Picosecond structural dynamics of myoglobin following photolysis of carbon monoxide
Picosecond structural dynamics of myoglobin following photolysis of carbon monoxide
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DOI：
10.1021/jp952483c
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发表时间：
1996-02-22
影响因子：
--
通讯作者：
Dyer, RB
中科院分区：
文献类型：
--
作者：
Causgrove, TP;Dyer, RB
我们利用皮秒红外（IR）瞬态吸收光谱在酰胺I波段探测一氧化碳光解后肌红蛋白（Mb）的蛋白质运动动力学。脱氧蛋白构象的上升时间约为8 ps。在光解后50 ps时也测量了酰胺I的变化光谱，发现与静态红外差谱和时间分辨红外光谱相似。通过比较这里得到的结果与其他皮秒内从Mb光解CO的结果，我们得出结论，在酰胺I光谱中看到的大部分变化是由于血红素近端的整体运动。将酰胺I变化的时间尺度与分子动力学计算结果进行了比较。
We have used picosecond infrared (IR) transient absorption spectroscopy in the amide I band tp probe the dynamics of protein motion of myoglobin (Mb) following the photolysis of carbon monoxide. The rise time of the deoxy protein conformation is shown to be about 8 ps. The spectrum of amide I changes was also measured at 50 ps after photolysis and found to be similar to static IR difference spectra and to time-resolved IR spectra taken at times longer than 100 ns. By comparing the results obtained here with other picosecond results on photolysis of CO from Mb, we conclude that the majority of changes seen in the amide I spectra are due to global motion on the proximal side of the heme. The time scale for amide I changes are compared to the results of molecular dynamics calculations.