Assessing structural elements that influence Schiff base stability: mutants E113Q and D190N destabilize rhodopsin through different mechanisms.

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.

• Authors: Jay M Janz, David L Farrens
• Journal: Vision research (Vision Res) Vol. 43 Issue 28 Pg. 2991-3002 (Dec 2003) ISSN: 0042-6989 [Print] England
• PMID: 14611935 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Schiff Bases
• Hydroxylamine
• Rhodopsin

Topics

• Genetic Linkage
• Humans
• Hydrolysis
• Hydroxylamine (metabolism)
• Mutation (genetics)
• Retina (metabolism)
• Rhodopsin (genetics, metabolism)
• Schiff Bases (chemistry)
• Spectrum Analysis (methods)