Home > Publications database > Additive Effects of Chlorin E6 and Metal Ion Binding on the Thermal Stability of Rhodopsin in Vitro > print

001     5317
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024 7 _ |2 pmid
|a pmid:19267872
024 7 _ |2 DOI
|a 10.1111/j.1751-1097.2009.00539.x
024 7 _ |2 WOS
|a WOS:000266034900009
037 _ _ |a PreJuSER-5317
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
084 _ _ |2 WoS
|a Biophysics
100 1 _ |a Balem, F.
|b 0
|u FZJ
|0 P:(DE-Juel1)VDB86778
245 _ _ |a Additive Effects of Chlorin E6 and Metal Ion Binding on the Thermal Stability of Rhodopsin in Vitro
260 _ _ |a Malden, Mass.
|b Wiley-Blackwell
|c 2009
300 _ _ |a 471 - 478
336 7 _ |a Journal Article
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|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Photochemistry and Photobiology
|x 0031-8655
|0 15281
|y 2
|v 85
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Zinc (Zn(2+)) deficiency causes retinal dysfunctions such as night blindness and neurodegeneration. Because Zn(2+) binds directly to the photoreceptor rhodopsin and alters its stability, the stabilization of rhodopsin may be key to prevention and treatment of retinal dysfunctions. In this paper, we investigated if not only trace metals but also other nutrients may stabilize rhodopsin structure in vitro. Detailed studies of the thermal stability of secondary and tertiary structure of rhodopsin in the presence and absence of the chlorophyll derivative chlorin e6 alone and together with bivalent metal ions Zn(2+), Cu(2+), Fe(2+), Ni(2+), Mg(2+)and Mn(2+) over a temperature range 5-100 degrees C were conducted using circular dichroism and fluorescence spectroscopy. When both chlorin e6 and Zn(2+) are present, a pronounced increase in the thermal stability of overall secondary structure content is observed compared to either compound alone. This additive capacity is also noted with Cu(2+), but not when other metal ions and chlorin e6 are combined.
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Cattle
650 _ 2 |2 MeSH
|a Circular Dichroism
650 _ 2 |2 MeSH
|a Ions: chemistry
650 _ 2 |2 MeSH
|a Light
650 _ 2 |2 MeSH
|a Metals: chemistry
650 _ 2 |2 MeSH
|a Metals: metabolism
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Porphyrins: chemistry
650 _ 2 |2 MeSH
|a Porphyrins: metabolism
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Protein Denaturation
650 _ 2 |2 MeSH
|a Protein Structure, Secondary
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary
650 _ 2 |2 MeSH
|a Rhodopsin: chemistry
650 _ 2 |2 MeSH
|a Rhodopsin: metabolism
650 _ 2 |2 MeSH
|a Temperature
650 _ 7 |0 0
|2 NLM Chemicals
|a Ions
650 _ 7 |0 0
|2 NLM Chemicals
|a Metals
650 _ 7 |0 0
|2 NLM Chemicals
|a Porphyrins
650 _ 7 |0 19660-77-6
|2 NLM Chemicals
|a chlorin e6
650 _ 7 |0 9009-81-8
|2 NLM Chemicals
|a Rhodopsin
650 _ 7 |a J
|2 WoSType
700 1 _ |a Yanamala, N.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Klein-Seetharaman, J.
|b 2
|u FZJ
|0 P:(DE-Juel1)VDB44599
773 _ _ |a 10.1111/j.1751-1097.2009.00539.x
|g Vol. 85, p. 471 - 478
|p 471 - 478
|q 85<471 - 478
|0 PERI:(DE-600)2048860-9
|t Photochemistry and photobiology
|v 85
|y 2009
|x 0031-8655
856 7 _ |u http://dx.doi.org/10.1111/j.1751-1097.2009.00539.x
909 C O |o oai:juser.fz-juelich.de:5317
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914 1 _ |y 2009
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