Abstract
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 language | English |
|---|---|
| Title of host publication | Optogenetics |
| Subtitle of host publication | Light-Sensing Proteins and their Applications |
| Publisher | Springer Japan |
| Pages | 89-109 |
| Number of pages | 21 |
| ISBN (Electronic) | 9784431555162 |
| ISBN (Print) | 9784431555155 |
| DOIs | |
| Publication status | Published - Jan 1 2015 |
Keywords
- 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)