Assessing structural elements that influence Schiff base stability: mutants E113Q and D190N destabilize rhodopsin through different mechanisms
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Updated: Aug 11, 2026
A Rhodopsin Transport Assay by High-Content Imaging Analysis
Published on: January 16, 2019
1Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Mail Code L224 3181 S.W. Sam Jackson Park Road, Portland, OR 97239, USA.
Abstract:
The stability of the retinal chromophore attachment varies between different visual pigments and may factor in some retinal disease states. Opsin appears to stabilize this Schiff base linkage by: (i) affecting the hydrolysis chemistry, (ii) shielding the retinal linkage from solvent, or (iii) acting as a kinetic trap to slow retinal release. Here we describe methods to determine Schiff base stability in rhodopsin, present examples of dark state and MII rhodopsin stability differences, and show that studies of mutants E113Q and D190N demonstrate different parts of rhodopsin influence Schiff base stability in different ways.
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