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• W1569753682 abstract "Abstract Fluorescence emission spectra of the oxidized and reduced forms of thioredoxin (thioredoxin-S2 and thioredoxin-(SH)2, respectively) from Escherichia coli were determined at varying pH, solvent composition, and concentration of urea or guanidine hydrochloride. Thioredoxin-S2, with only 2 tryptophan residues at positions 28 and 31, showed a strongly quenched tryptophan fluorescence (Q = 0.02) which remained constant from pH 2 to pH 10. Addition of ethanol or dioxan up to 50% (v/v) at pH 7.0 did not perturb the tryptophan emission. Guanidine hydrochloride from 2 to 4 m increased the fluorescence intensity of thioredoxin-S2 3-fold and the emission maximum was shifted from 342 nm to 355 nm indicating unfolding of the protein. The beginning of this reversible transition was also observed in 6 m urea. Between 4 to 7 m guanidine only a small increase in tryptophan fluorescence occurred, indicating that thioredoxin-S2 was largely unfolded. Thioredoxin-(SH)2, obtained by chemical reduction of thioredoxin-S2 by dithiothreitol, showed a pronounced pH dependence of fluorescence with a maximum at pH 5, where the emission intensity was 6.5-fold higher than that of thioredoxin-S2. The fluorescence intensity decreased on the alkaline side of pH 5 and seemed to fit a titration curve with an apparent pK of 6.75. Between 0 to 2 m guanidine hydrochloride the fluorescence intensity for thioredoxin-(SH)2 increased almost 2-fold in a transition not observed with thioredoxin-S2. Between 2 to 4 m guanidine the fluorescence intensity decreased in a transition similar to the increase in intensity for thioredoxin-S2. Under all experimental conditions, the tryptophan fluorescence intensity of thioredoxin-(SH)2 was higher than that of thioredoxin-S2, suggesting that the disulfide bond of thioredoxin-S2 was an important quenching group. The fluorescence emission spectrum of yeast thioredoxin, which has a single tryptophan residue in a position homologous to Trp-31 of E. coli thioredoxin, showed a low quantum yield, (Q = 0.03), of tryptophan fluorescence in its oxidized form. Reduction of the disulfide bond increased the fluorescence intensity 1.2-fold. This suggests that the conformational change which accompanies reduction of thioredoxin-S2 from E. coli has its main effect on the emission of Trp-28." @default.
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• W1569753682 date "1972-04-01" @default.
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• W1569753682 title "Tryptophan Fluorescence Study of Conformational Transitions of the Oxidized and Reduced Form of Thioredoxin" @default.
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• W1569753682 doi "https://doi.org/10.1016/s0021-9258(19)45481-1" @default.
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