Mimicking Microbial Rhodopsin Isomerization in a Single Crystal

Ghanbarpour, Alireza; Nairat, Muath; Nosrati, Meisam; Santos, Elizabeth M.; Vasileiou, Chrysoula; Dantus, Marcos; Borhan, Babak; Geiger, James H.

doi:10.1021/jacs.8b12493

Title: Mimicking Microbial Rhodopsin Isomerization in a Single Crystal

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Abstract

Bacteriorhodopsin represents the simplest, and possibly most abundant, phototropic system requiring only a retinal-bound transmembrane protein to convert photons of light to an energy-generating proton gradient. The creation and interrogation of a microbial rhodopsin mimic, based on an orthogonal protein system, would illuminate the design elements required to generate new photoactive proteins with novel function. We describe a microbial rhodopsin mimic, created using a small soluble protein as a template, that specifically photoisomerizes all-trans to 13-cis retinal followed by thermal relaxation to the all-trans isomer, mimicking the bacteriorhodopsin photocycle, in a single crystal. The key element for selective isomerization is a tuned steric interaction between the chromophore and protein, similar to that seen in the microbial rhodopsins. Additionally, it is further demonstrated that a single mutation converts the system to a protein photoswitch without chromophore photoisomerization or conformational change.

Authors:

Ghanbarpour, Alireza ^[1]; Nairat, Muath ^[1]; Nosrati, Meisam ^[1]; Santos, Elizabeth M. ^[1]; Vasileiou, Chrysoula ^[2]; Dantus, Marcos ^[1];

^[1]; Geiger, James H. ^[1]

Michigan State Univ., East Lansing, MI (United States)
Michigan State Univ., East Lansing, MI (United States); Dow Performance Silicones, Midland, MI (United States)

Publication Date:: Sat Dec 22 00:00:00 EST 2018

Research Org.:: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Org.:: USDOE; Michigan Economic Development Corporation; National Institutes of Health (NIH)

OSTI Identifier:: 1544875

Grant/Contract Number:: AC02-06CH11357; 085P1000817; GM101353

Resource Type:: Accepted Manuscript

Journal Name:: Journal of the American Chemical Society

Additional Journal Information:: Journal Volume: 141; Journal Issue: 4; Journal ID: ISSN 0002-7863

Publisher:: American Chemical Society (ACS)

Country of Publication:: United States

Language:: ENGLISH

Subject:: 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; peptides and proteins; chromophores; isomerization; molecular structure; irradiation

Citation Formats


                    Ghanbarpour, Alireza, Nairat, Muath, Nosrati, Meisam, Santos, Elizabeth M., Vasileiou, Chrysoula, Dantus, Marcos, Borhan, Babak, and Geiger, James H. Mimicking Microbial Rhodopsin Isomerization in a Single Crystal.  United States: N. p., 2018. 
Web.  doi:10.1021/jacs.8b12493.

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                    Ghanbarpour, Alireza, Nairat, Muath, Nosrati, Meisam, Santos, Elizabeth M., Vasileiou, Chrysoula, Dantus, Marcos, Borhan, Babak, & Geiger, James H. Mimicking Microbial Rhodopsin Isomerization in a Single Crystal.  United States.  https://doi.org/10.1021/jacs.8b12493

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                    Ghanbarpour, Alireza, Nairat, Muath, Nosrati, Meisam, Santos, Elizabeth M., Vasileiou, Chrysoula, Dantus, Marcos, Borhan, Babak, and Geiger, James H. Sat .  
"Mimicking Microbial Rhodopsin Isomerization in a Single Crystal".  United States.  https://doi.org/10.1021/jacs.8b12493.  https://www.osti.gov/servlets/purl/1544875.

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@article{osti_1544875,

  title        = {Mimicking Microbial Rhodopsin Isomerization in a Single Crystal},

  author       = {Ghanbarpour, Alireza and Nairat, Muath and Nosrati, Meisam and Santos, Elizabeth M. and Vasileiou, Chrysoula and Dantus, Marcos and Borhan, Babak and Geiger, James H.},

  abstractNote = {Bacteriorhodopsin represents the simplest, and possibly most abundant, phototropic system requiring only a retinal-bound transmembrane protein to convert photons of light to an energy-generating proton gradient. The creation and interrogation of a microbial rhodopsin mimic, based on an orthogonal protein system, would illuminate the design elements required to generate new photoactive proteins with novel function. We describe a microbial rhodopsin mimic, created using a small soluble protein as a template, that specifically photoisomerizes all-trans to 13-cis retinal followed by thermal relaxation to the all-trans isomer, mimicking the bacteriorhodopsin photocycle, in a single crystal. The key element for selective isomerization is a tuned steric interaction between the chromophore and protein, similar to that seen in the microbial rhodopsins. Additionally, it is further demonstrated that a single mutation converts the system to a protein photoswitch without chromophore photoisomerization or conformational change.},

  doi          = {10.1021/jacs.8b12493},

  journal      = {Journal of the American Chemical Society},

  number       = 4,

  volume       = 141,

  place        = {United States},

  year         = {Sat Dec 22 00:00:00 EST 2018},

  month        = {Sat Dec 22 00:00:00 EST 2018}

}

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