Dartigalongue Thibault, Niezborala Claire, Hache François
Laboratoire d'Optique et Biosciences, Ecole Polytechnique, CNRS, INSERM, 91128 Palaiseau cedex, France.
Phys Chem Chem Phys. 2007 Apr 7;9(13):1611-5. doi: 10.1039/b616173a. Epub 2007 Feb 6.
A thorough absorption and circular dichroism study is performed in carbonmonoxy-myoglobin with a sub-picosecond visible pump, ultraviolet probe experiment. Differential absorption in the 220-360 nm range shows that the time-resolved response mainly comes from the heme and that aromatic amino acids do not contribute significantly. Time-resolved CD at 260 nm shows no dynamics and confirms this result. On the contrary, a strong CD dynamics is observed at 230 nm. This signal could originate from transient deformation of the alpha-helices in the protein.
利用亚皮秒可见泵浦-紫外探测实验对一氧化碳肌红蛋白进行了全面的吸收和圆二色性研究。220 - 360 nm范围内的差分吸收表明,时间分辨响应主要来自血红素,芳香族氨基酸的贡献不显著。260 nm处的时间分辨圆二色性没有动力学变化,证实了这一结果。相反,在230 nm处观察到强烈的圆二色性动力学。该信号可能源于蛋白质中α-螺旋的瞬时变形。