Mimicking Microbial Rhodopsin Isomerization in a Single Crystal.
J Am Chem Soc
; 141(4): 1735-1741, 2019 01 30.
Article
en En
| MEDLINE
| ID: mdl-30580520
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. It is further demonstrated that a single mutation converts the system to a protein photoswitch without chromophore photoisomerization or conformational change.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Bacteriorodopsinas
/
Biomimética
Idioma:
En
Año:
2019
Tipo del documento:
Article