Barrierless Photoisomerization of 11-cis Retinal Protonated Schiff Base in Solution

Giovanni Bassolino; Tina Sovdat; Alex Soares Duarte; Jong Min Lim; Christoph Schnedermann; Matz Liebel; Barbara Odell; Timothy D.W. Claridge; Stephen P. Fletcher; Philipp Kukura

doi:10.1021/jacs.5b06492

Barrierless Photoisomerization of 11-cis Retinal Protonated Schiff Base in Solution

Giovanni Bassolino, Tina Sovdat, Alex Soares Duarte, Jong Min Lim, Christoph Schnedermann, Matz Liebel, Barbara Odell, Timothy D.W. Claridge, Stephen P. Fletcher, Philipp Kukura

Research output: Contribution to journal › Article › peer-review

33 Scopus citations

Abstract

A hallmark of the primary visual event is the barrierless, ultrafast, and efficient 11-cis to all-trans photoisomerization of the retinal protonated Schiff base (RPSB) chromophore. The remarkable reactivity of RPSB in the visual pigment rhodopsin has been attributed to potential energy surface modifications enabled by evolution-optimized chromophore-protein interactions. Here, we use a combined synthetic and ultrafast spectroscopic approach to show that barrierless photoisomerization is an intrinsic property of 11-cis RPSB, suggesting that the protein may merely adjust the ratio between fast reactive and slow unreactive decay channels. These results call for a re-evaluation of our understanding and theoretical description of RPSB photochemistry.

Original language	English
Pages (from-to)	12434-12437
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	137
Issue number	39
DOIs	https://doi.org/10.1021/jacs.5b06492
State	Published - 7 Oct 2015

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abstract = "A hallmark of the primary visual event is the barrierless, ultrafast, and efficient 11-cis to all-trans photoisomerization of the retinal protonated Schiff base (RPSB) chromophore. The remarkable reactivity of RPSB in the visual pigment rhodopsin has been attributed to potential energy surface modifications enabled by evolution-optimized chromophore-protein interactions. Here, we use a combined synthetic and ultrafast spectroscopic approach to show that barrierless photoisomerization is an intrinsic property of 11-cis RPSB, suggesting that the protein may merely adjust the ratio between fast reactive and slow unreactive decay channels. These results call for a re-evaluation of our understanding and theoretical description of RPSB photochemistry.",

author = "Giovanni Bassolino and Tina Sovdat and {Soares Duarte}, Alex and Lim, {Jong Min} and Christoph Schnedermann and Matz Liebel and Barbara Odell and Claridge, {Timothy D.W.} and Fletcher, {Stephen P.} and Philipp Kukura",

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AU - Bassolino, Giovanni

AU - Sovdat, Tina

AU - Soares Duarte, Alex

AU - Lim, Jong Min

AU - Schnedermann, Christoph

AU - Liebel, Matz

AU - Odell, Barbara

AU - Claridge, Timothy D.W.

AU - Fletcher, Stephen P.

AU - Kukura, Philipp

PY - 2015/10/7

Y1 - 2015/10/7

N2 - A hallmark of the primary visual event is the barrierless, ultrafast, and efficient 11-cis to all-trans photoisomerization of the retinal protonated Schiff base (RPSB) chromophore. The remarkable reactivity of RPSB in the visual pigment rhodopsin has been attributed to potential energy surface modifications enabled by evolution-optimized chromophore-protein interactions. Here, we use a combined synthetic and ultrafast spectroscopic approach to show that barrierless photoisomerization is an intrinsic property of 11-cis RPSB, suggesting that the protein may merely adjust the ratio between fast reactive and slow unreactive decay channels. These results call for a re-evaluation of our understanding and theoretical description of RPSB photochemistry.

AB - A hallmark of the primary visual event is the barrierless, ultrafast, and efficient 11-cis to all-trans photoisomerization of the retinal protonated Schiff base (RPSB) chromophore. The remarkable reactivity of RPSB in the visual pigment rhodopsin has been attributed to potential energy surface modifications enabled by evolution-optimized chromophore-protein interactions. Here, we use a combined synthetic and ultrafast spectroscopic approach to show that barrierless photoisomerization is an intrinsic property of 11-cis RPSB, suggesting that the protein may merely adjust the ratio between fast reactive and slow unreactive decay channels. These results call for a re-evaluation of our understanding and theoretical description of RPSB photochemistry.

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Barrierless Photoisomerization of 11-cis Retinal Protonated Schiff Base in Solution

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