Synthesis and properties of 12-fluororetinal and 12-fluororhodopsin. Model system for fluorine-19 NMR studies of visual pigments

Liu, Robert S. H.; Matsumoto, Hiroyuki; Asato, Alfred E.; Denny, Marlene; Shichida, Yoshinori; Yoshizawa, Tôru; Dahlquist, Frederick W.

doi:10.1021/ja00414a026

Cited by 77 publications

(40 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Typical experimental results are shown in Figure la. The photochemical behavior of 12-F-rhodopsin at -191 O C (Figure lb) is similar to that of rhodopsin (Liu et al, 1981). Namely, on irradiation of 12-F-rhodopsin with 437-nm light at -191 OC, the spectrum shifted to longer wavelengths with an isosbestic point at 532 nm during the early stage of the irradiation, owing to the formation of a bathoproduct (batho-12-F-rhodopsin).…”

Section: Resultsmentioning

confidence: 71%

Electrostatic interaction between retinylidene chromophore and opsin in rhodopsin studied by fluorinated rhodopsin analogs

et al. 1987

Self Cite

View full text Add to dashboard Cite

Photochemical reactions of fluorinated rhodopsin analogues (F-rhodopsins) prepared from 10- or 12-fluorinated retinals (10- or 12-F-retinals) and cattle opsin were investigated by means of low-temperature spectrophotometry. On irradiation with blue light at liquid nitrogen temperature (-191 degrees C), the F-rhodopsins were converted to their respective batho intermediates. On warming, they decomposed to their respective fluororetinals and cattle opsin through lumi and meta intermediates. There was a difference in photochemical behavior between batho-12-F-rhodopsin and batho-10-F-rhodopsin. Upon irradiation with red light at -191 degrees C, batho-12-F-rhodopsin was converted to a mixture of 12-F-rhodopsin and 9-cis-12-F-rhodopsin like that of the natural bathorhodopsin, whereas batho-10-F-rhodopsin was not converted to 9-cis-10-F-rhodopsin but only to 10-F-rhodopsin. This fact suggests that the fluorine substituent at the C10 position (i.e., 10-fluoro) of the retinylidene chromophore may interact with the protein moiety during the process of isomerization of the chromophore or in the state of the batho intermediate. On irradiation with blue light at -191 degrees C, 9-cis-10-F-rhodopsin was converted to another bathochromic intermediate that was different in absorption spectrum from batho-10-F-rhodopsin. 9-cis-10-F-rhodopsin was practically "photoinsensitive" at liquid helium temperature (-265 degrees C), whereas 10-F-rhodopsin was converted to a photo-steady-state mixture of 10-F-rhodopsin and batho-10-F-rhodopsin. The specific interaction between the fluorine atom at the C10 position of the retinylidene chromophore and the opsin was discussed in terms of electrostatic interactions.

show abstract

Section: Resultsmentioning

confidence: 71%

Electrostatic interaction between retinylidene chromophore and opsin in rhodopsin studied by fluorinated rhodopsin analogs

et al. 1987

Self Cite

View full text Add to dashboard Cite

show abstract

“…For the preparation of flavonoid pigments, see: Fringuelli et al (1994). For sexual pheromones, see: Liu et al (1981). For the manufacture of light-emitting diodes (LEDs) with air-stable electrodes, see: Maruyama et al (1998); Segura et al (1999); Gó mez et al (1999).…”

Section: Related Literaturementioning

confidence: 99%

2,5-Diphenylpenta-2,4-dienenitrile

Archana¹,

Balamurugan²,

Manimekalai³

et al. 2009

Acta Cryst E

View full text Add to dashboard Cite

show abstract

“…An extended effort (26,28,29) led to compilation of the 19 F chemical shifts of 15 vinyl F-rhodopsin analogs. The corresponding PSBs were also prepared, and the F-shifts in solution were measured.…”

Section: Background Informationmentioning

confidence: 99%

The molecular basis for the high photosensitivity of rhodopsin

Liu

Colmenares

2003

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

Based on structural information derived from the F NMR data of labeled rhodopsins, rhodopsin crystal structure, and excited-state properties of model polyenes, we propose a molecular mechanism that accounts specifically for the causes of the well-known enhanced photoreactivity of rhodopsin (increased rates and quantum yield of isomerization). Rhodopsin is a heptahelical membrane protein responsible for scotopic vision. It is a photo-receptor protein activated by the 11-cis-retinal (1) (Structure 1) chromophore covalently bonded to Lys-296 through a protonated Schiff base (PSB) linkage. The photoisomerization of the chromophore initiates the vision process (1). The pigment is known to possess unusually high photochemical reactivity. For example, its quantum yield of isomerization is 0.65 (2, 3) (a recently refined value from the long accepted number of 0.67; ref. 4), more than two times higher than that of the same chromophore in solution (0.24, 0.22) (5, 6). The rate of isomerization is also much faster in protein (146 fsec) (7) than in solution (1-2 psec) (8). In this article, we propose a detailed molecular model accounting for the unusual protein assistance to the isomerization process. Background Information

show abstract

Synthesis and properties of 12-fluororetinal and 12-fluororhodopsin. Model system for fluorine-19 NMR studies of visual pigments

Cited by 77 publications

References 0 publications

Electrostatic interaction between retinylidene chromophore and opsin in rhodopsin studied by fluorinated rhodopsin analogs

Electrostatic interaction between retinylidene chromophore and opsin in rhodopsin studied by fluorinated rhodopsin analogs

2,5-Diphenylpenta-2,4-dienenitrile

The molecular basis for the high photosensitivity of rhodopsin

Contact Info

Product

Resources

About