Color tuning in retinylidene proteins

Kota Katayama, Sivakumar Sekharan, Yuki Sudo

Research output: Chapter in Book/Report/Conference proceedingChapter

17 Citations (Scopus)


Retinylidene proteins (also called rhodopsins) are membrane-embedded photoreceptors that contain a vitamin A aldehyde linked to a lysine residue by a Schiff base as their light-sensing chromophore. The chromophore is surrounded by seven-transmembrane α-helices and absorbs light at different wavelengths due to differences in the electronic energy gap between its ground and excited states. The variation in the wavelength of maximal absorption (λmax: 360–620 nm) of rhodopsins arises due to interaction between the apoprotein (opsin) and the retinyl chromophore, the ‘opsin shift’. This chapter reviews the color tuning mechanisms in type-1 microbial and type-2 animal rhodopsins as revealed mainly by our experimental and theoretical studies.

Original languageEnglish
Title of host publicationOptogenetics
Subtitle of host publicationLight-Sensing Proteins and their Applications
PublisherSpringer Japan
Number of pages21
ISBN (Electronic)9784431555162
ISBN (Print)9784431555155
Publication statusPublished - Jan 1 2015


  • Color tuning
  • Color variant
  • Retinal
  • Rhodopsin
  • Visible light
  • Vitamin-A
  • Water molecule
  • π-conjugation

ASJC Scopus subject areas

  • Medicine(all)
  • Neuroscience(all)
  • Biochemistry, Genetics and Molecular Biology(all)


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