Serine 85 in Transmembrane Helix 2 of Short-Wavelength Visual Pigments Interacts with the Retinylidene Schiff Base Counterion†

Biochemistry ◽  
2001 ◽  
Vol 40 (50) ◽  
pp. 15098-15108 ◽  
Author(s):  
Abhiram Dukkipati ◽  
Bryan W. Vought ◽  
Deepak Singh ◽  
Robert R. Birge ◽  
Barry E. Knox
Keyword(s):  
Schiff Base ◽  
Short Wavelength ◽  
Transmembrane Helix ◽  
Visual Pigments

Regulation of Photoactivation in Vertebrate Short Wavelength Visual Pigments:  Protonation of the Retinylidene Schiff Base and a Counterion Switch

Biochemistry ◽  
2007 ◽  
Vol 46 (18) ◽  
pp. 5330-5340 ◽  
Author(s):  
Lavoisier S. Ramos ◽  
Min-Hsuan Chen ◽  
Barry E. Knox ◽  
Robert R. Birge
Keyword(s):  
Schiff Base ◽  
Short Wavelength ◽  
Visual Pigments

Regulation of Phototransduction in Short-Wavelength Cone Visual Pigments via the Retinylidene Schiff Base Counterion†

Biochemistry ◽  
2001 ◽  
Vol 40 (46) ◽  
pp. 13760-13766 ◽  
Author(s):  
Kunnel R. Babu ◽  
Abhiram Dukkipati ◽  
Robert R. Birge ◽  
Barry E. Knox
Keyword(s):  
Schiff Base ◽  
Short Wavelength ◽  
Visual Pigments

scholarly journals Euphausiid visual pigments. The rhodopsins of Euphausia superba and Meganyctiphanes norvegica (Crustacea, Euphausiacea).

1982 ◽  
Vol 80 (3) ◽  
pp. 451-472 ◽  
Author(s):  
C J Denys ◽  
P K Brown
Keyword(s):  
Schiff Base ◽  
Euphausia Superba ◽  
Visual Pigments ◽  
Long Wavelength ◽  
Spectral Changes ◽  
Accessory Pigment ◽  
Meganyctiphanes Norvegica ◽  
Ph Dependent ◽  
Wavelength Light ◽  
Absorbance Spectra

The rhabdoms of Euphausia superba contain one digitonin-extractable rhodopsin, lambda max 485 nm. The rhodopsin undergoes unusual pH-dependent spectral changes: above neutrality, the absorbance decreases progressively at 485 nm and rises near 370 nm. This change is reversible and appears to reflect an equilibrium between a protonated and an unprotonated form of the rhodopsin Schiff-base linkage. Near neutral pH and at 10 degrees C, the rhodopsin is partiaLly converted by 420-nm light to a stable 493-nm metarhodopsin. The metarhodopsin is partially photoconverted to rhodopsin by long-wavelength light in the absence of NH2OH; in the presence of NH2OH, it is slowly converted to retinal oxime and opsin. The rhodopsin of Meganyctiphanes norvegica measured in fresh rhabdoms by microspectrophotometry has properties very similar to those of the extracted rhodopsin of E. superba. Its lambda max is 488 nm and it is partially photoconverted by short wavelength irradiation to a stable photoconvertible metarhodopsin similar to that of E. superba. In the presence of light and NH2OH, the M. norvegica metarhodopsin is converted to retinal oxime and opsin. Our results indicate that previous determinations of euphausiid rhodopsin absorbance spectra were incorrect because of accessory pigment contamination.

