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Asp 83 , Glu 113 and Glu 134 are not specifically involved in Schiff base protonation or wavelength regulation in bovine rhodopsin
Author(s) -
Janssen J.J.M.,
De Caluwé G.L.J.,
De Grip W.J.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80080-3
Subject(s) - rhodopsin , protonation , schiff base , chromophore , chemistry , pigment , mutagenesis , stereochemistry , photochemistry , biochemistry , mutant , retinal , organic chemistry , ion , gene
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 Asp 83 by Asn (D 83 N), Glu 113 by Gln (E 113 Q) or Glu 134 by Asp (E 134 D), 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.