PMID: 2105232Jan 15, 1990Paper

Asp83, Glu113 and Glu134 are not specifically involved in Schiff base protonation or wavelength regulation in bovine rhodopsin

FEBS Letters
J J JanssenW J de Grip

Abstract

Site-specific mutagenesis was employed to investigate the proposed contribution of proton-donating residues (Glu, Asp) in the membrane domains of bovine rhodopsin to protonation of the Schiff base-linking protein and chromophore or to wavelength modulation of this visual pigment. Three point-mutations were introduced to replace the highly conserved residues Asp83 by Asn (D83N), Glu113 by Gln (E113 Q) or Glu134 by Asp (E134D), respectively. All 3 substitutions had only marginal effects on the spectral properties of the final pigment (less than or equal to 3 nm blue-shift relative to native rhodopsin). Hence, none of these residues by itself is specifically involved in Schiff base protonation or wavelength modulation of bovine rhodopsin.

References

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Citations

Dec 1, 1990·Trends in Pharmacological Sciences·J Findlay, E Eliopoulos
Sep 1, 1995·Biophysical Chemistry·G L DeCaluwéW J de Grip
Aug 1, 1991·Current Opinion in Neurobiology·M L Applebury
Oct 15, 1996·Proceedings of the National Academy of Sciences of the United States of America·P J ReevesH G Khorana
Jan 1, 1992·DNA and Cell Biology·W C ProbstS C Sealfon
Oct 28, 2009·Molecular Biology and Evolution·Tohru SugawaraNorihiro Okada
Feb 11, 2014·Molecular Biology and Evolution·Ryan K SchottBelinda S W Chang
Feb 19, 2016·Protein Science : a Publication of the Protein Society·Ilke van HazelBelinda S W Chang

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