Investigating the role of the strong field ligands in [FeFe] hydrogenase: spectroscopic and functional characterization of a semi-synthetic mono-cyanide active site,Chemical Science

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Investigating the role of the strong field ligands in [FeFe] hydrogenase: spectroscopic and functional characterization of a semi-synthetic mono-cyanide active site
Chemical Science ( IF 7.6 ) Pub Date : 2022-08-11 , DOI: 10.1039/d2sc02271k
Marco Lorenzi ₁ , Joe Gellett ₂ , Afridi Zamader _{1,

3} , Moritz Senger ₄ , Zehui Duan ₂ , Patricia Rodríguez-Maciá ₂ , Gustav Berggren ₁

Affiliation

Artificial maturation of hydrogenases provides a path towards generating new semi-synthetic enzymes with novel catalytic properties. Here enzymes featuring a synthetic asymmetric mono-cyanide cofactor have been prepared using two different hydrogenase scaffolds. Their structure and reactivity was investigated in order to elucidate the design rationale behind the native di-cyanide cofactor, and by extension the second coordination sphere of the active-site pocket. Surprisingly, the choice of host enzyme was found to have a dramatic impact on reactivity. Moreover, the study shows that synthetic manipulations of the active-site can significantly increase inhibitor tolerance, as compared to native [FeFe] hydrogenase, while retaining the enzyme's native capacity for reversible catalysis.

中文翻译：

研究强场配体在 [FeFe] 氢化酶中的作用：半合成单氰化物活性位点的光谱和功能表征

氢化酶的人工成熟提供了产生具有新颖催化特性的新型半合成酶的途径。这里使用两种不同的氢化酶支架制备了具有合成不对称单氰化物辅因子的酶。研究了它们的结构和反应性，以阐明天然二氰化物辅因子背后的设计原理，并通过扩展活性位点袋的第二配位球。令人惊讶的是，发现宿主酶的选择对反应性具有显着影响。此外，研究表明，与天然 [FeFe] 氢化酶相比，活性位点的合成操作可以显着提高抑制剂耐受性，同时保留酶的天然可逆催化能力。

更新日期：2022-08-11

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