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Absence of tryptophan fluorescence quenching by metal cations in delipidated bacteriorhodopsin
Author(s) -
Jang Du-Jeon,
van den Berg R.,
El-Sayed M.A.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80571-y
Subject(s) - bacteriorhodopsin , tryptophan , quenching (fluorescence) , chemistry , fluorescence , photochemistry , metal , picosecond , analytical chemistry (journal) , chromatography , biochemistry , organic chemistry , amino acid , laser , physics , membrane , optics , quantum mechanics
The addition of metal cations to deionized bacteriorhodopsin (bR) quenches the steady‐state tryptophan (Trp) fluorescence intensity and reduces the decay times of some of its picosecond components. Similar quenching processes of the Trp emission are not observed in deionized 75% delipidated bR (dLbR). The results are discussed in terms of conformational changes taking place in the protein upon delipidation.