Probing the structural basis of oxygen binding in a cofactor‐independent dioxygenase

Li Kunhua; Fielding Elisha N.; Condurso Heather L.Bruner Steven D.

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Probing the structural basis of oxygen binding in a cofactor‐independent dioxygenase

机译：探测氧结合的结构基础一个代数余子式独立加双氧酶

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The enzyme DpgC is included in the small family of cofactor‐independent dioxygenases. The chemistry of DpgC is uncommon as the protein binds and utilizes dioxygen without the aid of a metal or organic cofactor. Previous structural and biochemical studies identified the substrate‐binding mode and the components of the active site that are important in the catalytic mechanism. In addition, the results delineated a putative binding pocket and migration pathway for the co‐substrate dioxygen. Here, structural biology is utilized, along with site‐directed mutagenesis, to probe the assigned dioxygen‐binding pocket. The key residues implicated in dioxygen trafficking were studied to probe the process of binding, activation and chemistry. The results support the proposed chemistry and provide insight into the general mechanism of dioxygen binding and activation.

机译：这种酶DpgC包含在小户型的代数余子式非独立加双氧酶。蛋白结合和DpgC是罕见没有金属的援助或利用分子氧有机辅助因子。生化研究确定了衬底的绑定模式的组件重要的催化活性位点机制。假定的绑定口袋和迁移途径公司检测底物分子氧。利用生物学,以及地理位置指示诱变,探针双氧非绑定的口袋里。与走私分子氧进行了研究探针结合的过程中,激活化学。化学和提供洞察一般双氧绑定和激活机制。

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《Acta crystallographica. Section D, Structural biology.》 |2017年第7期|573-580|共8页
作者
Li Kunhua; Fielding Elisha N.; Condurso Heather L.Bruner Steven D.;
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作者单位

Department of Chemistry, Boston College, Chestnut Hill, MA02467, USA;

Department of Chemistry, University of Florida, Gainesville, FL32611, USA;

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正文语种英语
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关键词
oxygen; Binding; Exploration with a probeNatural productsDioxygenDioxygenasesOXYGEN BINDINGActive Site;

机译：氧气,绑定;probeNatural勘探productsDioxygenDioxygenasesOXYGEN BINDINGActive网站;

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Probing the structural basis of oxygen binding in a cofactor‐independent dioxygenase

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