Investigations of retinal proteins - Vison and optogenetics -

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  • Wada Akimori
    Laboratory of Organic Chemistry for Life Science, Kobe Pharmaceutical University

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Other Title
  • IV．レチナールタンパク質の研究　―視覚からオプトジェネティクスへ―
  • レチナールタンパク質の研究 : 視覚からオプトジェネティクスへ
  • レチナールタンパクシツ ノ ケンキュウ : シカク カラ オプトジェネティクス エ
  • 特集　―脂溶性ビタミン研究70 年―

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Abstract

Retinal proteins are now identfied over a thousand spiecies and classfied two family types, animal- and microbial-rhodopsins, from their origin. These proteins consist of the chromophre retinal and a seven-transmembrane helix apoprotein (opsin), and these two components were covalently bonded through a protonated Shiff base. When light energy was absorbed, the double bond isomerization of the chromophore occurred from 11-cis to all-trans in animal rhodopsins and from all-trans to 13-cis in microbial rhodopshins with a conformational structure change of the opsin, and the important biological functions such as vision, isomerization, ion-pumping and cation channels in living cells were performed. In this paper, I would like to briefly overview our investigations of retinal proteins for vision and optogenetics.

Journal

  • VITAMINS

    VITAMINS 94 (3), 133-136, 2020-03-25

    THE VITAMIN SOCIETY OF JAPAN

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