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首页> 外文期刊>IUCrJ >Ligand pathways in neuroglobin revealed by low-temperature photodissociation and docking experiments
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Ligand pathways in neuroglobin revealed by low-temperature photodissociation and docking experiments

机译：低温光解离和对接实验揭示神经球蛋白中的配体途径

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A combined biophysical approach was applied to map gas-docking sites within murine neuroglobin (Ngb), revealing snapshots of events that might govern activity and dynamics in this unique hexacoordinate globin, which is most likely to be involved in gas-sensing in the central nervous system and for which a precise mechanism of action remains to be elucidated. The application of UV–visible microspectroscopy in crystallo, solution X-ray absorption near-edge spectroscopy and X-ray diffraction experiments at 15–40 K provided the structural characterization of an Ngb photolytic intermediate by cryo-trapping and allowed direct observation of the relocation of carbon monoxide within the distal heme pocket after photodissociation. Moreover, X-ray diffraction at 100 K under a high pressure of dioxygen, a physiological ligand of Ngb, unravelled the existence of a storage site for O2 in Ngb which coincides with Xe-III, a previously described docking site for xenon or krypton. Notably, no other secondary sites were observed under our experimental conditions.
机译：一种组合的生物物理方法被用于绘制鼠神经球蛋白（Ngb）内的气体停靠位点，揭示了可能控制这种独特的六坐标球蛋白的活动和动力学的事件的快照，该事件最有可能参与中枢神经系统的气体传感系统，其精确的作用机理还有待阐明。紫外可见光谱在结晶，溶液X射线吸收近边缘光谱和X射线衍射实验中在15–40 K的应用提供了Ngb光解中间体的低温捕获结构特征，并可以直接观察迁移光解离后血红素远端囊袋内的一氧化碳此外，在高压下（Ngb的生理学配体）双氧在100 K下进行的X射线衍射揭示了Ngb中O2的储存位点的存在，该位点与Xe-III（先前描述的氙或k的对接位点）一致。值得注意的是，在我们的实验条件下没有观察到其他次要位点。

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