scholarly journals Red-Tuning of the Channelrhodopsin Spectrum Using Long Conjugated Retinal Analogues

Biochemistry ◽  
2018 ◽  
Vol 57 (38) ◽  
pp. 5544-5556 ◽  
Author(s):  
Yi-Chung Shen ◽  
Toshikazu Sasaki ◽  
Take Matsuyama ◽  
Takahiro Yamashita ◽  
Yoshinori Shichida ◽  
...  
Keyword(s):  
Retinal Analogues

Use of retinal analogues for the study of visual pigment function

2002 ◽  
pp. 29-48 ◽  
Author(s):  
Rosalie K. Crouch ◽  
Vladimir Kefalov ◽  
Wolfgang Gartner ◽  
M. Carter Cornwall
Keyword(s):  
Visual Pigment ◽  
Retinal Analogues

Synthesis of C11-to-C14 methyl-shifted all-trans-retinal analogues and their activities on human aldo-keto reductases

2020 ◽  
Vol 18 (25) ◽  
pp. 4788-4801
Author(s):  
Aurea Rivas ◽  
Raquel Pequerul ◽  
Vito Barracco ◽  
Marta Domínguez ◽  
Susana López ◽  
...  
Keyword(s):  
Vitamin A ◽  
Retinal Analogues

Human aldo-keto reductases (AKRs) are enzymes involved in the reduction, among other substrates, of all-trans-retinal to all-trans-retinol (vitamin A), thus contributing to the control of the levels of retinoids in organisms.

scholarly journals Modulation of spectral properties and pump activity of proteorhodopsins by retinal analogues

2015 ◽  
Vol 467 (2) ◽  
pp. 333-343 ◽  
Author(s):  
Srividya Ganapathy ◽  
Odette Bécheau ◽  
Hanka Venselaar ◽  
Siebren Frölich ◽  
Jeroen B. van der Steen ◽  
...  
Keyword(s):  
Vitamin A ◽  
Spectral Properties ◽  
Proton Pumps ◽  
Pump Activity ◽  
Retinal Analogues ◽  
Vitamin A Derivative ◽  
Absorbance Band

Microbial proteorhodopsins are light-driven proton pumps, using the vitamin A derivative retinal as chromophore. We show that retinal analogues can shift their absorbance band with preservation of functionality. This may provide attractive opportunities in biotechnology, optogenetics and as potential sensors.

Studies on Pyry I retinal Analogues of Bacteriorhodopsin

1999 ◽  
Vol 70 (6) ◽  
pp. 949-956
Author(s):  
Joydip Das ◽  
Rosalie K. Crouch ◽  
Rajni Govindjee ◽  
Sergei Balashov ◽  
Thomas Ebrey
Keyword(s):  
Retinal Analogues

The spectral properties and photosensitivities of analogue photopigments regenerated with 10- and 14-substituted retinal analogues

1988 ◽  
Vol 233 (1270) ◽  
pp. 55-76 ◽  
Keyword(s):  
Schiff Base ◽  
Binding Site ◽  
Steric Hindrance ◽  
Visual Pigment ◽  
Spectral Properties ◽  
The Other ◽  
Porichthys Notatus ◽  
Counter Ion ◽  
Two Systems ◽  
Retinal Analogues

Analogues of 11- cis - and 9- cis -retinal with substitutions at positions 10 and 14 were used to regenerate analogue photopigments with two opsins: that of the transmuted (cone-like) 521-pigment of Gekko gekko and that of the rhodopsin of Porichthys notatus . The spectral absorbances and photosensitivities of the regenerated photopigments were determined and compared, first, between the two systems of analogue photopigments, and second, in the responses to the two opsins. Unlike the 10-fluoropigments, the comparable 14-compounds were significantly redshifted by 19–30 nm and their sensitivity to light was similar to that of the parent 11- cis - and 9- cis -pigments. These were the results for both analogue pigments. In contrast, the 10-pigments were spectrally located close to the wavelengths of the parent compounds and the photosensitivity was significantly reduced, especially in the case of the 9- cis -analogues. Evidence was obtained for a steric hindrance effect at position 14, for no regeneration was obtained when methyl or ethyl groups were at this carbon. In the 10-substituted retinals, steric hindrance was noted only for the gecko; only the fluorosubstituted, but not the chloro-, the methyl- or the ethyl-substituted, retinals reacted. With the fish opsin, pigments were regenerated with all but the ethyl-substituted retinal. The gecko opsin appears to have a more restricted binding site. Another feature of the gecko was related to the chloride bathochromic and hyperchromic effects, in which the 521-pigment prepared in a chloride-deficient state has a blue-shifted spectrum compared with the spectrum obtained after the addition of chloride, and its extinction is raised by the addition of chloride to give a mean ratio of 1.23 for the two extinctions, one with, the other without, added chloride. The 11- cis -10-F-analogue pigment gave both chloride effects and the hyperchromic ratio was the same as that recorded for the native visual pigment. In contrast, the pigment formed with 11- cis -14-F-retinal gave a hyperchromic ratio significantly greater than 1.23. A similar contrast in the responses to chloride was obtained with the analogue photopigments regenerated with the 9- cis -10-F- and 9- cis -14-F-chromophores. This difference between the two systems is interpreted as the result of a specific configurational feature of the gecko opsin when in the chloride-deficient state that is relevant to the binding of the retinal analogue. Together, the results point to a different interaction with the visual protein on the part of the 10- and 14-substituted retinals. The latter adjust the pigment colour by acting specifically at the opsin site of the negative counter ion responsible for adjusting the degree of protonation of the Schiff base nitrogen.

ChemInform Abstract: A Laser Flash Photolysis Study of 11-Cis-Locked Retinal Analogues.

ChemInform ◽  
2010 ◽  
Vol 27 (20) ◽  
pp. no-no
Author(s):  
P. F. MCGARRY ◽  
J. CHEH ◽  
B. RUIZ-SILVA ◽  
S. HU ◽  
J. WANG ◽  
...  
Keyword(s):  
Flash Photolysis ◽  
Laser Flash Photolysis ◽  
Laser Flash ◽  
Retinal Analogues

scholarly journals Photoreaction Dynamics of Red-Shifting Retinal Analogues Reconstituted in Proteorhodopsin

2019 ◽  
Vol 123 (19) ◽  
pp. 4242-4250 ◽  
Author(s):  
Yusaku Hontani ◽  
Srividya Ganapathy ◽  
Sean Frehan ◽  
Miroslav Kloz ◽  
Willem J. de Grip ◽  
...  
Keyword(s):  
Retinal Analogues
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