2P284 Effect of Schiff base protonation on the quantum yield of visual pigments

2005 ◽  
Vol 45 (supplement) ◽  
pp. S190
Author(s):  
K. Tsutsui ◽  
H. Imai ◽  
Y. Shichida
Keyword(s):  
Schiff Base ◽  
Quantum Yield ◽  
Visual Pigments

Visual pigments in the early life stages of Pacific northwest marine fishes

2001 ◽  
Vol 204 (14) ◽  
pp. 2581-2587 ◽  
Author(s):  
Lyle L. Britt ◽  
Ellis R. Loew ◽  
William N. McFarland
Keyword(s):  
Pacific Northwest ◽  
Marine Fish ◽  
Short Wavelength ◽  
Fish Larvae ◽  
Visual Pigments ◽  
Rods And Cones ◽  
Marine Fish Larvae ◽  
Wavelength Sensitivity ◽  
Single Instance ◽  
Cone Type

SUMMARY Microspectrophotometry was used to measure the visual pigments in the rods and cones of 22 species of marine fish larvae netted from the surface waters off Friday Harbor Laboratories, Washington, USA. 13 species had rods, 12 of which contained visual pigments with a wavelength of maximum absorbance near 500nm, while one, the sand lance (Ammodytes hexapterus), had its absorbance maximum at 482nm. The 22 species of fish larvae possessed varied combinations of single, double and twin cones, ranging in peak absorbance from 353nm to 584nm. Of these, green-sensitive single cones were present in 20 of the 22 species, and were the dominant cone type. Double and twin cones were present in 13 of the species. Most common were identical green-sensitive (twin) cones (in 11 species). Green/yellow-sensitive double cones occurred in four species. In a single instance (Hemilepidotus hemilepidotus) twin blue-sensitive, twin green-sensitive and double blue/yellow-sensitive cones were recorded. Of particular interest was the finding that 18 of the species had ultraviolet- and/or violet-absorbing single cones. It has been suggested that short-wavelength photosensitivity may be beneficial for planktivory by extending the spectral range over which vision can occur. The high percentage (82%) of ultraviolet and violet visual pigments in Pacific northwest fish larvae supports the prediction that short-wavelength sensitivity may be common in marine fish larvae.

Chicken blue and chicken violet, short wavelength sensitive visual pigments

1981 ◽  
Vol 21 (4) ◽  
pp. 581-586 ◽  
Author(s):  
Lei Yen Fager ◽  
Roger S. Fager
Keyword(s):  
Short Wavelength ◽  
Visual Pigments

scholarly journals Spectral tuning and evolution of primate short-wavelength-sensitive visual pigments

2011 ◽  
Vol 279 (1727) ◽  
pp. 387-393 ◽  
Author(s):  
Livia S. Carvalho ◽  
Wayne L. Davies ◽  
Phyllis R. Robinson ◽  
David M. Hunt
Keyword(s):  
Phylogenetic Analysis ◽  
Spectral Analysis ◽  
Short Wavelength ◽  
Primate Evolution ◽  
Visual Pigments ◽  
Uv Sensitivity ◽  
Tuning Mechanism ◽  
Initial Event ◽  
Primary Mechanism

The peak sensitivities ( λ max ) of the short-wavelength-sensitive-1 (SWS1) pigments in mammals range from the ultraviolet (UV) (360–400 nm) to the violet (400–450 nm) regions of the spectrum. In most cases, a UV or violet peak is determined by the residue present at site 86, with Phe conferring UV sensitivity (UVS) and either Ser, Tyr or Val causing a shift to violet wavelengths. In primates, however, the tuning mechanism of violet-sensitive (VS) pigments would appear to differ. In this study, we examine the tuning mechanisms of prosimian SWS1 pigments. One species, the aye-aye, possesses a pigment with Phe86 but in vitro spectral analysis reveals a VS rather than a UVS pigment. Other residues (Cys, Ser and Val) at site 86 in prosimians also gave VS pigments. Substitution at site 86 is not, therefore, the primary mechanism for the tuning of VS pigments in primates, and phylogenetic analysis indicates that substitutions at site 86 have occurred at least five times in primate evolution. The sole potential tuning site that is conserved in all primate VS pigments is Pro93, which when substituted by Thr (as found in mammalian UVS pigments) in the aye-aye pigment shifted the peak absorbance into the UV region with a λ max value at 371 nm. We, therefore, conclude that the tuning of VS pigments in primates depends on Pro93, not Tyr86 as in other mammals. However, it remains uncertain whether the initial event that gave rise to the VS pigment in the ancestral primate was achieved by a Thr93Pro or a Phe86Tyr substitution.

Sign in / Sign up

Export Citation Format

Share Document