期刊
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
卷 7, 期 22, 页码 4547-4553出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.6b02043
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资金
- ECHO Grant of The Netherlands Organisation for Scientific Research (NWO) [712.012.005]
- European Research Council (ERC) [EnLight-277755]
- University of Pisa [PRA-2016-46]
- Spanish Ministerio de Economia y Competitividad [RYC2011-08918]
- Agencia de Gestio d'Ajuts Universitaris i de Recerca from Generalitat de Catalunya [SGR2014-1189]
Light sensing in photoreceptor proteins is subtly modulated by the multiple interactions between the chromophoric unit and its binding pocket. Many theoretical and experimental studies have tried to uncover the fundamental origin of these interactions but reached contradictory conclusions as to whether electrostatics, polarization, or intrinsically quantum effects prevail. Here, we select rhodopsin as a prototypical photoreceptor system to reveal the molecular mechanism underlying these interactions and regulating the spectral tuning. Combining a multireference perturbation method and density functional. theory with a classical but atomistic and polarizable embedding scheme, Induction we show that accounting for electrostatics only leads to a qualitatively wrong picture, while a responsive environment can successfully capture both the classical and quantum dominant effects. Several residues are found to tune the excitation by both differentially stabilizing ground and excited states and through nonclassical inductive resonance interactions. The results obtained with such a quantum-in-classical model are validated against both experimental data and fully quantum calculations.
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