Reinvestigation of Absorption Spectroscopic Thermal Dynamics of Archaerhodopsin 3 Based Voltage Sensor QuasAr1.

ABSTRACT: The long-time absorption spectroscopic development of the genetically encoded microbial rhodopsin fluorescent voltage indicator QuasAr1 at room temperature in the dark was reinvestigated, mainly theoretically. The data analysis indicates protein aggregation within one day to some ten-nanometer sized Mie scattering particles. The absorption coefficient spectra can be deduced from measured attenuation coefficient spectra by scattering contribution subtraction. The initially present protonated retinal Schiff base (PRSB) Ret_580 isomerized and then deprotonated to neutral retinal Schiff base (RSB). One part of Ret_580, Ret_580_I, (fraction 43%), isomerized moderately fast to Ret_500 which then deprotonated to neutral retinal Schiff base Ret_405 (time constant ≈ 1000 h). The other par

SUBMITTER: Penzkofer A 

PROVIDER: S-EPMC12729394 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature