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Light isomerizes the chromophore of bacteriorhodopsin

Nature volume 287, pages 351–353 (1980)Cite this article

Abstract

The primary photochemical event in the two light-transducing pigments whose chromophore is retinal, rhodopsin or bacteriorhodopsin, is a source of controversy. It was originally proposed that the primary photoevent in the bleaching of rhodopsin is the photoisomerization of the chromophore from 11-cis to all-trans retinal1,2. Photochemical considerations suggested that a photoisomerization is the primary event in both rhodopsin and bacteriorhodopsin3–7. However, this description of bacteriorhodopsin's photochemistry has been questioned8–10. To elucidate this problem, we determined the isomeric conformation of retinal for two of the photolytic intermediates of bacteriorhodopsin, using a method that enables us to extract chromophores from the photocycle intermediates L and M at low temperatures (−74 °C), and have determined the isomeric conformation of the extracted retinals by HPLC11,12. Here we provide direct evidence that isomerization of the chromophore has taken place in two of the early photocycle intermediates (L and M) of bacteriorhodopsin.

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Author notes

  1. Motoyuki Tsuda: Department of Physics, Sapporo Medical College, Sapporo, Japan

  2. Moira Glaccum: Department of Genetics, Stanford University School of Medicine, Stanford, California 94305.

Authors and Affiliations

  1. Department of Physiology and Biophysics, 524 Burrill Hall, University of Illinois, Urbana, Illinois, 61801

    Motoyuki Tsuda, Moira Glaccum, Burr Nelson & Thomas G. Ebrey

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  1. Motoyuki Tsuda
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  3. Burr Nelson
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Tsuda, M., Glaccum, M., Nelson, B. et al. Light isomerizes the chromophore of bacteriorhodopsin. Nature 287, 351–353 (1980). https://doi.org/10.1038/287351a0

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