条件下避免有害反应的能力，包括暴露于O-2。自然体系中二铁簇合物的多功能化学性质可能会激发新型合成催化剂的设计，用于H-2氧化。
Nature is a valuable source of inspiration in the design of catalysts, and various approaches are used to elucidate the mechanism of hydrogenases, the enzymes that oxidize or produce H-2. In FeFe hydrogenases, H-2 oxidation occurs at the H-cluster, and catalysis involves H-2 binding on the vacant coordination site of an iron centre. Here, we show that the reversible oxidative inactivation of this enzyme results from the binding of H-2 to coordination positions that are normally blocked by intrinsic CO ligands. This flexibility of the coordination sphere around the reactive iron centre confers on the enzyme the ability to avoid harmful reactions under oxidizing conditions, including exposure to O-2. The versatile chemistry of the diiron cluster in the natural system might inspire the design of novel synthetic catalysts for H-2 oxidation.