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

Jay M. Janz; David L. Farrens

doi:10.1016/j.visres.2003.08.010

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

Jay M. Janz, David L. Farrens

Chemical Physiology and Biochemistry

Research output: Contribution to journal › Article › peer-review

32 Scopus citations

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 language	English (US)
Pages (from-to)	2991-3002
Number of pages	12
Journal	Vision Research
Volume	43
Issue number	28
DOIs	https://doi.org/10.1016/j.visres.2003.08.010
State	Published - Dec 2003

Keywords

Arrhenius analysis
Retinal
Rhodopsin
Schiff base hydrolysis
Thermal stability

ASJC Scopus subject areas

Ophthalmology
Sensory Systems

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10.1016/j.visres.2003.08.010

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title = "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.",

keywords = "Arrhenius analysis, Retinal, Rhodopsin, Schiff base hydrolysis, Thermal stability",

author = "Janz, {Jay M.} and Farrens, {David L.}",

note = "Funding Information: This research was supported in part by grants EY12095 and DA14896 to D.L. Farrens and T32-EY07123-09 to J.M. Janz from the National Institutes of Health. The authors wish to thank Dr. John Denu and Dr. Ujwal Shinde for helpful discussion. A preliminary version of this data was presented at the 7th Annual Vision Research Conference: The Retinoid Cycle and Retina Disease, Fort Lauderdale, FL, 2003.",

year = "2003",

month = dec,

doi = "10.1016/j.visres.2003.08.010",

language = "English (US)",

volume = "43",

pages = "2991--3002",

journal = "Vision Research",

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publisher = "Elsevier Limited",

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T1 - Assessing structural elements that influence Schiff base stability

T2 - Mutants E113Q and D190N destabilize rhodopsin through different mechanisms

AU - Janz, Jay M.

AU - Farrens, David L.

N1 - Funding Information: This research was supported in part by grants EY12095 and DA14896 to D.L. Farrens and T32-EY07123-09 to J.M. Janz from the National Institutes of Health. The authors wish to thank Dr. John Denu and Dr. Ujwal Shinde for helpful discussion. A preliminary version of this data was presented at the 7th Annual Vision Research Conference: The Retinoid Cycle and Retina Disease, Fort Lauderdale, FL, 2003.

PY - 2003/12

Y1 - 2003/12

N2 - 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.

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.

KW - Arrhenius analysis

KW - Retinal

KW - Rhodopsin

KW - Schiff base hydrolysis

KW - Thermal stability

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U2 - 10.1016/j.visres.2003.08.010

DO - 10.1016/j.visres.2003.08.010

M3 - Article

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AN - SCOPUS:0242494305

SN - 0042-6989

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JO - Vision Research

JF - Vision Research

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ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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