Asp83, Glu113and Glu134are not specifically involved in Schiff base protonation or wavelength regulation in bovine rhodopsin
- 15 January 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 260 (1) , 113-118
- https://doi.org/10.1016/0014-5793(90)80080-3
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 (E113Q) or Glu134 by Asp (E134D), respectively. All 3 substitutions had only marginal effects on the spectral properties of the final pigment (⩽ 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.Keywords
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