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• W3048720378 abstract "Rhodopsin is the photosensitive protein, which binds to 11-cis-retinal as its chromophore. In the dark, rhodopsin exists as a stable complex between the opsin moiety and 11-cis-retinal. The absorption of a light photon converts 11-cis-retinal to all-trans-retinal and initiates our vision. As a result, the increase in the rate of dark activation of rhodopsin reduces its photosensitivity resulting in night blindness. The mutations, G90D and T94I are night blindness-causing mutations that exhibit completely different physicochemical characteristics associated with the dark activation of rhodopsin, such as a high rate of thermal isomerization of 11-cis-retinal and a slow pigment regeneration. To elucidate the molecular mechanism by which G90D and T94I mutations affect rhodopsin dark activation and regeneration, we performed light-induced difference FTIR spectroscopy on dark and primary photo-intermediate states of G90D and T94I mutants. The FTIR spectra clearly show that both charged G90D and hydrophobic T94I mutants alter the H-bond network at the Schiff base region of the chromophore, which weakens the electrostatic interaction with Glu113 counterion. Our results further show an altered water-mediated H-bond network around the central transmembrane region of mutant rhodopsin, which is reminiscent of the active Meta-II state. This altered water-mediated H-bond network may cause thermal isomerization of the chromophore and facilitate rhodopsin dark activation." @default.
• W3048720378 created "2020-08-18" @default.
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• W3048720378 date "2020-09-01" @default.
• W3048720378 modified "2023-10-14" @default.
• W3048720378 title "Disruption of Hydrogen-Bond Network in Rhodopsin Mutations Cause Night Blindness" @default.
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• W3048720378 doi "https://doi.org/10.1016/j.jmb.2020.08.006" @default.
• W3048720378 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32795534" @default.
• W3048720378 hasPublicationYear "2020" @default.
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