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具有蒽骨架的单铁氢化酶的结构与功能综合模型。

Structural and functional synthetic model of mono-iron hydrogenase featuring an anthracene scaffold.

机构信息

Department of Chemistry, The University of Texas at Austin, Austin, Texas 78712, USA.

出版信息

Nat Chem. 2017 Jun;9(6):552-557. doi: 10.1038/nchem.2707. Epub 2017 Jan 23.

Abstract

Mono-iron hydrogenase was the third type of hydrogenase discovered. Its Lewis acidic iron(II) centre promotes the heterolytic cleavage of the H-H bond and this non-redox H activation distinguishes it from the well-studied dinuclear [FeFe] and [NiFe] hydrogenases. Cleavage of the H-H bond is followed by hydride transfer to the enzyme's organic substrate, HMPT, which serves as a CO 'carrier' in methanogenic pathways. Here we report a scaffold-based synthetic approach by which to model mono-iron hydrogenase using an anthracene framework, which supports a biomimetic fac-C,N,S coordination motif to an iron(II) centre. This arrangement includes the biomimetic and organometallic Fe-C σ bond, which enables bidirectional activity reminiscent of the native enzyme: the complex activates H under mild conditions, and catalyses C-H hydride abstraction plus H generation from a model substrate. Notably, neither H activation nor C-H hydride abstraction was observed in the analogous complex with a pincer-type mer-C,N,S ligation, emphasizing the importance of the fac-C,N,S-iron(II) motif in promoting enzyme-like reactivity.

摘要

单铁氢化酶是第三种被发现的氢化酶。其路易斯酸性的铁(II)中心促进 H-H 键的异裂,这种非氧化还原的 H 激活使其与研究充分的双核 [FeFe] 和 [NiFe] 氢化酶区分开来。H-H 键的断裂随后是氢化物向酶的有机底物 HMPT 的转移,HMPT 在产甲烷途径中充当 CO“载体”。在这里,我们报告了一种基于支架的合成方法,使用蒽框架来模拟单铁氢化酶,该框架支持仿生 fac-C,N,S 配位模式到铁(II)中心。这种排列包括仿生和有机金属 Fe-C σ 键,使具有类似天然酶的双向活性成为可能:该配合物在温和条件下激活 H,并从模型底物中催化 C-H 氢化物的提取和 H 的生成。值得注意的是,在具有钳式 mer-C,N,S 配位的类似配合物中未观察到 H 激活或 C-H 氢化物的提取,这强调了 fac-C,N,S-铁(II) 基序在促进酶样反应性方面的重要性。

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