Document Detail


Picosecond kinetic absorption and fluorescence studies of bovine rhodopsin with a fixed 11-ene.
MedLine Citation:
PMID:  6626668     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A synthetic retinal having a fixed 11-cis geometry has been used to prepare a nonbleachable analogue of bovine rhodopsin. Marked differences in the picosecond absorption and fluorescence behavior of this analogue at room temperature, compared with that of natural rhodopsin, were observed. This not only indicates that the 11-cis to trans isomerization of the retinal moiety is the crucial primary event in the photolysis of rhodopsin, but also it establishes that this isomerization must occur on the picosecond time scale or faster.
Authors:
J Buchert; V Stefancic; A G Doukas; R R Alfano; R H Callender; J Pande; H Akita; V Balogh-Nair; K Nakanishi
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biophysical journal     Volume:  43     ISSN:  0006-3495     ISO Abbreviation:  Biophys. J.     Publication Date:  1983 Sep 
Date Detail:
Created Date:  1983-12-17     Completed Date:  1983-12-17     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  279-83     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Cattle
Kinetics
Lasers
Retinal Pigments / metabolism*
Rhodopsin / metabolism*
Spectrometry, Fluorescence
Spectrophotometry
Stereoisomerism
Time Factors
Grant Support
ID/Acronym/Agency:
EY01253/EY/NEI NIH HHS; EY02515/EY/NEI NIH HHS
Chemical
Reg. No./Substance:
0/Retinal Pigments; 9009-81-8/Rhodopsin
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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