Development of inter-molecular interaction theory for excited states

激发态分子间相互作用理论的发展

• 批准号: 21685002
• 负责人: HASEGAWA Jun-ya
• 金额: $ 15.81万
• 依托单位: Kyoto University
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Young Scientists (A)
• 财政年份: 2009
• 资助国家: 日本
• 起止时间: 2009 至 2011
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-21685002/
• 关键词: 理論化学; 量子化学; 電子状態理論; マルチフィジクス理論; 励起状態理論; 分子間相互作用; 光機能性蛋白質; カラーチューニング; 励起状態; 分子軌道局在化法; ソルバトクロミズム; オプシンシフト; 励起エネルギー移動; 脱プロトン化シッフ塩基; 蛍光蛋白質; レチナール蛋白質; SAC-CI; QM; MM; 蛋白質の電子状態

Depending on molecular environment, some photo-functional proteins(human visual cone pigments and fluorescent proteins) significantly change their photo-absorption/emission energy. We performed quantum chemical calculations to analyze the mechanism. We found that, upon excitation, the charge distributions of the chromophores change significantly and the proteins produce polarized electrostatic potential. These two facts cause a synergy effect on the excitation energy. We also found that the wave functions of amino acids close to the chromophore also affect the excitation energy in some retinal proteins. To analyze the electronic effect of the protein environment, we have developed a new localization scheme that can localize MOs into predefined shapes and regions. This localization scheme was applied to analyze the pathway for the excitation transfer.

根据分子环境，一些光功能蛋白（人类视锥色和荧光蛋白）显着改变其光吸收/发射能。我们进行了量子化学计算以分析机制。我们发现，在激发时，发色团的电荷分布发生了显着变化，并且蛋白质产生偏振电位。这两个事实对激发能产生协同作用。我们还发现，接近发色团的氨基酸的波功能也会影响某些视网膜蛋白的激发能。为了分析蛋白质环境的电子效应，我们开发了一种新的定位方案，该方案可以将MOS定位到预定义的形状和区域中。该定位方案用于分析激发转移的途径。

项目成果

Circular Dichroism and Absorption Spectroscopy for Three-membered Ring Compounds Using Symmetry-adapted Cluster-Configuration Interaction(SAC-CI) Method

使用对称性簇构型相互作用 (SAC-CI) 方法对三元环化合物进行圆二色性和吸收光谱分析

• DOI: 10.1246/bcsj.82.1215
• 发表时间: 2009
• 期刊: Bull. Chem. Soc. Jpn
• 作者: T. Miyahara;J. Hasegawa;and H. Nakatsuji
• 通讯作者: and H. Nakatsuji

Theoretical Study of the Excited States of the Photosynthetic Reaction Center in Photo system II: Elecronic Sructure, Interactions, and Their Origin

光系统光合反应中心激发态的理论研究II：电子结构、相互作用及其起源

• DOI: 10.1016/j.bpc.2011.06.011
• 发表时间: 2011
• 期刊: Biophys. Chem
• 作者: Y. Kitagawa;K. Matsuda;and J. Hasegawa
• 通讯作者: and J. Hasegawa

Theoretical Study of the Opsin Shift of Deprotonated Retinal Schiff Base in the Mstate of Bacteriorhodopsin

细菌视紫红质状态下去质子化视网膜希夫碱视蛋白位移的理论研究

• DOI: 10.1039/c0cp00361a
• 发表时间: 2010
• 期刊: Phys. Chem. Chem. Phys
• 作者: K. Fujimoto;K. Asai;and J. Hasegawa
• 通讯作者: and J. Hasegawa

Excited states of photo functional molecules in protein : Electronic structure and interaction Invited talk)

蛋白质中光功能分子的激发态：电子结构和相互作用（特邀报告）

• 发表时间: 2009
• 作者: K. Hotta;A. Yamaguchi;N. Teramae;J. Hasegawa
• 通讯作者: J. Hasegawa

Color tuning in human cone visual pigments

人锥视色素的颜色调节

• 期刊: Progress in Theoretical Physics and Chemistry
• 作者: J. Hasegawa;K. Fujimoto;and H. Nakatsuji
• 通讯作者: and H. Nakatsuji