Ruthenium models of the [FeFe]-hydrogenase active site: seeking the terminal hydride

The [FeFe]-hydrogenase enzymes are some of the best catalysts know for generating hydrogen. We have an ongoing programme to understand how their chemistry works, and to replicate the core 'active site' of the enzyme. Recent literature reports have shown that replacing iron by ruthenium in the enzyme can allow isolation of a long sought 'terminal hydride' intermediate. Here, we will seek evidence that this intriguing compound can be seen by muon spectroscopy.

[FeFe]-氢化酶（[FeFe]-hydrogenase）是目前已知性能最优的产氢催化剂之一。本团队正推进一项持续开展的研究计划，旨在阐明其催化反应机制，并复刻该酶的核心‘活性位点’。近期文献报道显示，在该酶中用钌替换铁原子后，可分离得到长期以来备受追寻的‘端基氢化物中间体’。本研究将通过μ子光谱学（muon spectroscopy）探寻可观测到该极具研究价值的化合物的实验证据。