Relationship between protein structural fluctuations and rebinding dynamics in ferric haem nitrosyls.
Relationship between protein structural fluctuations and rebinding dynamics in ferric haem nitrosyls.
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亚硝酰亚铁血红素中蛋白质结构波动与重新结合动力学之间的关系。
DOI：
10.1042/bj20101496
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发表时间：
2011
期刊：
影响因子：
--
通讯作者：
Hunt NT
中科院分区：
文献类型：
--
作者：
Hunt NT
一氧化氮(NO)与血红素蛋白的相互作用在生物学中广泛存在。在本文中，我们首次提出了血红素亚硝化的超快2D-IR(二维红外)光谱分析，并结合时间分辨红外泵浦-探测研究，研究了血红素环境的平衡振动动力学与Fe(III)-NO中心的NO光解后的配体重新结合行为之间的关系。对扮演不同生理作用的两种血红蛋白Mb(肌红蛋白)和CC(细胞色素)的研究表明，含有Hem的蛋白质口袋的超快波动形成了明显的对比，表明Mb口袋比CC更具弹性。这与观察到的Mb-NO比CC-NO更慢的光解重结合动力学密切相关，并表明超快波动与生物功能之间的直接联系。此外，这表明线性反应理论在蛋白质配基结合方面的有效性。最后，2D-IR表明，CC-NO在室温下显示了两个不同的结构亚位，它们在通过NO振动寿命可获得的时间尺度上不交换。
The interaction of nitric oxide (NO) with haem proteins is widespread in biology. In the current paper, we present the first ultrafast 2D-IR (two-dimensional infrared) spectroscopic analysis of haem nitrosylation, which has been combined with time-resolved IR pump–probe studies to investigate the relationship between equilibrium vibrational dynamics of the haem environment and ligand rebinding behaviour following photolysis of NO from the Fe(III)–NO site. Studies of two haem proteins, Mb (myoglobin) and Cc (cytochromec), which play different physiological roles, reveal marked contrasts in the ultrafast fluctuations of the protein pockets containing the haem, showing that the Mb pocket is somewhat more flexible than that of Cc. This correlates strongly with slower observed photolysis rebinding kinetics of Mb–NO compared with Cc–NO, and indicates a direct link between ultrafast fluctuations and biological functionality. Furthermore, this indicates the validity of linear response theories in relation to protein ligand binding. Finally, 2D-IR shows that Cc–NO displays two distinct structural sub-sites at room temperature that do not exchange on the timescales accessible via the NO vibrational lifetime.
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影响因子：
15
作者：
Benabbas, Abdelkrim;Ye, Xiong;Kubo, Minoru;Zhang, Zhenyu;Maes, Estelle M.;Montfort, William R.;Champion, Paul M.
通讯作者：
Champion, Paul M.
NO 结合肌红蛋白：NO 配体的结构多样性和动力学。
影响因子：
15
作者：
T. Żemojtel;M. Rini;K. Heyne;T. Dandekar;E. Nibbering;P. Kozlowski
通讯作者：
P. Kozlowski
影响因子：
15
作者：
Kubo, Minoru;Gruia, Flaviu;Benabbas, Abdelkrim;Barabanschikov, Alexander;Montfort, William R.;Maes, Estelle M.;Champion, Paul M.
通讯作者：
Champion, Paul M.
影响因子：
2.9
作者：
TILTON, RF;KUNTZ, ID;PETSKO, GA
通讯作者：
PETSKO, GA
亚硝基肌红蛋白中的三价铁和二价铁：稳定和亚稳态及其红外光谱的计算机模拟。
影响因子：
2.9
作者：
D. R. Nutt;M. Meuwly
通讯作者：
M. Meuwly