Color tuning in retinylidene proteins

Kota Katayama; Sivakumar Sekharan; Yuki Sudo

doi:10.1007/978-4-431-55516-2_7

Color tuning in retinylidene proteins

Kota Katayama, Sivakumar Sekharan, Yuki Sudo

Research output: Chapter in Book/Report/Conference proceeding › Chapter

15 Citations (Scopus)

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	https://doi.org/10.1007/978-4-431-55516-2_7
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)

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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 {\textquoteleft}opsin shift{\textquoteright}. 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.",

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AU - Sekharan, Sivakumar

AU - Sudo, Yuki

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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.

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KW - Visible light

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Color tuning in retinylidene proteins

Abstract

Keywords

ASJC Scopus subject areas

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