Solid-state NMR of the retinal protonated Schiff base in microbial rhodopsins  

作　　者：Sari Kumagai Izuru Kawamura 

机构地区：[1]Graduate School of Engineering Science,Yokohama National University,Yokohama,240-8501,Japan

出　　处：《Magnetic Resonance Letters》2024年第3期11-18,共8页磁共振快报（英文）

基　　金：supported in part by JSPS KAKENHI Grant Numbers in Japan(JP21H05229 to I.K.);JST CREST(JPMJCR21B2);The authors also thank Nobuko Yamaguchi for the financial support.

摘　　要：Rhodopsin is a seven-helical transmembrane protein with a retinal chromophore covalently bound to a conserved lysine in helix G via a retinal protonated Schiff base(RPSB).Microbial rhodopsins absorb light through chromophore and play a fundamental role in optogenetics.Numerous microbial rhodopsins have been discovered,contributing to diverse functions and colors.Solid-state NMR spectroscopy has been instrumental in elucidating the conformation of chromophores and the three-dimensional structure of microbial rhodopsins.This review focuses on the 15N chemical shift values of RPSB and summarizes recent progress in the field.We displayed the correlation between the 15N isotropic chemical shift values of RPSB and the maximum absorption wavelength of rhodopsin using solid-state NMR spectroscopy.

关 键 词：Membrane proteins Microbial rhodopsin RETINAL Solid-state NMR Protonated Schiff base 

分 类 号：Q503[生物学—生物化学] O482.532[理学—固体物理]