Probing the Role of the Internal Disulfide Bond in Regulating Conformational Dynamics in Neuroglobin
Probing the Role of the Internal Disulfide Bond in Regulating Conformational Dynamics in Neuroglobin
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DOI：
10.1016/j.bpj.2010.04.033
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发表时间：
2010-07-21
影响因子：
3.4
通讯作者：
Miksovska, Jaroslava
中科院分区：
文献类型：
--
作者：
Astudillo, Luisana;Bernad, Sophie;Miksovska, Jaroslava
在本报告中，我们证明了人神经球蛋白内部的二硫桥调节与配体光解离与血红素活性位点相关的结构变化。这一点从时间分辨光热研究中可以明显看出，该研究显示，当配体从人神经球蛋白中释放时，CO的体积增加13.4 +/- 0.9 mL mol(-1)，而CO从大鼠神经球蛋白中分离时，体积变化明显更小（δ V = 4.6 +/- 0.3 mL mol(-1)）。人神经球蛋白内部二硫键的减少导致构象变化（由AV反映），几乎与大鼠Ngb观察到的相同。我们的数据支持Cys（46）和Cys（55）之间的二硫键调节人类神经球蛋白功能的假设。
In this report, we demonstrate that the internal disulfide bridge in human neuroglobin modulates structural changes associated with ligand photo-dissociation from the heme active site. This is evident from time-resolved photothermal studies of CO photo-dissociation, which reveal a 13.4 +/- 0.9 mL mol(-1) volume expansion upon ligand photo-release from human neuroglobin, whereas the CO dissociation from rat neuroglobin leads to a significantly smaller volume change (Delta V = 4.6 +/- 0.3 mL mol(-1)). Reduction of the internal disulfide bond in human neuroglobin leads to conformational changes (reflected by AV) nearly identical to those observed for rat Ngb. Our data favor the hypothesis that the disulfide bond between Cys(46) and Cys(55) modulates the functioning of human neuroglobin.