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Fluorescence of the Retinal Chromophore in Microbial and Animal Rhodopsins.

ABSTRACT: Fluorescence of the vast majority of natural opsin-based photoactive proteins is extremely low, in accordance with their functions that depend on efficient transduction of absorbed light energy. However, several recently proposed classes of engineered rhodopsins with enhanced fluorescence, along with the discovery of a new natural highly fluorescent rhodopsin, NeoR, opened a way to exploit these transmembrane proteins as fluorescent sensors and draw more attention to studies on this untypical rhodopsin property. Here, we review the available data on the fluorescence of the retinal chromophore in microbial and animal rhodopsins and their photocycle intermediates, as well as different isomers of the protonated retinal Schiff base in various solvents and the gas phase.

SUBMITTER: Nikolaev DM

PROVIDER: S-EPMC10743670 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature

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Fluorescence of the Retinal Chromophore in Microbial and Animal Rhodopsins.

Nikolaev Dmitrii M DM Shtyrov Andrey A AA Vyazmin Sergey Yu SY Vasin Andrey V AV Panov Maxim S MS Ryazantsev Mikhail N MN

International journal of molecular sciences 20231208 24

Fluorescence of the vast majority of natural opsin-based photoactive proteins is extremely low, in accordance with their functions that depend on efficient transduction of absorbed light energy. However, several recently proposed classes of engineered rhodopsins with enhanced fluorescence, along with the discovery of a new natural highly fluorescent rhodopsin, NeoR, opened a way to exploit these transmembrane proteins as fluorescent sensors and draw more attention to studies on this untypical rh ...[more]

PMID: 38139098

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