Improved Electro- and Photocatalytic Water Reduction by Confined Cobalt Catalysts in Streptavidin
Improved Electro- and Photocatalytic Water Reduction by Confined Cobalt Catalysts in Streptavidin
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DOI：
10.1021/acscatal.8b04981
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发表时间：
2019-07-01
期刊：
影响因子：
12.9
通讯作者：
Lloret-Fillol, Julio
中科院分区：
文献类型：
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作者：
Call, Arnau;Casadevall, Carla;Lloret-Fillol, Julio
将衍生自三氮杂环壬烷支架的生物素化的氨基吡啶钴络合物并入链霉亲和素蛋白中导致形成用于将水还原成氢的人工金属酶。合成的人工金属酶具有较低的过电位（在半峰高达100 mV）和更高的光催化析氢活性（高达14-和10倍增加TOF和TON，分别在pH 12.5）比自由的生物素化的钴络合物。1H-1-NMR，EPR和XAS突出了金属配合物的存在下，超分子连接到链霉亲和素。pH依赖的催化研究和分子动力学（MD）模拟表明，催化活性的增加可以诱导的蛋白质残基定位接近金属中心。这些发现说明了生物素-链霉亲和素技术生产用于光催化和电催化析氢反应的人工金属蛋白的能力。
Incorporation of biotinylated aminopyridine cobalt complexes derived from the triazacyclononane scaffold into the streptavidin protein leads to formation of artificial metalloenzymes for water reduction to hydrogen. The synthesized artificial metalloenzymes have lower overpotential (at the half-peak up to 100 mV) and higher photocatalytic hydrogen evolution activity (up to 14- and 10-fold increase in TOF and TON, respectively, at pH 12.5) than the free biotinylated cobalt complexes. H-1-NMR, EPR and XAS highlight the presence of the metal complexes upon supramolecular attachment to the streptavidin. pH-dependent catalytic studies and molecular dynamics (MD) simulations suggest that the increase in the catalytic activity could be induced by the protein residues positioned close to the metal centers. These findings illustrate the ability of the biotin-streptavidin technology to produce artificial metalloproteins for photo- and electrocatalytic hydrogen evolution reaction.