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在周转条件下,光诱导嗜热菌 Aquifex aeolicus 中耐氧膜结合[Ni-Fe]氢化酶的重新激活。

Light-induced reactivation of O2-tolerant membrane-bound [Ni-Fe] hydrogenase from the hyperthermophilic bacterium Aquifex aeolicus under turnover conditions.

机构信息

Bioénergétique et Ingénierie des Protéines, Institut de Microbiologie de la Méditerranée - CNRS-AMU, 31 Chemin Aiguier, 13009 Marseille, France.

出版信息

Phys Chem Chem Phys. 2013 Oct 21;15(39):16463-7. doi: 10.1039/c3cp52596a. Epub 2013 Sep 2.

DOI:10.1039/c3cp52596a
PMID:23999766
Abstract

We report the effect of UV-Vis light on the membrane-bound [Ni-Fe] hydrogenase from Aquifex aeolicus under turnover conditions. Using electrochemistry, we show a potential dependent light sensitivity and propose that a light-induced structural change of the [Ni-Fe] active site is related to an enhanced reactivation of the hydrogenase under illumination at high potentials.

摘要

我们报告了在周转条件下紫外可见光照对来自水生栖热菌的膜结合 [Ni-Fe] 氢化酶的影响。通过电化学方法,我们发现了一种依赖于电位的光敏感性,并提出光诱导的 [Ni-Fe] 活性中心结构变化与在高电位下光照下氢化酶的增强再激活有关。

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Light-induced reactivation of O2-tolerant membrane-bound [Ni-Fe] hydrogenase from the hyperthermophilic bacterium Aquifex aeolicus under turnover conditions.在周转条件下,光诱导嗜热菌 Aquifex aeolicus 中耐氧膜结合[Ni-Fe]氢化酶的重新激活。
Phys Chem Chem Phys. 2013 Oct 21;15(39):16463-7. doi: 10.1039/c3cp52596a. Epub 2013 Sep 2.
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Original design of an oxygen-tolerant [NiFe] hydrogenase: major effect of a valine-to-cysteine mutation near the active site.耐氧[NiFe]氢化酶的原始设计:活性位点附近的缬氨酸到半胱氨酸突变的主要影响。
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