在具有生理还原剂 H 的天然 [FeFe]-氢化酶中，氢化物状态的积累支持其催化相关性。

Department of Chemistry, Physical Chemistry, Uppsala University, 75120 Uppsala, Sweden.

Department of Chemistry, Molecular Biomimetics, Uppsala University, 75120 Uppsala, Sweden.

Chem Commun (Camb). 2022 Jun 23;58(51):7184-7187. doi: 10.1039/d2cc00671e.

Small molecules in solution may interfere with mechanistic investigations, as they can affect the stability of catalytic states and produce off-cycle states that can be mistaken for catalytically relevant species. Here we show that the hydride state (H), a proposed central intermediate in the catalytic cycle of [FeFe]-hydrogenase, can be formed in wild-type [FeFe]-hydrogenases treated with H in absence of other, non-biological, reductants. Moreover, we reveal a new state with unclear role in catalysis induced by common low pH buffers.

溶液中的小分子可能会干扰机制研究，因为它们会影响催化态的稳定性，并产生可能被误认为与催化相关的非循环态。在这里，我们表明，在没有其他非生物还原剂的情况下，用 H 处理野生型[FeFe]-氢化酶可以形成氢化酶催化循环中的提议的中心中间体（H）。此外，我们还揭示了由常见的低 pH 缓冲液诱导的、在催化中作用不明的新状态。