Solid-state NMR studies of the mechanism of the opsin shift in the visual pigment rhodopsin.
作者： Steven O. Smith , Ilona Palings , Mary E. Miley , Jacques Courtin , Huub De Groot
DOI: 10.1021/BI00487A025
关键词:
摘要: Solid-state 13C NMR spectra have been obtained of bovine rhodopsin and isorhodopsin regenerated with retinal selectively labeled along the polyene chain. In rhodopsin, chemical shifts for 13C-5, 13C-6, 13C-7, 13C-14, 13C-15 correspond closely to observed in 11-cis protonated Schiff base (PSB) model compound. Differences shift relative PSB chloride salt are positions 8 through 13, largest deshielding (6.2 ppm) localized at position 13. The C-13 supports previous models opsin that place a protein perturbation vicinity Spectra 13C-labeled 9-cis-retinals reveal large perturbations 13C-7 13C-13. similar 13C-13 resonance both pigments presence near However, 7 12 not analogous those suggest binding site interactions these different two pigments. implications results mechanism proteins discussed.
acs.org
sci-hub.se 参考文章(42)
Gerard S. Harbison, Steven O. Smith, Johannes A. Pardoen, Patrick P. J. Mulder, Johan Lugtenburg, Judith Herzfeld, Richard Mathies, Robert G. Griffin, Solid-state 13C NMR studies of retinal in bacteriorhodopsin. Biochemistry. ,vol. 23, pp. 2662- 2667 ,(1984) , 10.1021/BI00307A019
J. Lugtenburg, The synthesis of 13 C-labelled retinals Pure and Applied Chemistry. ,vol. 57, pp. 753- 762 ,(1985) , 10.1351/PAC198557050753
J. A. Pardoen, C. Winkel, P. P. J. Mulder, J. Lugtenburg, Synthesis of retinals labelled at positions 14 and 15 (with 13C and/or 2H) Recueil des Travaux Chimiques des Pays-Bas. ,vol. 103, pp. 135- 141 ,(2010) , 10.1002/RECL.19841030408
Judith Herzfeld, Alan E. Berger, Sideband intensities in NMR spectra of samples spinning at the magic angle Journal of Chemical Physics. ,vol. 73, pp. 6021- 6030 ,(1980) , 10.1063/1.440136
Johan Lugtenburg, Maria Muradin-Szweykowska, Carola Heeremans, Johannes A Pardoen, None, Mechanism for the opsin shift of retinal's absorption in bacteriorhodopsin Journal of the American Chemical Society. ,vol. 108, pp. 3104- 3105 ,(1986) , 10.1021/JA00271A050
G. S. Harbison, S. O. Smith, J. A. Pardoen, C. Winkel, J. Lugtenburg, J. Herzfeld, R. Mathies, R. G. Griffin, Dark-adapted bacteriorhodopsin contains 13-cis, 15-syn and all-trans, 15-anti retinal Schiff bases Proceedings of the National Academy of Sciences of the United States of America. ,vol. 81, pp. 1706- 1709 ,(1984) , 10.1073/PNAS.81.6.1706
G. S. Harbison, S. O. Smith, J. A. Pardoen, J. M. L. Courtin, J. Lugtenburg, J. Herzfeld, R. A. Mathies, R. G. Griffin, Solid-state 13C NMR detection of a perturbed 6-s-trans chromophore in bacteriorhodopsin. Biochemistry. ,vol. 24, pp. 6955- 6962 ,(1985) , 10.1021/BI00345A031
Ronald F. Childs, Gary S. Shaw, Roderick E. Wasylishen, Solid-state studies of some retinal iminium salts and related compounds: evidence for a 6-s-trans conformation Journal of the American Chemical Society. ,vol. 109, pp. 5362- 5366 ,(1987) , 10.1021/JA00252A010
Paul E. Blatz, Jonathan H. Mohler, Himanshoo V. Navangul, Anion-induced wavelength regulation of absorption maxima of Schiff bases of retinal Biochemistry. ,vol. 11, pp. 848- 855 ,(1972) , 10.1021/BI00755A026
Steven O. Smith, Ilona Palings, Valerie Copie, Daniel P. Raleigh, Jacques Courtin, Johannes A. Pardoen, Johan Lugtenburg, Richard A. Mathies, Robert G. Griffin, Low-temperature solid-state 13C NMR studies of the retinal chromophore in rhodopsin. Biochemistry. ,vol. 26, pp. 1606- 1611 ,(1987) , 10.1021/BI00380A018