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. 1989 Jan;55(1):193–196. doi: 10.1016/S0006-3495(89)82791-2

Halorhodopsin and sensory rhodopsin contain a C6-C7 s-trans retinal chromophore.

D R Baselt 1, S P Fodor 1, R van der Steen 1, J Lugtenburg 1, R A Bogomolni 1, R A Mathies 1
PMCID: PMC1330454  PMID: 2930820

Abstract

Halorhodopsin (HR) and sensory rhodopsin (SR) have been regenerated with retinal analogues that are covalently locked in the 6-s-cis or 6-s-trans conformations. Both pigments regenerate more completely with the locked 6-s-trans retinal and produce analogue pigments with absorption maxima (577 nm for HR and 592 nm for SR) nearly identical to those of the native pigments (577 and 587 nm). This indicates that HR and SR bind retinal in the 6-s-trans conformation. The opsin shift for the locked 6-s-trans analogue in HR is 1,200 cm-1 less than that for the native chromophore (5,400 cm-1). The opsin shift for the 6-s-trans analogue in SR is 1,100 cm-1 less than that for the native retinal (5,700 cm-1). This demonstrates that approximately 20% of the opsin shift in these pigments arises from a protein-induced change in the chromophore conformation from twisted 6-s-cis in solution to planar 6-s-trans in the protein. The reduced opsin shift observed for the locked 6-s-cis analogue pigments compared with the locked 6-s-trans pigments may be due to a positive electrostatic perturbation near C7.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Fodor S. P., Bogomolni R. A., Mathies R. A. Structure of the retinal chromophore in the hRL intermediate of halorhodopsin from resonance raman spectroscopy. Biochemistry. 1987 Oct 20;26(21):6775–6778. doi: 10.1021/bi00395a029. [DOI] [PubMed] [Google Scholar]
  2. Fodor S. P., Pollard W. T., Gebhard R., van den Berg E. M., Lugtenburg J., Mathies R. A. Bacteriorhodopsin's L550 intermediate contains a C14-C15 s-trans-retinal chromophore. Proc Natl Acad Sci U S A. 1988 Apr;85(7):2156–2160. doi: 10.1073/pnas.85.7.2156. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Harbison G. S., Herzfeld J., Griffin R. G. Solid-state nitrogen-15 nuclear magnetic resonance study of the Schiff base in bacteriorhodopsin. Biochemistry. 1983 Jan 4;22(1):1–4. doi: 10.1021/bi00270a600. [DOI] [PubMed] [Google Scholar]
  4. Harbison G. S., Smith S. O., Pardoen J. A., Courtin J. M., Lugtenburg J., Herzfeld J., Mathies R. A., Griffin R. G. Solid-state 13C NMR detection of a perturbed 6-s-trans chromophore in bacteriorhodopsin. Biochemistry. 1985 Nov 19;24(24):6955–6962. doi: 10.1021/bi00345a031. [DOI] [PubMed] [Google Scholar]
  5. Honig B., Greenberg A. D., Dinur U., Ebrey T. G. Visual-pigment spectra: implications of the protonation of the retinal Schiff base. Biochemistry. 1976 Oct 19;15(21):4593–4599. doi: 10.1021/bi00666a008. [DOI] [PubMed] [Google Scholar]
  6. Honig B., Hudson B., Sykes B. D., Karplus M. Ring orientation in -ionone and retinals. Proc Natl Acad Sci U S A. 1971 Jun;68(6):1289–1293. doi: 10.1073/pnas.68.6.1289. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Lanyi J. K. Halorhodopsin: a light-driven chloride ion pump. Annu Rev Biophys Biophys Chem. 1986;15:11–28. doi: 10.1146/annurev.bb.15.060186.000303. [DOI] [PubMed] [Google Scholar]
  8. Smith S. O., Marvin M. J., Bogomolni R. A., Mathies R. A. Structure of the retinal chromophore in the hR578 form of halorhodopsin. J Biol Chem. 1984 Oct 25;259(20):12326–12329. [PubMed] [Google Scholar]
  9. Spudich J. L., Bogomolni R. A. Mechanism of colour discrimination by a bacterial sensory rhodopsin. Nature. 1984 Dec 6;312(5994):509–513. doi: 10.1038/312509a0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Spudich J. L., Bogomolni R. A. Sensory rhodopsins of halobacteria. Annu Rev Biophys Biophys Chem. 1988;17:193–215. doi: 10.1146/annurev.bb.17.060188.001205. [DOI] [PubMed] [Google Scholar]
  11. Spudich J. L., Bogomolni R. A. Spectroscopic discrimination of the three rhodopsinlike pigments in Halobacterium halobium membranes. Biophys J. 1983 Aug;43(2):243–246. doi: 10.1016/S0006-3495(83)84345-8. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Spudich J. L., McCain D. A., Nakanishi K., Okabe M., Shimizu N., Rodman H., Honig B., Bogomolni R. A. Chromophore/protein interaction in bacterial sensory rhodopsin and bacteriorhodopsin. Biophys J. 1986 Feb;49(2):479–483. doi: 10.1016/S0006-3495(86)83657-8. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Stoeckenius W., Bogomolni R. A. Bacteriorhodopsin and related pigments of halobacteria. Annu Rev Biochem. 1982;51:587–616. doi: 10.1146/annurev.bi.51.070182.003103. [DOI] [PubMed] [Google Scholar]
  14. Taylor M. E., Bogomolni R. A., Weber H. J. Purification of photochemically active halorhodopsin. Proc Natl Acad Sci U S A. 1983 Oct;80(20):6172–6176. doi: 10.1073/pnas.80.20.6172. [DOI] [PMC free article] [PubMed] [Google Scholar]

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