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FLUORESCENCE STUDIES ON ANTHRYL BACTERIORHODOPSINS

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Field Value
 
Title FLUORESCENCE STUDIES ON ANTHRYL BACTERIORHODOPSINS
 
Creator SINGH, AK
ROY, M
 
Subject hydrogen-bonded chain
halobacterium-halobium
purple membrane
light energy
proton pump
opsin shift
mechanism
protein
photoisomerization
photochemistry
bacteriorhodopsin
bacteriorhodopsin analogs
fluorescence
energy transfer
 
Description Fluorescence properties of bacteriorhodopsin analogues containing 3-methyl-5-(9'-anthryl)-2E,4E-pentadienal and 3,7-dimethyl-9-(9'-anthryl)-2E,4E,6E,8E-nonatetraenal chromophores as built-in fluorescence probes are described. Determination of fluorescence quantum yields, fluorescence quenching and energy transfer efficiencies in terms of the Forster's energy transfer between tryptophans (Trp) and the anthrylidene moiety indicates that Trp residues lie at a critical distance (R(o)) of ca. 27 angstrom from the chromophore bound at Lys-216 on the apo-protein.
 
Publisher ELSEVIER SCIENCE SA LAUSANNE
 
Date 2011-07-29T07:20:11Z
2011-12-26T12:48:32Z
2011-12-27T05:43:21Z
2011-07-29T07:20:11Z
2011-12-26T12:48:32Z
2011-12-27T05:43:21Z
1991
 
Type Article
 
Identifier JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY, 8(3), 325-335
1011-1344
http://dx.doi.org/10.1016/1011-1344(91)80089-Z
http://dspace.library.iitb.ac.in/xmlui/handle/10054/7630
http://hdl.handle.net/10054/7630
 
Language en