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Protein Dynamics Preceding Photoisomerization of the Retinal Chromophore in Bacteriorhodopsin Revealed by Deep-UV Femtosecond Stimulated Raman Spectroscopy

Journal of Physical Chemistry Letters, ISSN: 1948-7185, Vol: 10, Issue: 18, Page: 5422-5427
2019
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Protein changes precede photoisomerization of retinal chromophore

The sequence of changes that light triggers in a bacterial photoreceptor starts with its protein scaffolding rather than the light-absorbing chromophore, an all-RIKEN team has shown. This finding goes against conventional wisdom and sheds new light on how photoreceptors can convert light into chemical energy so efficiently.

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Bacteriorhodopsin is a prototypical photoreceptor protein that functions as a light-driven proton pump. The retinal chromophore of bacteriorhodopsin undergoes C=C trans-to-cis isomerization upon photoexcitation, and it has been believed to be the first event that triggers the cascaded structural changes in bacteriorhodopsin. We investigated the protein dynamics of bacteriorhodopsin using deep-ultraviolet resonance femtosecond stimulated Raman spectroscopy. It was found that the stimulated Raman signals of tryptophan and tyrosine residues exhibit significant changes within 0.2 ps after photoexcitation while they do not noticeably change during the isomerization process. This result implies that the protein environment changes first, and its change is small during isomerization. The obtained femtosecond stimulated Raman data indicate that ultrafast change is induced in the protein part by the sudden creation of the large dipole of the excited-state chromophore, providing an environment that realizes efficient and selective isomerization.

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