Model systems for understanding absorption tuning by opsin proteins

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Standard

Model systems for understanding absorption tuning by opsin proteins. / Nielsen, Mogens Brøndsted.

I: Chemical Society Reviews, Bind 38, Nr. 4, 2009, s. 913-924.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Nielsen, MB 2009, 'Model systems for understanding absorption tuning by opsin proteins', Chemical Society Reviews, bind 38, nr. 4, s. 913-924. https://doi.org/10.1039/b802068j

APA

Nielsen, M. B. (2009). Model systems for understanding absorption tuning by opsin proteins. Chemical Society Reviews, 38(4), 913-924. https://doi.org/10.1039/b802068j

Vancouver

Nielsen MB. Model systems for understanding absorption tuning by opsin proteins. Chemical Society Reviews. 2009;38(4):913-924. https://doi.org/10.1039/b802068j

Author

Nielsen, Mogens Brøndsted. / Model systems for understanding absorption tuning by opsin proteins. I: Chemical Society Reviews. 2009 ; Bind 38, Nr. 4. s. 913-924.

Bibtex

@article{c490a9201a0f11deb43e000ea68e967b,
title = "Model systems for understanding absorption tuning by opsin proteins",
abstract = "This tutorial review reports on model systems that have been synthesised and investigated for elucidating how opsin proteins tune the absorption of the protonated retinal Schiff base chromophore. In particular, the importance of the counteranion is highlighted. In addition, the review advocates for redefining the opsin shift, using the intrinsic absorption maximum (610 nm) of the protonated retinal Schiff base as a reference value, obtained by gas phase investigations, rather than the corresponding solvent value (441 nm). Hereby the necessity of correcting for solvent and counteranion effects is avoided, and it becomes clear that opsin proteins induce blueshifts in the chromophore absorption rather than redshifts.",
keywords = "Absorption, Animals, Crystallography, X-Ray, Gases, Humans, Models, Chemical, Opsins, Protein Engineering",
author = "Nielsen, {Mogens Br{\o}ndsted}",
year = "2009",
doi = "10.1039/b802068j",
language = "English",
volume = "38",
pages = "913--924",
journal = "Chemical Society Reviews",
issn = "0306-0012",
publisher = "Royal Society of Chemistry",
number = "4",

}

RIS

TY - JOUR

T1 - Model systems for understanding absorption tuning by opsin proteins

AU - Nielsen, Mogens Brøndsted

PY - 2009

Y1 - 2009

N2 - This tutorial review reports on model systems that have been synthesised and investigated for elucidating how opsin proteins tune the absorption of the protonated retinal Schiff base chromophore. In particular, the importance of the counteranion is highlighted. In addition, the review advocates for redefining the opsin shift, using the intrinsic absorption maximum (610 nm) of the protonated retinal Schiff base as a reference value, obtained by gas phase investigations, rather than the corresponding solvent value (441 nm). Hereby the necessity of correcting for solvent and counteranion effects is avoided, and it becomes clear that opsin proteins induce blueshifts in the chromophore absorption rather than redshifts.

AB - This tutorial review reports on model systems that have been synthesised and investigated for elucidating how opsin proteins tune the absorption of the protonated retinal Schiff base chromophore. In particular, the importance of the counteranion is highlighted. In addition, the review advocates for redefining the opsin shift, using the intrinsic absorption maximum (610 nm) of the protonated retinal Schiff base as a reference value, obtained by gas phase investigations, rather than the corresponding solvent value (441 nm). Hereby the necessity of correcting for solvent and counteranion effects is avoided, and it becomes clear that opsin proteins induce blueshifts in the chromophore absorption rather than redshifts.

KW - Absorption

KW - Animals

KW - Crystallography, X-Ray

KW - Gases

KW - Humans

KW - Models, Chemical

KW - Opsins

KW - Protein Engineering

U2 - 10.1039/b802068j

DO - 10.1039/b802068j

M3 - Journal article

C2 - 19421571

VL - 38

SP - 913

EP - 924

JO - Chemical Society Reviews

JF - Chemical Society Reviews

SN - 0306-0012

IS - 4

ER -

ID: 11552984