Abstract
Bovine rhodopsin and isorhodopsin were excited with a single 530-nm, 7-ps light pulse emitted by a mode-locked Nd 3+ glass laser at room temperature. Within 3 ps of excitation, absorbance changes due to formation of bathorhodopsin were observed. The difference spectra generated during and 100 ps after pulse excitation are presented. The data show that bathorhodopsin formation is completed within 3 ps for both the primary pigments and suggest that a single common bathorhodopsin is photochemically formed from both primary pigments. Our findings provide additional support for the cis-trans isomerization model of the primary event in vision. Additional absorption transients that were observed near 670 and 460 nm are discussed.
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- Applebury M. L., Peters K. S., Rentzepis P. M. Primary intermediates in the photochemical cycle of bacteriorhodopsin. Biophys J. 1978 Sep;23(3):375–382. doi: 10.1016/S0006-3495(78)85456-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Applebury M. L., Zuckerman D. M., Lamola A. A., Jovin T. M. Rhodopsin. Purification and recombination with phospholipids assayed by the metarhodopsin I leads to metarhodopsin II transition. Biochemistry. 1974 Aug 13;13(17):3448–3458. doi: 10.1021/bi00714a005. [DOI] [PubMed] [Google Scholar]
- Aton B., Callender R. H., Honig B. Photochemical cis-trans isomerisation of bovine rhodopsin at liquid helium temperatures. Nature. 1978 Jun 29;273(5665):784–786. doi: 10.1038/273784a0. [DOI] [PubMed] [Google Scholar]
- Busch G. E., Applebury M. L., Lamola A. A., Rentzepis P. M. Formation and decay of prelumirhodopsin at room temperatures. Proc Natl Acad Sci U S A. 1972 Oct;69(10):2802–2806. doi: 10.1073/pnas.69.10.2802. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ebrey T. G., Honig B. Molecular aspects of photoreceptor function. Q Rev Biophys. 1975 May;8(2):129–184. doi: 10.1017/s0033583500001785. [DOI] [PubMed] [Google Scholar]
- Eyring G., Mathies R. Resonance Raman studies of bathorhodopsin: evidence for a protonated Schiff base linkage. Proc Natl Acad Sci U S A. 1979 Jan;76(1):33–37. doi: 10.1073/pnas.76.1.33. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Goldschmidt C. R., Ottolenghi M., Rosenfeld T. Primary processes in photochemistry of rhodopsin at room temperature. Nature. 1976 Sep 9;263(5573):169–171. doi: 10.1038/263169a0. [DOI] [PubMed] [Google Scholar]
- Green B. H., Monger T. G., Alfano R. R., Aton B., Callender R. H. Cis-trans isomerisation in rhodopsin occurs in picoseconds. Nature. 1977 Sep 8;269(5624):179–180. doi: 10.1038/269179a0. [DOI] [PubMed] [Google Scholar]
- Hong K., Hubbell W. L. Lipid requirements for Rhodopsin regenerability. Biochemistry. 1973 Oct 23;12(22):4517–4523. doi: 10.1021/bi00746a033. [DOI] [PubMed] [Google Scholar]
- Honig B., Ebrey T. G. The structure and spectra of the chromophore of the visual pigments. Annu Rev Biophys Bioeng. 1974;3(0):151–177. doi: 10.1146/annurev.bb.03.060174.001055. [DOI] [PubMed] [Google Scholar]
- Hubbard R., Kropf A. THE ACTION OF LIGHT ON RHODOPSIN. Proc Natl Acad Sci U S A. 1958 Feb;44(2):130–139. doi: 10.1073/pnas.44.2.130. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hurley J. B., Ebrey T. G., Honig B., Ottolenghi M. Temperature and wavelength effects on the photochemistry of rhodopsin, isorhodopsin, bacteriorhodopsin and their photoproducts. Nature. 1977 Dec 8;270(5637):540–542. doi: 10.1038/270540a0. [DOI] [PubMed] [Google Scholar]
- Oseroff A. R., Callender R. H. Resonance Raman spectroscopy of rhodopsin in retinal disk membranes. Biochemistry. 1974 Sep 24;13(20):4243–4248. doi: 10.1021/bi00717a027. [DOI] [PubMed] [Google Scholar]
- Peters K., Applebury M. L., Rentzepis P. M. Primary photochemical event in vision: proton translocation. Proc Natl Acad Sci U S A. 1977 Aug;74(8):3119–3123. doi: 10.1073/pnas.74.8.3119. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rosenfeld T., Alchalal A., Ottolenghi M. Nanosecond laser photolysis of rhodopsin in solution. Nature. 1972 Dec 22;240(5382):482–483. doi: 10.1038/240482a0. [DOI] [PubMed] [Google Scholar]
- Wald G. Molecular basis of visual excitation. Science. 1968 Oct 11;162(3850):230–239. doi: 10.1126/science.162.3850.230. [DOI] [PubMed] [Google Scholar]
- YOSHIZAWA T., WALD G. Pre-lumirhodopsin and the bleaching of visual pigments. Nature. 1963 Mar 30;197:1279–1286. doi: 10.1038/1971279a0. [DOI] [PubMed] [Google Scholar]
- van der Meer K., Mulder J. J., Lugtenburg J. A new facet in rhodopsin photochemistry. Photochem Photobiol. 1976 Oct;24(4):363–367. doi: 10.1111/j.1751-1097.1976.tb06837.x. [DOI] [PubMed] [Google Scholar]