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J Phys Chem B. 2019 Dec 19;123(50):10631-10641. doi: 10.1021/acs.jpcb.9b08189. Epub 2019 Dec 5.

Theoretical Insights into the Mechanism of Wavelength Regulation in Blue-Absorbing Proteorhodopsin.

Author information

1
C. Eugene Bennett Department of Chemistry , West Virginia University , Morgantown , West Virginia 26506 , United States.
2
XtalPi Inc , 245 Main Street, 12th Floor , Cambridge , Massachusetts 01242 , United States.
3
WVU Cancer Institute , West Virginia University , Morgantown , West Virginia 26506 , United States.

Abstract

Proteorhodopsin (PR) is a light-driven proton pump that is most notable for ushering in the discovery of an ever-increasing number of microbial retinal proteins that are at the forefront of fields such as optogenetics. Two variants, blue (BPR) and green (GPR) proteorhodopsin, have evolved to harvest light at different depths of the ocean. The color-tuning mechanism in PR is controlled by a single residue at position 105: in BPR it is a glutamine, whereas in GPR it is a leucine. Although the majority of studies on the spectral tuning mechanism in PR have focused on GPR, detailed understanding of the electronic environment responsible for spectral tuning in BPR is lacking. In this work, several BPR models were investigated using quantum mechanics/molecular mechanics (QM/MM) calculations to obtain fundamental insights into the color tuning mechanism of BPR. We find that the molecular mechanism of spectral tuning in BPR depends on two geometric parameters, the bond length alternation and the torsion angle deviation of the all-trans-retinyl chromophore. Both parameters are influenced by the strength of the hydrogen-bonded networks in the chromophore-binding pocket, which shows how BPR is different from other microbial rhodopsins.

PMID:
31757123
DOI:
10.1021/acs.jpcb.9b08189

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