Počet záznamů: 1

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

SYSNO ASEP	0352596
Druh ASEP	J - Článek v odborném periodiku
Zařazení RIV	J - Článek v odborném periodiku
Poddruh J	Článek ve WOS
Název	Excited-state properties of the 16 kDa red carotenoid protein from Arthrospira maxima
Tvůrce(i)	Chábera, P. (CZ) Durchan, Milan (BC-A)_RID Shih, P.M. (US) Kerfeld, C.A. (US) Polívka, Tomáš (BC-A)_{RID, ORCID}
Zdroj.dok.	Biochimica Et Biophysica Acta-Bioenergetics. - : Elsevier - ISSN 0005-2728 Roč. 1807, č. 1 (2011), s. 30-35
Poč.str.	6 s.
Jazyk dok.	eng - angličtina
Země vyd.	NL - Nizozemsko
Klíč. slova	cyanobacteria ; carotenoid ; excited-state
Vědní obor RIV	BO - Biofyzika
CEZ	AV0Z50510513 - UMBR-M, BC-A (2005-2011)
UT WOS	000285121300004
DOI	10.1016/j.bbabio.2010.08.013
Anotace	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.
Pracoviště	Biologické centrum (od r. 2006)
Kontakt	Dana Hypšová, eje@eje.cz, Tel.: 387 775 214
Rok sběru	2012

Počet záznamů: 1