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Biophysics

A cold break for photoreceptors

Nature volume 392, pages 131–133 (1998)Cite this article

Bacteria, plants and animals all perceive light using photoreceptors, each of which carries a bound, organic molecule known as a chromophore. When hit by a photon, the chromophore undergoes an apparently simple reaction — a cis-to-trans isomerization around a double bond. Light-perception by the chromophore is ultra-fast, taking only a few hundred femtoseconds. But the ensuing structural changes of the chromophore and its protein environment are thermally driven and much slower. For example, it takes more than 108 times longer for a photoreceptor to reach its signalling state, generate a cellular signal and, finally, to complete the ‘photocycle’ by returning to its original state.

How do these photoreceptors translate femtosecond events into millisecond responses so efficiently? In the atomic-resolution study reported by Genick et al.1 on page 206 of this issue, we get a first impression of a biological photoreceptor that has been trapped very shortly after excitation. The authors studied the photoactive yellow protein (PYP), which was discovered in the halophilic bacterium Ectothiorhodospira halophila2. There, as well as in other phototrophic purple bacteria, PYP serves as a light sensor which, presumably, mediates the negatively phototactic response of these bacteria to blue light.

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Figure 1: Chromophores from different photoreceptors.
Figure 2: Energy diagrams for the photoisomerization of 1,2-disubstituted ethenes.

References

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Authors and Affiliations

  1. the Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, Martinsried bei München, D-82152, Germany

    Lars-Oliver Essen & Dieter Oesterhelt

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  1. Lars-Oliver Essen
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  2. Dieter Oesterhelt
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Essen, LO., Oesterhelt, D. A cold break for photoreceptors. Nature 392, 131–133 (1998). https://doi.org/10.1038/32294

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