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  The interplay between chromophore and protein determines the extended excited state dynamics in a single-domain phytochrome

Slavov, C., Fischer, T., Barnoy, A., Shin, H., Rao, A. G., Wiebeler, C., et al. (2020). The interplay between chromophore and protein determines the extended excited state dynamics in a single-domain phytochrome. Proceedings of the National Academy of Sciences of the United States of America, 117(28), 16356-16362. doi:10.1073/pnas.1921706117.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0007-D4D4-A Version Permalink: https://hdl.handle.net/21.11116/0000-0007-D4D5-9
Genre: Journal Article

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 Creators:
Slavov, Chavdar1, Author
Fischer, Tobias2, Author           
Barnoy, Avishai1, Author
Shin, Heewhan1, Author
Rao, Aditya G.1, Author
Wiebeler, Christian1, Author
Zeng, Xiaoli1, Author
Sun, Yafang1, Author
Xu, Qianzhao1, Author
Gutt, Alexander3, Author           
Zhao, Kai-Hong1, Author
Gärtner, Wolfgang4, Author           
Yang, Xiaojing1, Author
Schapiro, Igor2, Author           
Wachtveitl, Josef5, Author           
Affiliations:
1external, ou_persistent22              
2External Organizations, ou_persistent22              
3Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society, ou_3023871              
4MPI for Polymer Research, Max Planck Society, ou_1309545              
5Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565160              

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 Abstract: Phytochromes are a diverse family of bilin-binding photoreceptors that regulate a wide range of physiological processes. Their pho-tochemical properties make them attractive for applications in optogenetics and superresolution microscopy. Phytochromes un-dergo reversible photoconversion triggered by the Z reversible arrow E photo-isomerization about the double bond in the bilin chromophore. However, it is not fully understood at the molecular level how the protein framework facilitates the complex photoisomerization dynamics. We have studied a single-domain bilin-binding photo-receptor All2699g1 (Nostoc sp. PCC 7120) that exhibits photocon-version between the red light-absorbing (Pr) and far red-absorbing (Pfr) states just like canonical phytochromes. We present the crys-tal structure and examine the photoisomerization mechanism of the Pr form as well as the formation of the primary photoproduct Lumi-R using time-resolved spectroscopy and hybrid quantum me-chanics/molecular mechanics simulations. We show that the un-usually long excited state lifetime (broad lifetime distribution centered at similar to 300 picoseconds) is due to the interactions between the isomerizing pyrrole ring D and an adjacent conserved Tyr142. The decay kinetics shows a strongly distributed character which is imposed by the nonexponential protein dynamics. Our findings offer a mechanistic insight into how the quantum efficiency of the bilin photoisomerization is tuned by the protein environ-ment, thereby providing a structural framework for engineer-ing bil in-based optical agents for imaging and optogenetics applications.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000553289400011
DOI: 10.1073/pnas.1921706117
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Alternative Title : PNAS
  Alternative Title : Proceedings of the National Academy of Sciences of the USA
  Alternative Title : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 117 (28) Sequence Number: - Start / End Page: 16356 - 16362 Identifier: ISSN: 0027-8424
n.a.: /journals/resource/954925427230