Institute of Chemistry, Academia Sinica – Research

含氯和氫硫基之雙鐵化合物為鐵鐵氫化酵素之氧氣穩定態的擬態

Angew. Chem. Int. Ed. 2024, 63, e202408142.
Yih-Chern Horng,* Ming-Hsi Chiang* et al.

雖然鐵鐵氫化酶對產氫和氫氧化反應有相當卓越的催化效率，這些酶對氧的耐受性不高，阻礙了將它們部署在氫氣生產裝置和燃料電池中的實際應用。最近研究發現，鐵鐵氫化酶活化中心具有ㄧ個少見的氧穩定態（H_inact），具有抗氧降解的能力。我們的研究中，[2Fe-2S]化合物鍵結末端Cl（t-Cl）或SH（t-SH）配位基，其結構與 DdHydAB 和 CbA5H 的 H_inact 態極為相似。我們研究結果為了解酶氧穩定狀態的特性以及控制失活和再活化轉化機制的關鍵因素提供了寶貴的見解。這項工作有助於推動仿生分子催化劑研究的進步以及將酵素和人工催化劑整合到產氫裝置和燃料電池應用中。

[FeFe] hydrogenases demonstrate remarkable catalytic efficiency in hydrogen evolution and oxidation processes. However, susceptibility of these enzymes to oxygen-induced degradation impedes their practical deployment in hydrogen-production devices and fuel cells. Recent investigations into the oxygen-stable (H_inact) state of the H-cluster revealed its inherent capacity to resist oxygen degradation. Herein, we present findings on terminal Cl- and SH-bound [2Fe-2S] complexes, bearing relevance to the oxygen-stable state of DdHydAB and CbA5H. The findings garnered from these investigations offer valuable insights into properties of the enzymatic O₂-stable state, and key factors governing deactivation and reactivation conversion. This work contributes to the advancement of bio-inspired molecular catalysts and the integration of enzymes and artificial catalysts into H₂-evolution devices and fuel-cell applications.