Fluorescence quenching of anthracene in charged micelles by pyridinium and iodide ions

Biochemistry ◽  
1974 ◽  
Vol 13 (12) ◽  
pp. 2594-2597 ◽  
Author(s):  
Henry J. Pownall ◽  
Louis C. Smith

RSC Advances ◽  
2015 ◽  
Vol 5 (58) ◽  
pp. 46485-46492 ◽  
Author(s):  
Eva Bernal ◽  
José Antonio Lebron ◽  
Beatriz Sarrion ◽  
Pilar Lopez-Cornejo ◽  
Carmen Carmona ◽  
...  

Applicability of the pseudophase model to photochemical reactions in the presence of receptors (micelles) in spite of the fact that the equilibrium condition between free and bound reactants does not hold.



2015 ◽  
Vol 3 (9) ◽  
pp. 1922-1928 ◽  
Author(s):  
Zi Li ◽  
Huijun Yu ◽  
Tong Bian ◽  
Yufei Zhao ◽  
Chao Zhou ◽  
...  

Nitrogen-doped carbon quantum dots (N-CQDs) prepared via a one-step hydrothermal reaction exhibited highly selective and sensitive detection of Hg2+ and I− through fluorescence quenching and recovery processes, respectively.



1991 ◽  
Vol 176 (2) ◽  
pp. 167-172 ◽  
Author(s):  
Marek Mac ◽  
Anna Wach ◽  
Jan Najbar


RSC Advances ◽  
2021 ◽  
Vol 11 (44) ◽  
pp. 27645-27652
Author(s):  
Kai Wang ◽  
Cuihuan Geng ◽  
Fang Wang ◽  
Yajun Zhao ◽  
Zongling Ru

Urea-doped carbon dots (N-CDs) have been successfully fabricated for monitoring iodide ions; the reduced lifetime of N-CDs demonstrated that the excited energy dissipation led to a dynamic fluorescence quenching process.



2002 ◽  
Vol 49 (3) ◽  
pp. 671-682 ◽  
Author(s):  
Alicja Stachelska ◽  
Zbigniew Wieczorek ◽  
Katarzyna Ruszczyńska ◽  
Ryszard Stolarski ◽  
Monika Pietrzak ◽  
...  

Translation initiation factor eIF4E binds the m(7)G cap of eukaryotic mRNAs and mediates recruitment of mRNA to the ribosome during cap-dependent translation initiation. This event is the rate-limiting step of translation and a major target for translational control. In the nematode Caenorhabditis elegans, about 70% of genes express mRNAs with an unusual cap structure containing m(3)(2,2,7)G, which is poorly recognized by mammalian eIF4E. C. elegans expresses five isoforms of eIF4E (IFE-1, IFE-2, etc.). Three of these (IFE-3, IFE-4 and IFE-5) were investigated by means of spectroscopy and structural modelling based on mouse eIF4E bound to m(7)GDP. Intrinsic fluorescence quenching of Trp residues in the IFEs by iodide ions indicated structural differences between the apo and m(7)G cap bound proteins. Fluorescence quenching by selected cap analogues showed that only IFE-5 forms specific complexes with both m(7)G- and m(3)(2,2,7)G-containing caps (K(as) 2 x 10(6) M(-1) to 7 x 10(6) M(-1)) whereas IFE-3 and IFE-4 discriminated strongly in favor of m(7)G-containing caps. These spectroscopic results quantitatively confirm earlier qualitative data derived from affinity chromatography. The dependence of K(as) on pH indicated optimal cap binding of IFE-3, IFE-4 and IFE-5 at pH 7.2, lower by 0.4 pH units than that of eIF4E from human erythrocytes. These results provide insight into the molecular mechanism of recognition of structurally different caps by the highly homologous IFEs.



2012 ◽  
Vol 29 (4) ◽  
pp. 440
Author(s):  
Yaqiong WANG ◽  
Shaopu LIU ◽  
Zhongfang LIU ◽  
Xiaoli HU


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