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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0016315,
umls-concept:C0033684,
umls-concept:C0035323,
umls-concept:C0035499,
umls-concept:C0042567,
umls-concept:C0053463,
umls-concept:C0206055,
umls-concept:C0441712,
umls-concept:C1260969,
umls-concept:C1704675,
umls-concept:C1879547,
umls-concept:C2004457,
umls-concept:C2587213,
umls-concept:C2603343
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pubmed:issue |
23
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pubmed:dateCreated |
1994-7-21
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pubmed:abstractText |
The photoreactions of rhodopsin regenerated with three 9-cis retinal analogs, modified at or in the vicinity of the beta-ionone ring (namely 5,6-epoxy, 7,8-diH, diethyl-acyclic) have been investigated by UV-vis and FTIR difference spectroscopy. In parallel, the ability to catalyze the GDP-->GTP exchange of G-protein (transducin) has been monitored by time-dependent fluorescence spectroscopy. The first photoproduct obtained with all three pigments at liquid nitrogen temperature is a blue-shifted intermediate (BSI), followed by a lumi-like intermediate at 170 K. For the 5,6-epoxy-ISO and 7,8-diH-ISO pigment we obtain two further intermediates similar to the META-I and META-II states of native RHO. For the diethyl-acyclic-ISO pigment only one further intermediate can be stabilized at 280 K. As compared to META-II the respective photoproduct exhibits striking differences. The latter two pigments have also been investigated in the solubilized lipid-free state (detergent: dodecyl maltoside) at 280 K. For the 5,6-epoxy-ISO pigment, the UV-vis, FTIR, and activation data agree with the formation of a META-II-like photoproduct (81% activation). Less META-II formation is observed for the 7,8-dihydro-ISO pigment in membranes (65% activation), but full formation in detergent (100% activation). Neither the membrane-bound nor the solubilized diethyl-acyclic-ISO pigment forms a META-II-like intermediate (18% and 0% activation, respectively). Therefore, we conclude that the substitution of the beta-ionone ring by two ethyl groups abolishes steric interactions with the protein, which are essential for META-II formation.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Norisoprenoids,
http://linkedlifedata.com/resource/pubmed/chemical/Rhodopsin,
http://linkedlifedata.com/resource/pubmed/chemical/Terpenes,
http://linkedlifedata.com/resource/pubmed/chemical/beta-ionone
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
33
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7389-97
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8003504-Animals,
pubmed-meshheading:8003504-Cold Temperature,
pubmed-meshheading:8003504-GTP-Binding Proteins,
pubmed-meshheading:8003504-Norisoprenoids,
pubmed-meshheading:8003504-Rhodopsin,
pubmed-meshheading:8003504-Spectrometry, Fluorescence,
pubmed-meshheading:8003504-Spectrophotometry, Ultraviolet,
pubmed-meshheading:8003504-Spectroscopy, Fourier Transform Infrared,
pubmed-meshheading:8003504-Terpenes
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pubmed:year |
1994
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pubmed:articleTitle |
Interactions of the beta-ionone ring with the protein in the visual pigment rhodopsin control the activation mechanism. An FTIR and fluorescence study on artificial vertebrate rhodopsins.
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pubmed:affiliation |
Institut für Biophysik und Strahlenbiologie, Albert-Ludwigs-Universität Freiburg, FRG.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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