We will discuss the preparation of [FeFe] hydrogenase mimetic metallopolymers via atom tranfer radical polymerization to enhance the electrocatalytic activity of these materials for H2 production. Transition metal-sulfides, both as clusters and as materials, are known to catalyze a wide variety of chemical transformations. In biology iron-sulfur clusters play key roles in electron transfer processes and redox activation of small molecules. As one important example, the butterfly [2Fe-2S] clusters in the active sites of [FeFe]-hydrogenase enzymes have been shown to reduce protons to molecular hydrogen at rates on the order of 10,000 molecules of hydrogen per enzyme per second. However, the electrocatalytic lifetime of these materials are often very short due to decomposition of the [2Fe-2S] complex under HER conditions. To alleve this limitation, we have pursued the preparation of metallopolymers from the functional [2Fe-2S] clusters via ATRP of various vinylic comonomers to introduce well-defined (co)polymers to site isolate the complex during electrocatalysis. We will discuss in this presentation this new synthetic approach along as well as the critical role of controlled radical polymerizations and ATRP to afford next generation catalytic systems for H2 production via water splitting.

Artificial enzymes via ATRP from [2Fe-2S] metallopolymers for H2 production via water splitting

2019 Spring National Meeting

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