Modulation of Light Energy Transfer from Chromophore to Protein in the Channelrhodopsin ReaChR.

ABSTRACT: The function of photoreceptors relies on efficient transfer of absorbed light energy from the chromophore to the protein to drive conformational changes that ultimately generate an output signal. In retinal-binding proteins, mainly two mechanisms exist to store the photon energy after photoisomerization: 1) conformational distortion of the prosthetic group retinal, and 2) charge separation between the protonated retinal Schiff base (RSBH⁺) and its counterion complex. Accordingly, energy transfer to the protein is achieved by chromophore relaxation and/or reduction of the charge separation in the RSBH⁺-counterion complex. Combining FTIR and UV-Vis spectroscopy along with molecular dynamics simulations, we show here for the widely used, red-activatable Volvox carteri ch

SUBMITTER: Kaufmann JCD 

PROVIDER: S-EPMC7399494 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature