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Retinal β-Iionone Ring-Salinixanthin Interactions in Xanthorhodopsin: a Study Using Artificial Pigments.
MedLine Citation:
PMID:  23331279     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Xanthorhodopsin (xR) is a retinal protein that contains, in addition to the retinal chromophore, a carotenoid (salinixanthin) which functions as a light-harvesting antenna (1). The center-center distance of the two polyene chains is 12-13 Å, but the distance between the two rings of the retinal and salinixanthin is surprisingly small ( ca. 5 Å) with an angle of ca. 45° (2). We aimed to clarify the role of the β-ionone ring in the retinal binding process to apo-xR, as well as a possible role that the β-ionone ring plays in fixation of the salinixanthin 4-keto ring. The binding process of native retinal and series of synthetic retinal analogues modified in the β-ionone ring to the apo-xR was monitored by absorption and circular dichroism (CD) spectroscopies. The results indicate that the β-ionone ring modification significantly affected the retinal-protein covalent bond formation as well as the pigment absorption and CD spectra. It was observed that several retinal analogs modified in the retinal β-ionone ring, did not bind to the apo-xR and did not form the pigment. All of these analogs did not induce the fixation of the salinixanthin 4-keto ring as well. In addition, we show that the native retinal within its binding site adopts exclusively 6-s-trans ring-chain conformation.
Authors:
Elena Smolensky Koganov; Mordechai Sheves
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-21
Journal Detail:
Title:  Biochemistry     Volume:  -     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-21     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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