THE ‘OPSIN SHIFT’ IN BACTERIORHODOPSIN: STUDIES WITH ARTIFICIAL BACTERIORHODOPSINS
- 1 April 1981
- journal article
- Published by Wiley in Photochemistry and Photobiology
- Vol. 33 (4) , 483-488
- https://doi.org/10.1111/j.1751-1097.1981.tb05449.x
Abstract
Abstract— The difference (in cm−1) in absorption maxima between the protonated Schiff base of retinals and the pigment derived therefrom has been defined as the opsin shift. It represents the influence of the opsin binding site on the chromophore. The analysis of the opsin shifts of a series of dihydrobacteriorhodopsins has led to the external point‐charge model, which in addition to a counter anion near the Schiff base ammonium, carries another negative charge in the vicinity of the β‐ionone ring. This is in striking contrast to the external point‐charge model proposed earlier for the bovine visual pigment. The absorption maxima of rhodopsins formed from bromo‐ and phenyl retinals support the two models. A retinal carrying a photoaffinity label has yielded a nonbleachable bacteriorhodopsin.Keywords
This publication has 19 references indexed in Scilit:
- Path of the polypeptide in bacteriorhodopsin.Proceedings of the National Academy of Sciences, 1980
- Hydroretinals and hydrorhodopsinsJournal of the American Chemical Society, 1979
- An external point-charge model for wavelength regulation in visual pigmentsJournal of the American Chemical Society, 1979
- Photoaffinity Labeling of Biological SystemsAnnual Review of Biochemistry, 1979
- Partial primary structure of bacteriorhodopsin: sequencing methods for membrane proteins.Proceedings of the National Academy of Sciences, 1979
- THE PURPLE MEMBRANE FROM HALOBACTERIUM HALOBIUMAnnual Review of Biophysics and Bioengineering, 1977
- Photoreceptor protein from the purple membrane of Halobacterium halobium. Molecular weight and retinal binding siteBiochemistry, 1976
- Effect of selected anions and solvents on the electronic absorption, nuclear magnetic resonance, and infrared spectra of the N-retinylidenebutylammonium cationBiochemistry, 1975
- Ring Orientation in βIonone and RetinalsProceedings of the National Academy of Sciences, 1971
- N-retinylidene-1-amino-2-propanol: A Schiff base analog for rhodopsinVision Research, 1968