Enantioselective binding of an 11-cis-locked cyclopropyl retinal. The conformation of retinal in bovine rhodopsin

Organic Letters

Volumn 1, Issue 1, 1999, Pages 51-54

  Lou, Jihong ^a   Hashimoto, Masaru ^a,b   Berova, Nina ^a   Nakanishi, Koji ^a  

^a Och Spine at New York Presbyterian Hospitals   (United States)

^b HIROSAKI UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

4 (2 ((1,3,3 TRIMETHYLCYCLOHEXEN 2 YL)ETHENYL)PROPYLIDENE) 2,3 METHYLENECYCLOHEPT 1 YLMETHYLENEMETHANAL; 4-(2-((1,3,3-TRIMETHYLCYCLOHEXEN-2-YL)ETHENYL)PROPYLIDENE)-2,3-METHYLENECYCLOHEPT-1-YLMETHYLENEMETHANAL; BICYCLO COMPOUND; DRUG DERIVATIVE; RETINAL; RHODOPSIN;

ANIMAL; ARTICLE; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; CONFORMATION; PROTEIN BINDING; STEREOISOMERISM; ULTRAVIOLET SPECTROPHOTOMETRY;

ANIMALS; BICYCLO COMPOUNDS; CATTLE; CIRCULAR DICHROISM; MODELS, MOLECULAR; MOLECULAR CONFORMATION; PROTEIN BINDING; RETINALDEHYDE; RHODOPSIN; SPECTROPHOTOMETRY, ULTRAVIOLET; STEREOISOMERISM;

EID: 0033565019     PISSN: 15237060     EISSN: None     Source Type: Journal    
DOI: 10.1021/ol990048l     Document Type: Article

References (39)

1. (a) Sakmar, T. P. Prog. Nucl. Acid Res. Mol. Biol. 1998, 59, 1.
2. (b) Watson, S.; Atkinstall, S. The G-Protein Linked Receptor Facts Book; Academic: London, San Diego, 1994.
3. (c) Gudermann, T.; Nurnbeg, B.; Schultz, G. J. Mol. Med. 1995, 73, 51.
4. For reviews, see: (a) Photophysics and Photochemistry of Retinal Proteins. Isr. J. Chem. 1995, 35, special issue,
5. (b) Nakanishi, K.; Crouch, R. Isr. J. Chem. 1995, 35, 253.
6. (a) Yoshizawa, T.; Wald, G. Nature 1963, 197, 1279.
7. (b) Bownds, D. Nature 1967, 216, 1178.
8. (c) Wald, G. Nature 1968, 219, 800.
9. (d) Schertler, G. F. X.; Villa, C.; Henderson, R. Nature 1993, 362, 770.
10. (a) Chan, W. K.; Nakanishi, K.; Ebrey, T. G.; Honig, B. J. Am. Chem. Soc. 1974, 96, 3642.
11. (b) For review, see: Rando, R. R. Chem. Biol. 1996, 3, 255.
12. (a) Konig, B.; Arendt, A.; McDowell, J. H.; Kohlert, M.; Hargrave, P. A.; Hofmann, K. P. Proc. Natl. Acad. Sci. U.S.A. 1989, 86, 6878.
13. (b) Stryer, L. J. Biol. Chem. 1991, 266, 1071.
14. (c) Hargrave, P. A.; McDowell, J. H. FASEB J. 1992, 6, 2323.
15. (d) Khorana, H. G. J. Biol. Chem. 1992, 26, 1.
16. (e) Nathans, J. Biochemistry 1992, 31, 4923.
17. Borhan, B.; Souto, M. L.; Nakanishi, K, in preparation.
18. (a) Nakanishi, K. Am. Zool. 1991, 31, 479.
19. (b) Nakanishi, K. Pure Appl. Chem. 1991, 63, 161.
20. (c) Yoshizawa, T. Biophys. Chem. 1994, 50, 17.
21. (a) Fukada, Y.; Shichida, Y.; Yoshizawa, T.; Ito, M.; Kodama, A.; Tsukida, K. Biochemistry 1984, 23, 5826.
22. (b) Ito, M.; Hiroshima, T.; Tsukida, K.; Shichida, Y.; Yoshizawa, T. J. Chem. Soc., Chem. Commun. 1985, 1443.
23. (c) Katsuta, Y.; Sakai, M.; Ito, M. J. Chem. Soc., Perkin Trans. 1 1993, 2185.
24. (d) Ito, M.; Katsuta, Y.; Imamoto, Y.; Shichida, Y.; Yoshizawa, T. Photochem. Photobiol. 1992, 56, 915.
25. Tan, Q.; Lou, J.; Borhan, B.; Karnaukhova, E.; Berova, N.; Nakanishi, K. Angew. Chem., Int. Ed. Engl. 1997, 36, 2089.
26. Nakanishi, K.; Berova, N. In Circular Dichroism: Principles and Applications; Nakanishi, K., Berova, N., Woody, R. W., Eds.; VCH Publishers: 1994; pp 361-398.
27. (a) Kakitani, H.; Kakitani, T.; Yomosa, S. J. Phys. Soc. Jpn. 1977, 42, 996.
28. (b) Han, M.; Smith, S. O. Biochemistry 1995, 34, 1425; 1997, 36, 7280.
29. (b) Han, M.; Smith, S. O. Biochemistry 1995, 34, 1425; 1997, 36, 7280.
30. Buss, V.; Kolster, K.; Terstegen, F.; Vahrenhorst, R. Angew. Chem., Int. Ed. Engl. 1998, 37, 1893.
31. Akita, H.; Tanis, S. P.; Adams, M.; Balogh-Nair, V.; Nakanishi, K. J. Am. Chem. Soc. 1980, 102, 6370.
32. (a) Johnson, C. R.; Bis, S. J. Tetrahedron Lett. 1992, 33, 7287.
33. (b) Pearson, A. J.; Lai, Y. S.; Lu, W.; Pinkerton, A. A. J. Org. Chem. 1989, 54, 3882.
34. 1H NMR of its MPA ester derivatives. The optical rotation value of 6 agrees with literature value (see ref 14).
35. (b) The cis geometry between hydroxyl group and cyclopropyl ring in 7 was confirmed by NOESY, HMQC, and COSY NMR experiments.
36. A stock solution of opsin in 10 mM CHAPSO/HEPES buffer (pH 7.0) was added to a pair of UV cuvettes (1 mL solution each), and the background of the UV spectrometer was scanned. A solution of retinal analogue 2 or 3 in EtOH (5 μL) was added to the sample cuvette, and 5 μL of EtOH was added to the control cuvette; UV were measured every 10 min over a 1 h period. The initial band (taken within 1 min of mixing) in UV corresponds to unbound retinal analogues in buffer. The binding of chromophore to opsin is accompanied by a decrease in the intensity of the unbound chromophore band and a growth of a new band at longer wavelength corresponding to PSB formation. Unchanged UV indicates that the chromophore remains unbound throughout the whole period. The binding of 2 was further confirmed by incubating the pigment with 11-cis-retinal. No new band at 500 nm in UV/vis was detected, suggesting that the retinal binding site was occupied by 2.
37. Litman, B. J. Methods Enzymol. 1982, 81, 150.
38. (a) Nakanishi, K.; Yudd, A. P.; Crouch, R. K.; Olson, G. L.; Cheung, H. C.; Govindjee, R.; Ebrey, T. G.; Patel, D. J. J. Am. Chem. Soc. 1976, 98, 236.
39. (b) Blatchly, R. A.; Carriker, J. D.; Balogh-Nair, V.; Nakanishi, K. J. Am. Chem. Soc. 1980, 102, 2495.