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

11 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

Fingerprint

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

Katayama, K., Sekharan, S., & Sudo, Y. (2015). Color tuning in retinylidene proteins. In Optogenetics: Light-Sensing Proteins and their Applications (pp. 89-109). Springer Japan. https://doi.org/10.1007/978-4-431-55516-2_7

@inbook{da7ee4156f7c4a5dba315c283d6f76ce,

title = "Color tuning in retinylidene proteins",

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.",

keywords = "Color tuning, Color variant, Retinal, Rhodopsin, Visible light, Vitamin-A, Water molecule, π-conjugation",

author = "Kota Katayama and Sivakumar Sekharan and Yuki Sudo",

year = "2015",

month = jan

day = "1",

doi = "10.1007/978-4-431-55516-2_7",

language = "English",

isbn = "9784431555155",

pages = "89--109",

booktitle = "Optogenetics",

publisher = "Springer Japan",

}

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

AN - SCOPUS:84943269585

SN - 9784431555155

SP - 89

EP - 109

BT - Optogenetics

PB - Springer Japan

ER -

Access to Document

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