Mechanism of Transient Dark Activity of 13-Desmethylretinal/Rod Opsin Complex

We report the studies employing 11-cis-13-desmethylretinal (13dm) 1, its dihydro analogue 2H13dm 2, and 11-cis sixmembered ring-locked analogue ret6 3, to clarify the mechanism of dark activity of the 13-desmethylretinal/rod opsin complex. Rhodopsin (Rh) is composed of a retinal chromophore linked to Lys 296 of the apoprotein opsin via a protonated Schiff base (PSB).1 Light-induced retinal 11-cis f trans isomerization triggers protein conformational changes leading to metarhodopsin II (Meta-II) which activates the G-protein transducin to initiate the enzymatic cascade of visual transduction.2 Phosphorylation of Meta-II by rhodopsin kinase and subsequent binding of arrestin deactivate Meta-II.3 Recently it has been observed that opsin can be activated by retinal analogues including all-trans-retinal, all-trans-13dm 4, alltrans-C15 5, and â-ionone 6 in the absence of light.4 Dark activity

[1]  Susan Band Horwitz,et al.  Structure–Activity Relationship of the Epothilones and the First In Vivo Comparison with Paclitaxel† , 1997 .

[2]  Akinori Kidera,et al.  Surface of bacteriorhodopsin revealed by high-resolution electron crystallography , 1997, Nature.

[3]  Gebhard F. X. Schertler,et al.  Arrangement of rhodopsin transmembrane α-helices , 1997, Nature.

[4]  K. Palczewski,et al.  Activation and inactivation steps in the visual transduction pathway , 1997, Current Opinion in Neurobiology.

[5]  K. Fahmy,et al.  Spectroscopic evidence for altered chromophore--protein interactions in low-temperature photoproducts of the visual pigment responsible for congenital night blindness. , 1996, Biochemistry.

[6]  K. Palczewski,et al.  Mechanisms of Opsin Activation* , 1996, The Journal of Biological Chemistry.

[7]  K. Hofmann,et al.  Opsin/all-trans-retinal complex activates transducin by different mechanisms than photolyzed rhodopsin. , 1996, Biochemistry.

[8]  G. Fain,et al.  Bleached pigment activates transduction in salamander cones , 1995, The Journal of general physiology.

[9]  K. Palczewski,et al.  Rod outer segment retinol dehydrogenase: substrate specificity and role in phototransduction. , 1994, Biochemistry.

[10]  E. MacNichol,et al.  Relief of opsin desensitization and prolonged excitation of rod photoreceptors by 9-desmethylretinal. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[11]  D. Oprian,et al.  Mechanism of activation and inactivation of opsin: role of Glu113 and Lys296. , 1992, Biochemistry.

[12]  J. Nathans,et al.  Rhodopsin: structure, function, and genetics. , 1992, Biochemistry.

[13]  S. Martinis,et al.  RNA tetraloops as minimalist substrates for aminoacylation. , 1992, Biochemistry.

[14]  P. Detwiler,et al.  The influence of arrestin (48K protein) and rhodopsin kinase on visual transduction , 1992, Neuron.

[15]  H. Khorana.  Rhodopsin, photoreceptor of the rod cell. An emerging pattern for structure and function. , 1992, The Journal of biological chemistry.

[16]  L. Stryer.  Visual excitation and recovery. , 1991, The Journal of biological chemistry.

[17]  H. Khorana,et al.  Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[18]  W. Zimmerman,et al.  Preparation and characterization of sealed bovine rod cell outer segments. , 1982, Methods in enzymology.

[19]  J. West,et al.  Light activation of bovine rod phosphodiesterase by non‐physiological visual pigments , 1980, FEBS letters.

[20]  L. Salem,et al.  Conversion of a photon to an electrical signal by sudden polarisation in the N-retinylidene visual chromophore , 1975, Nature.

[21]  T. Yoshizawa,et al.  Existence of a β-ionone ring-binding site in the rhodopsin molecule , 1975, Nature.

[22]  J. Dawes,et al.  Phosphorylation of frog photoreceptor membranes induced by light. , 1972, Nature: New biology.

[23]  G. Wald.  The Molecular Basis of Visual Excitation , 1968, Nature.

[24]  G. Wald,et al.  Pre-Lumirhodopsin and the Bleaching of Visual Pigments , 1963, Nature.