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Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy v.174, 2017년, pp.25 - 31   SCI SCIE
본 등재정보는 저널의 등재정보를 참고하여 보여주는 베타서비스로 정확한 논문의 등재여부는 등재기관에 확인하시기 바랍니다.

pH-dependent absorption spectra of rhodopsin mutant E113Q: On the role of counterions and protein

Xie, Peng (State Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, Liaoning 116023, People's Republic of China ) ; Zhou, Panwang (State Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, Liaoning 116023, People's Republic of China ) ; Alsaedi, Ahmed (Nonlinear Analysis and Applied Mathematics (NAAM) Research Group, Department of Mathematics, Faculty of Science, King Abdulaziz University, Jeddah 21589, Saudi Arabia ) ; Zhang, Yan (State Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, Liaoning 116023, People's Republic of China ) ;
  • 초록  

    Abstract The absorption spectra of bovine rhodopsin mutant E113Q in solutions were investigated at the molecular level by using a hybrid quantum mechanics/molecular mechanics (QM/MM) method. The calculations suggest the mechanism of the absorption variations of E113Q at different pH values. The results indicate that the polarizations of the counterions in the vicinity of Schiff base under protonation and unprotonation states of the mutant E113Q would be a crucial factor to change the energy gap of the retinal to tune the absorption spectra. Glu-181 residue, which is close to the chromophore, cannot serve as the counterion of the protonated Schiff base of E113Q in dark state. Moreover, the results of the absorption maximum in mutant E113Q with the various anions (Cl − , Br − , I − and NO 3 − ) manifested that the mutant E113Q could have the potential for use as a template of anion biosensors at visible wavelength. Highlights The absorption spectral tuning mechanism of E113Q rhodopsin in dark state at different pH values is elaborated. The counterions around Schiff base are more crucial than the protein environments to affect the absorption spectra of E113Q. E113Q rhodopsin has the potential for use as a template of anion biosensors at visible wavelength. Graphical Abstract [DISPLAY OMISSION]


  • 주제어

    Spectra tuning .   QM/MM .   E113Q rhodopsin .   Hydrogen-bond .   Anion biosensor.  

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