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

Jay M. Janz, David Farrens

Research output: Contribution to journalArticle

25 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)2991-3002
Number of pages12
JournalVision Research
Volume43
Issue number28
DOIs
StatePublished - Dec 2003

Fingerprint

Rhodopsin
Schiff Bases
Opsins
Retinal Diseases
Retinal Pigments
Hydrolysis

Keywords

  • Arrhenius analysis
  • Retinal
  • Rhodopsin
  • Schiff base hydrolysis
  • Thermal stability

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems

Cite this

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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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AU - Farrens, David

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AB - 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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KW - Schiff base hydrolysis

KW - Thermal stability

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