Role of hydrogen-bond network in energy storage of bacteriorhodopsin's light-driven proton pump revealed by ab initio normal-mode analysis
Role of hydrogen-bond network in energy storage of bacteriorhodopsin's light-driven proton pump revealed by ab initio normal-mode analysis
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DOI：
10.1021/ja047506s
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发表时间：
2004-09-01
影响因子：
15
通讯作者：
Schulten, K
中科院分区：
文献类型：
--
作者：
Hayashi, S;Tajkhorshid, E;Schulten, K
通过从头算量子力学/分子力学 (QM/MM) 方法研究了细菌视紫红质 (bR)（盐细菌中充当光驱动质子泵的蛋白质）结合位点的氢键网络的振动模式。对内部水分子的 O−D 和 N−D 拉伸模式以及早期中间状态 K 的视网膜生色团席夫碱进行的正态模式分析计算，很好地再现了实验观察到的振动光谱。与观察到的光谱一致，QM/MM 计算表明发色团光异构化时减弱的氢键是 bR 中能量储存的重要手段。
Vibrational modes of the hydrogen-bond network in the binding site of bacteriorhodopsin (bR), a protein in halobacteria functioning as a light-driven proton pump, were investigated by an ab initio quantum mechanical/molecular mechanical (QM/MM) method. Normal-mode analysis calculations for O−D and N−D stretching modes of internal water molecules and the Schiff base of the retinal chromophore in the early intermediate state, K, reproduced well experimentally observed vibrational spectra. Supported by agreement with observed spectra, the QM/MM calculation suggests that weakened hydrogen bonds upon photoisomerization of the chromophore are an important means of energy storage in bR.