E113 is required for the efficient photoisomerization of the unprotonated chromophore in a UV-absorbing visual pigment.
Protonation of the retinal Schiff base chromophore is responsible for the absorption of visible light and is stabilized by the counterion residue E113 in vertebrate visual pigments. However, this residue is also conserved in vertebrate UV-absorbing visual pigments (UV pigments) which have an unprotonated Schiff base chromophore. To elucidate the role played by this residue in the photoisomerization of the unprotonated chromophore in UV pigments, we measured the quantum yield of the E113Q mutant of the mouse UV cone pigment (mouse UV). The quantum yield of the mutant was much lower than that of the wild type, indicating that E113 is required for the efficient photoisomerization of the unprotonated chromophore in mouse UV. Introduction of the E113Q mutation into the chicken violet cone pigment (chicken violet), which has a protonated chromophore, caused deprotonation of the chromophore and a reduction in the quantum yield. On the other hand, the S90C mutation in chicken violet, which deprotonated the chromophore with E113 remaining intact, did not significantly affect the quantum yield. These results suggest that E113 facilitates photoisomerization in both UV-absorbing and visible light-absorbing visual pigments and provide a possible explanation for the complete conservation of E113 among vertebrate UV pigments.
Tsutsui
Kei
K
Department of Biophysics, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan.
Imai
Hiroo
H
Shichida
Yoshinori
Y
D000818:Animals; D002645:Chickens; D007536:Isomerism; D051379:Mice; D010777:Photochemistry; D012168:Retinal Pigments / Q000737:chemistry*; D012243:Rhodopsin / Q000737:chemistry / Q000235:genetics / Q000502:physiology*
D012168:Retinal Pigments; D012243:Rhodopsin