Ruhr-Universität Bochum, Fakultät für Biologie und Biotechnologie, Lehrstuhl für Biochemie der Pflanzen, AG Photobiotechnologie, 44801 Bochum, Germany.
Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany.
Nat Chem Biol. 2013 Oct;9(10):607-609. doi: 10.1038/nchembio.1311. Epub 2013 Aug 11.
Hydrogenases catalyze the formation of hydrogen. The cofactor ('H-cluster') of [FeFe]-hydrogenases consists of a [4Fe-4S] cluster bridged to a unique [2Fe] subcluster whose biosynthesis in vivo requires hydrogenase-specific maturases. Here we show that a chemical mimic of the [2Fe] subcluster can reconstitute apo-hydrogenase to full activity, independent of helper proteins. The assembled H-cluster is virtually indistinguishable from the native cofactor. This procedure will be a powerful tool for developing new artificial H₂-producing catalysts.
氢化酶催化氢气的形成。[FeFe]-氢化酶的辅因子('H- 簇')由一个[4Fe-4S] 簇桥接到一个独特的[2Fe]亚簇组成,其在体内的生物合成需要氢化酶特异性成熟酶。在这里,我们表明[2Fe]亚簇的化学模拟物可以在没有辅助蛋白的情况下重新组装成具有完整活性的脱辅基氢化酶。组装的 H- 簇与天然辅因子几乎无法区分。该程序将成为开发新型人工 H₂ 产生催化剂的有力工具。