| Retinal β-Iionone Ring-Salinixanthin Interactions in Xanthorhodopsin: a Study Using Artificial Pigments. | |
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MedLine Citation:
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PMID: 23331279 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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. |
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Authors:
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Elena Smolensky Koganov; Mordechai Sheves |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2013-1-21 |
Journal Detail:
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Title: Biochemistry Volume: - ISSN: 1520-4995 ISO Abbreviation: Biochemistry Publication Date: 2013 Jan |
Date Detail:
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Created Date: 2013-1-21 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
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