Thermal decay of rhodopsin: Role of hydrogen bonds in thermal isomerization of 11-cis retinal in the binding site and hydrolysis of protonated Schiff base

Journal of the American Chemical Society

Volumn 131, Issue 25, 2009, Pages 8750-8751

  Liu, Jian ^a   Liu, Monica Yun ^a   Nguyen, Jennifer B ^a   Bhagat, Aditi ^a   Mooney, Victoria ^a   Yan, Elsa C Y ^a  

^a YALE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADRENERGIC RECEPTORS; BINDING POCKETS; DARK NOISE; DEUTERIUM ISOTOPE EFFECT; G PROTEIN COUPLED RECEPTORS; HPLC ANALYSIS; HYDROGEN BONDING NETWORK; PROTONATED SCHIFF BASE; RATE DETERMINING STEP; THERMAL DECAYS; THERMAL ISOMERIZATION; THERMAL STABILITY; UV-VIS SPECTROSCOPY;

BINDING ENERGY; BINDING SITES; CIRCULAR DICHROISM SPECTROSCOPY; DEUTERIUM; DICHROISM; ELECTRON TRANSITIONS; HYDROGEN; HYDROLYSIS; ISOMERIZATION; ISOMERS; OPHTHALMOLOGY; STRUCTURAL ANALYSIS; THERMODYNAMIC STABILITY; ULTRAVIOLET SPECTROSCOPY;

HYDROGEN BONDS;

11 CIS RETINAL; RHODOPSIN; SCHIFF BASE;

ARTICLE; BINDING SITE; CHEMICAL REACTION KINETICS; CHROMATOPHORE; CONTROLLED STUDY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROGEN BOND; HYDROLYSIS; ISOMERIZATION; OPTICAL DENSITY; PROTEIN DEGRADATION; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; ULTRAVIOLET SPECTROSCOPY;

ANIMALS; BINDING SITES; HYDROGEN BONDING; HYDROLYSIS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; RETINALDEHYDE; RHODOPSIN; SCHIFF BASES; TEMPERATURE;

EID: 67649628230     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja903154u     Document Type: Article

References (16)

1. Menon, S. T.; Han, M.; Sakmar, T. P. Physiol. Rev. 2001, 81, 1659-1688.
2. Barlow, R. B.; Birge, R. R.; Kaplan, E.; Tallent, J. R. Nature 1993, 366, 64-66.
3. Aho, A. C.; Donner, K.; Hyden, C.; Larsen, L. O.; Reuter, T. Nature 1988, 334, 348-350.
4. Birge, R. R.; Barlow, R. B. Biophys. Chem. 1995, 55, 115-126.
5. Baylor, D.; Matthews, G.; Yau, K.-W. J. Physiol. 1980, 309, 591-621.
6. Baylor, D. A.; Nunn, B. J.; Schnapf, J. L. J. Physiol. 1984, 357, 575-607.
7. Janz, J. M.; Farrens, D. L. J. Biol. Chem. 2004, 279, 55886-55894.
8. Janz, J. M.; Fay, J. F.; Farrens, D. L. J. Biol. Chem. 2003, 278, 16982-16991.
9. Del Valle, L. J.; Ramon, E.; Bosch, L.; Manyosa, J.; Garriga, P. Cell. Mol. Life Sci. 2003, 60, 2532-2537.
10. Okada, T.; Fujiyoshi, Y.; Silow, M.; Navarro, J.; Landau, E. M.; Shichida, Y. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 5982-5987.
11. Yan, E. C. Y.; Kazmi, M. A.; Ganim, Z.; Hou, J. M.; Pan, D.; Chang, B. S. W.; Sakmar, T. P.; Mathies, R. A. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 9262-9267.
12. Yan, E. C. Y.; Epps, J.; Lewis, J. W.; Szundi, I.; Bhagat, A.; Sakmar, T. P.; Kliger, D. S. J. Phys. Chem. C 2007, 111, 8843-8848.
13. Tsutsui, K.; Imai, H.; Shichida, Y. Biochemistry 2007, 46, 6437-6445.
14. Crescitelli, F.; Mommaerts, W. F. H. M.; Shaw, T. I. Proc. Natl. Acad. Sci. U.S.A. 1966, 56, 1729-1734.
15. Legon, A. C.; Millen, D. J. Chem. Phys. Lett. 1988, 147, 484-489.
16. Li, J.; Edwards, P. C.; Burghammer, M.; Villa, C.; Schertler, G. F. J. Mol. Biol. 2004, 343, 1409-1438.