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

SYSNO ASEP	0352596
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Excited-state properties of the 16 kDa red carotenoid protein from Arthrospira maxima
Author(s)	Chábera, P. (CZ) Durchan, Milan (BC-A)_RID Shih, P.M. (US) Kerfeld, C.A. (US) Polívka, Tomáš (BC-A)_{RID, ORCID}
Source Title	Biochimica Et Biophysica Acta-Bioenergetics. - : Elsevier - ISSN 0005-2728 Roč. 1807, č. 1 (2011), s. 30-35
Number of pages	6 s.
Language	eng - English
Country	NL - Netherlands
Keywords	cyanobacteria ; carotenoid ; excited-state
Subject RIV	BO - Biophysics
CEZ	AV0Z50510513 - UMBR-M, BC-A (2005-2011)
UT WOS	000285121300004
DOI	10.1016/j.bbabio.2010.08.013
Annotation	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.
Workplace	Biology Centre (since 2006)
Contact	Dana Hypšová, eje@eje.cz, Tel.: 387 775 214
Year of Publishing	2012

Number of the records: 1