FTIR study of light-induced proton transfer and Ca²⁺ binding in T82D mutant of TAT rhodopsin.

ABSTRACT: Proton transfer reactions play important functional roles in many proteins, such as enzymes and transporters, which is also the case in rhodopsins. In fact, functional expression of rhodopsins accompanies intramolecular proton transfer reactions in many cases. One of the exceptional cases can be seen in the protonated form of marine bacterial TAT rhodopsin, which isomerizes the retinal by light but returns to the original state within 10^-5 s. Thus, light energy is converted into heat without any function. In contrast, the T82D mutant of TAT rhodopsin conducts the light-induced deprotonation of the Schiff base at high pH. In this article, we report the structural analysis of T82D by means of difference Fourier transform infrared (FTIR) spectroscopy. In the light-induced differenc

SUBMITTER: Sugimoto T 

PROVIDER: S-EPMC11700351 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature