Abstract
In visual and archaeal rhodopsins, light energy is stored in the chromophore-protein interaction after retinal photoisomerization. This paper reports a novel method to monitor the steric constraint after retinal isomerization by use of enhanced C-D stretching vibrations. In the difference FTIR spectra between an archaeal light-sensor pharaonis phoborhodopsin (ppR) and the primary K intermediate at 77 K, no peaks were observed in the 2160-2330 cm-1 region for deuterated retinals at position 7, 8, 10, 11, 12, and 15, whereas a strong peak appeared at 2244 cm-1 for the K intermediate of ppR possessing a C14-D-labeled retinal. The 2244-cm-1 band is assigned as the C14-D stretching vibration, and enhanced absorption in the K state probably originates from the local steric constraint at the C14-D position (also possible electrostatic field effects) after the C13=C14 double bond rotation.
| Original language | English |
|---|---|
| Pages (from-to) | 16036-16037 |
| Number of pages | 2 |
| Journal | Journal of the American Chemical Society |
| Volume | 127 |
| Issue number | 46 |
| DOIs | |
| Publication status | Published - Nov 23 2005 |
| Externally published | Yes |
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Steric constraint in the primary photoproduct of an archaeal rhodopsin from regiospecific perturbation of C-D stretching vibration of the retinyl chromophore. / Sudo, Yuki; Furutani, Yuji; Wada, Akimori; Ito, Masayoshi; Kamo, Naoki; Kandori, Hideki.
In: Journal of the American Chemical Society, Vol. 127, No. 46, 23.11.2005, p. 16036-16037.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Steric constraint in the primary photoproduct of an archaeal rhodopsin from regiospecific perturbation of C-D stretching vibration of the retinyl chromophore
AU - Sudo, Yuki
AU - Furutani, Yuji
AU - Wada, Akimori
AU - Ito, Masayoshi
AU - Kamo, Naoki
AU - Kandori, Hideki
PY - 2005/11/23
Y1 - 2005/11/23
N2 - In visual and archaeal rhodopsins, light energy is stored in the chromophore-protein interaction after retinal photoisomerization. This paper reports a novel method to monitor the steric constraint after retinal isomerization by use of enhanced C-D stretching vibrations. In the difference FTIR spectra between an archaeal light-sensor pharaonis phoborhodopsin (ppR) and the primary K intermediate at 77 K, no peaks were observed in the 2160-2330 cm-1 region for deuterated retinals at position 7, 8, 10, 11, 12, and 15, whereas a strong peak appeared at 2244 cm-1 for the K intermediate of ppR possessing a C14-D-labeled retinal. The 2244-cm-1 band is assigned as the C14-D stretching vibration, and enhanced absorption in the K state probably originates from the local steric constraint at the C14-D position (also possible electrostatic field effects) after the C13=C14 double bond rotation.
AB - In visual and archaeal rhodopsins, light energy is stored in the chromophore-protein interaction after retinal photoisomerization. This paper reports a novel method to monitor the steric constraint after retinal isomerization by use of enhanced C-D stretching vibrations. In the difference FTIR spectra between an archaeal light-sensor pharaonis phoborhodopsin (ppR) and the primary K intermediate at 77 K, no peaks were observed in the 2160-2330 cm-1 region for deuterated retinals at position 7, 8, 10, 11, 12, and 15, whereas a strong peak appeared at 2244 cm-1 for the K intermediate of ppR possessing a C14-D-labeled retinal. The 2244-cm-1 band is assigned as the C14-D stretching vibration, and enhanced absorption in the K state probably originates from the local steric constraint at the C14-D position (also possible electrostatic field effects) after the C13=C14 double bond rotation.
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UR - http://www.scopus.com/inward/citedby.url?scp=28044458965&partnerID=8YFLogxK
U2 - 10.1021/ja056203a
DO - 10.1021/ja056203a
M3 - Article
C2 - 16287285
AN - SCOPUS:28044458965
VL - 127
SP - 16036
EP - 16037
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 46
ER -