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Static Disorder in Excitation Energies of the Fenna–Matthews–Olson Protein: Structure-Based Theory Meets Experiment
The Journal of Physical Chemistry Letters ( IF 5.7 ) Pub Date : 2020-11-23 , DOI: 10.1021/acs.jpclett.0c03123
Marten L. Chaillet 1 , Florian Lengauer 2 , Julian Adolphs 3 , Frank Müh 2 , Alexander S. Fokas 4 , Daniel J. Cole 5 , Alex W. Chin 6 , Thomas Renger 2
Affiliation  

Inhomogeneous broadening of optical lines of the Fenna–Matthews–Olson (FMO) light-harvesting protein is investigated by combining a Monte Carlo sampling of low-energy conformational substates of the protein with a quantum chemical/electrostatic calculation of local transition energies (site energies) of the pigments. The good agreement between the optical spectra calculated for the inhomogeneous ensemble and the experimental data demonstrates that electrostatics is the dominant contributor to static disorder in site energies. Rotamers of polar amino acid side chains are found to cause bimodal distribution functions of site energy shifts, which can be probed by hole burning and single-molecule spectroscopy. When summing over the large number of contributions, the resulting distribution functions of the site energies become Gaussians, and the correlations in site energy fluctuations at different sites practically average to zero. These results demonstrate that static disorder in the FMO protein is in the realm of the central limit theorem of statistics.

中文翻译:

Fenna–Matthews–Olson蛋白的激发能中的静态障碍:基于结构的理论与实验相结合

通过将蛋白质的低能构象子状态的蒙特卡洛采样与局部过渡能(位能)的量子化学/静电计算相结合,研究了芬纳-马修斯-奥尔森(FMO)光捕获蛋白的光路的不均匀加宽)的颜料。为非均匀整体计算的光谱与实验数据之间的良好一致性表明,静电是位能中静电无序的主要因素。发现极性氨基酸侧链的旋转异构体引起位能转移的双峰分布功能,可以通过空穴燃烧和单分子光谱法进行探测。当对大量贡献进行求和时,所产生的位能分布函数变为高斯分布,而且不同站点的站点能量波动的相关性实际上平均为零。这些结果表明,FMO蛋白中的静态异常处于统计中心极限定理的范围内。
更新日期:2020-12-17
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