Details

Autor(en) / Beteiligte

• Pagano, Katiuscia
• Paolino, Marco
• Fusi, Stefania
• Zanirato, Vinicio
• Trapella, Claudio
• Giuliani, Germano
• Cappelli, Andrea
• Zanzoni, Serena
• Molinari, Henriette
• Ragona, Laura
• Olivucci, Massimo

Titel

Bile Acid Binding Protein Functionalization Leads to a Fully Synthetic Rhodopsin Mimic

Ist Teil von

• The journal of physical chemistry letters, 2019-05, Vol.10 (9), p.2235-2243

Ort / Verlag

United States: American Chemical Society

Erscheinungsjahr

2019

Link zum Volltext

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• Rhodopsins are photoreceptive proteins using light to drive a plethora of biological functions such as vision, proton and ion pumping, cation and anion channeling, and gene and enzyme regulation. Here we combine organic synthesis, NMR structural studies, and photochemical characterization to show that it is possible to prepare a fully synthetic mimic of rhodopsin photoreceptors. More specifically, we conjugate a bile acid binding protein with a synthetic mimic of the rhodopsin protonated Schiff base chromophore to achieve a covalent complex featuring an unnatural protein host, photoswitch, and photoswitch-protein linkage with a reverse orientation. We show that, in spite of its molecular-level diversity, light irradiation of the prepared mimic fuels a photochromic cycle driven by sequential photochemical and thermal Z/E isomerizations reminiscent of the photocycles of microbial rhodopsins.