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: Light-Sensing Proteins and their Applications |
| Publisher | Springer Japan |
| Pages | 89-109 |
| Number of pages | 21 |
| ISBN (Print) | 9784431555162, 9784431555155 |
| DOIs | |
| Publication status | Published - Jan 1 2015 |
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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)
Cite this
Color tuning in retinylidene proteins. / Katayama, Kota; Sekharan, Sivakumar; Sudo, Yuki.
Optogenetics: Light-Sensing Proteins and their Applications. Springer Japan, 2015. p. 89-109.Research output: Chapter in Book/Report/Conference proceeding › Chapter
}
TY - CHAP
T1 - Color tuning in retinylidene proteins
AU - Katayama, Kota
AU - Sekharan, Sivakumar
AU - Sudo, Yuki
PY - 2015/1/1
Y1 - 2015/1/1
N2 - 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.
AB - 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.
KW - Color tuning
KW - Color variant
KW - Retinal
KW - Rhodopsin
KW - Visible light
KW - Vitamin-A
KW - Water molecule
KW - π-conjugation
UR - http://www.scopus.com/inward/record.url?scp=84943269585&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84943269585&partnerID=8YFLogxK
U2 - 10.1007/978-4-431-55516-2_7
DO - 10.1007/978-4-431-55516-2_7
M3 - Chapter
SN - 9784431555162
SN - 9784431555155
SP - 89
EP - 109
BT - Optogenetics: Light-Sensing Proteins and their Applications
PB - Springer Japan
ER -