IHB OpenIR  > 藻类生物学及应用研究中心  > 期刊论文
The interplay between chromophore and protein determines the extended excited state dynamics in a single-domain phytochrome
Slavov, Chavdar1; Fischer, Tobias1; Barnoy, Avishai2; Shin, Heewhan3; Rao, Aditya G.2; Wiebeler, Christian2,5,7; Zeng, Xiaoli3,8; Sun, Yafang4; Xu, Qianzhao5; Gutt, Alexander6; Zhao, Kai-Hong4; Gaertner, Wolfgang5,6; Yang, Xiaojing3; Schapiro, Igor2; Wachtveitl, Josef1
Corresponding AuthorSlavov, Chavdar(chslavov@theochem.uni-frankfurt.de) ; Yang, Xiaojing(xiaojing@uic.edu) ; Schapiro, Igor(igor.schapiro@mail.huji.ac.il) ; Wachtveitl, Josef(wveitl@theochem.uni-frankfurt.de)
2020-07-14
Source PublicationPROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
ISSN0027-8424
Volume117Issue:28Pages:16356-16362
AbstractPhytochromes 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.
Keywordknotless phytochrome photoisomerization ultrafast spectroscopy X-ray structure QM/MM
DOI10.1073/pnas.192170611
Funding OrganizationDeutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship)
Indexed BySCI ; SCI
Language英语
Funding ProjectDeutsche Forschungsgemeinschaft[WI 4853/1-1] ; Deutsche Forschungsgemeinschaft[WI 4853/2-1] ; Deutsche Forschungsgemeinschaft[WA 1850/4-2] ; National Natural Science Foundation of China (NSFC)[31861143029] ; National Natural Science Foundation of China (NSFC)[44131770822] ; European Research Council (Horizon 2020)[678169] ; Protonation Dynamics in Protein Function (Mercator fellowship)[SFB 1078]
WOS Research AreaScience & Technology - Other Topics
WOS SubjectMultidisciplinary Sciences
WOS IDWOS:000553289400011
WOS KeywordGAF DOMAIN ; FEMTOSECOND ; BACTERIOPHYTOCHROME ; PHOTODYNAMICS ; CYANOBACTERIOCHROMES ; PHYCOCYANOBILIN ; PHOTOCONVERSION ; PHOTOCHEMISTRY ; HETEROGENEITY ; DIVERSE
PublisherNATL ACAD SCIENCES
Funding OrganizationDeutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; Deutsche Forschungsgemeinschaft ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; National Natural Science Foundation of China (NSFC) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; European Research Council (Horizon 2020) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship) ; Protonation Dynamics in Protein Function (Mercator fellowship)
Citation statistics
Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/342005/38604
Collection藻类生物学及应用研究中心_期刊论文
Corresponding AuthorSlavov, Chavdar; Yang, Xiaojing; Schapiro, Igor; Wachtveitl, Josef
Affiliation1.Goethe Univ, Inst Phys & Theoret Chem, D-60438 Frankfurt, Germany
2.Hebrew Univ Jerusalem, Inst Chem, Fritz Haber Ctr Mol Dynam Res, IL-9190401 Jerusalem, Israel
3.Univ Illinois, Dept Chem, Chicago, IL 60607 USA
4.Huazhong Agr Univ, Key State Lab Agr Microbiol, Wuhan 430070, Hubei, Peoples R China
5.Univ Leipzig, Inst Analyt Chem, D-04103 Leipzig, Germany
6.Max Planck Inst Chem Energy Convers, D-45470 Mulheim, Germany
7.Leibniz Inst Surface Engn, D-04318 Leipzig, Germany
8.Chinese Acad Sci, Inst Hydrobiol, Wuhan 430072, Hubei, Peoples R China
Recommended Citation
GB/T 7714
Slavov, Chavdar,Fischer, Tobias,Barnoy, Avishai,et al. The interplay between chromophore and protein determines the extended excited state dynamics in a single-domain phytochrome[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,2020,117(28):16356-16362.
APA Slavov, Chavdar.,Fischer, Tobias.,Barnoy, Avishai.,Shin, Heewhan.,Rao, Aditya G..,...&Wachtveitl, Josef.(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.
MLA Slavov, Chavdar,et al."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(2020):16356-16362.
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