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It's a two-way street: Photoswitching and reversible changes of the protein matrix in photoswitchable fluorescent proteins and bacteriophytochromes.

FEBS Lett. 597, 1319-1344 (2023)
Verlagsversion DOI PMC
Open Access Gold (Paid Option)
Creative Commons Lizenzvertrag
Chromophore-bearing proteins that are (reversibly) altered after light illumination are major functional components of nature. They gained considerable attention in the last decades since the dynamic interactions of the chromophore and protein matrix can be used to control downstream effects altering the functionality of proteins, cells, or complete organisms with light (optogenetics). Additionally, the photophysical effects can be employed to add capabilities to optical imaging. For example, light can be used to reversibly switch the signal on or off (e.g., fluorescence). In this article, we review chromophore and protein matrix interactions, focusing on photoswitching fluorescent proteins of the GFP family (RSFPs) and natively photoswitching bacteriophytochromes (BphPs). This review aims to provide an in-depth understanding of the dynamic interplay between photoswitching photophysics and the protein matrix and a thorough discussion on how this connection has been harnessed for the development of optogenetic and imaging tools.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Korrespondenzautor
Schlagwörter Bacteriophytochromes ; Optical Imaging ; Optogenetics ; Photophysics ; Protein Engineering ; Reversibly Switchable Fluorescent Proteins ; Structural Studies; Cis-trans Isomerization; Bacterial Phytochrome; Structural Basis; Histidine Kinases; Crystal-structure; Optical Control; Excited-state; Chromophore; Mechanism; Reveals
ISSN (print) / ISBN 0014-5793
e-ISSN 1873-3468
Zeitschrift FEBS Letters
Quellenangaben Band: 597, Heft: 10, Seiten: 1319-1344 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort 111 River St, Hoboken 07030-5774, Nj Usa
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Förderungen Horizon Europe - Pillar III
European Research Council (ERC)
Projekt DEAL
Deutsche Forschungsgemeinschaft
European Union
European Research Council (ERC) under the European Union