Excited-state properties of the 16 kDa red carotenoid protein from Arthrospira maxima

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F11%3A00352596" target="_blank" >RIV/60077344:_____/11:00352596 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60076658:12640/11:43882654

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.bbabio.2010.08.013" target="_blank" >http://dx.doi.org/10.1016/j.bbabio.2010.08.013</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bbabio.2010.08.013" target="_blank" >10.1016/j.bbabio.2010.08.013</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Excited-state properties of the 16 kDa red carotenoid protein from Arthrospira maxima

Popis výsledku v původním jazyce

We have studied spectroscopic properties of the 16 kDa red carotenoid protein (RCP), which is closely related to the orange carotenoid protein (OCP) from cyanobacteria. Both proteins bind the same chromophore, the carotenoid 3-hydroxyechinenone (hECN), and the major difference between the two proteins is lack of the C-terminal domain in the RCP; this results in exposure of part of the carotenoid. The excited-state lifetime of hECN in the RCP is 5.5 ps, which is markedly longer than in OCP (3.3 ps) but close to 6 ps obtained for hECN in organic solvent. This confirms that the binding of hECN to the C-terminal domain in the OCP changes conformation of hECN, thereby altering its excited-state properties. Hydrogen bonds between the C-terminal domain and the carotenoid are also absent in the RCP. This allows the conformation of hECN in the RCP to be similar to that in solution, which results in comparable excited-state properties of hECN in solution.

Název v anglickém jazyce

Excited-state properties of the 16 kDa red carotenoid protein from Arthrospira maxima

Popis výsledku anglicky

We have studied spectroscopic properties of the 16 kDa red carotenoid protein (RCP), which is closely related to the orange carotenoid protein (OCP) from cyanobacteria. Both proteins bind the same chromophore, the carotenoid 3-hydroxyechinenone (hECN), and the major difference between the two proteins is lack of the C-terminal domain in the RCP; this results in exposure of part of the carotenoid. The excited-state lifetime of hECN in the RCP is 5.5 ps, which is markedly longer than in OCP (3.3 ps) but close to 6 ps obtained for hECN in organic solvent. This confirms that the binding of hECN to the C-terminal domain in the OCP changes conformation of hECN, thereby altering its excited-state properties. Hydrogen bonds between the C-terminal domain and the carotenoid are also absent in the RCP. This allows the conformation of hECN in the RCP to be similar to that in solution, which results in comparable excited-state properties of hECN in solution.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

BO - Biofyzika

OECD FORD obor

—

Projekt

<a href="/cs/project/GA202%2F09%2F1330" target="_blank" >GA202/09/1330: Excitované stavy karotenoidových agregátů</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Biochimica Et Biophysica Acta-Bioenergetics

ISSN

0005-2728

e-ISSN

—

Svazek periodika

1807

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

6

Strana od-do

30-35

Kód UT WoS článku

000285121300004

EID výsledku v databázi Scopus

—