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首页> 外文期刊>Applied and Environmental Microbiology >Homologous and Heterologous Overexpression in Clostridium acetobutylicum and Characterization of Purified Clostridial and Algal Fe-Only Hydrogenases with High Specific Activities
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Homologous and Heterologous Overexpression in Clostridium acetobutylicum and Characterization of Purified Clostridial and Algal Fe-Only Hydrogenases with High Specific Activities

机译：丙酮丁醇梭菌中的同源和异源过表达以及纯化的具有高比活性的梭菌和藻类纯铁氢化酶的表征

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摘要

Clostridium acetobutylicum ATCC 824 was selected for the homologous overexpression of its Fe-only hydrogenase and for the heterologous expressions of the Chlamydomonas reinhardtii and Scenedesmus obliquus HydA1 Fe-only hydrogenases. The three Strep tag II-tagged Fe-only hydrogenases were isolated with high specific activities by two-step column chromatography. The purified algal hydrogenases evolve hydrogen with rates of around 700 μmol H2 min?1 mg?1, while HydA from C. acetobutylicum (HydACa) shows the highest activity (5,522 μmol H2 min?1 mg?1) in the direction of hydrogen uptake. Further, kinetic parameters and substrate specificity were reported. An electron paramagnetic resonance (EPR) analysis of the thionin-oxidized HydACa protein indicates a characteristic rhombic EPR signal that is typical for the oxidized H cluster of Fe-only hydrogenases.
机译：选择丙酮丁醇梭菌ATCC 824是由于其仅Fe的氢化酶的同源过表达，以及莱茵衣藻和斜生场面藻HydA1仅Fe的氢化酶的异源表达。通过两步柱色谱法以高比活度分离了三种带有Strep标签II标记的仅铁的氢化酶。纯化的藻类加氢酶以约700μmolH2 min？1 mg？1的速率释放出氢气，而丙酮丁醇梭菌（HydACa）的HydA在吸氢方向上显示出最高的活性（5,522μmolH2 min？1 mg？1）。 。此外，还报道了动力学参数和底物特异性。硫蛋白氧化的HydACa蛋白的电子顺磁共振（EPR）分析表明，特征性的菱形EPR信号对于纯铁氢化酶的氧化H簇而言是典型的。

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