Determination of acid-base equilibrium constants in the excited state

1979 ◽  
Vol 31 (4) ◽  
pp. 1317-1319
Author(s):  
L. M. Rubeko ◽  
B. M. Uzhinov

2010 ◽  
Vol 26 (08) ◽  
pp. 2109-2114 ◽  
Author(s):  
ZHANG Wei-Min ◽  
◽  
YANG Zhen-Dong ◽  
LIU Jia ◽  
SUN Zhong-Xi




1978 ◽  
Vol 56 (9) ◽  
pp. 1238-1245 ◽  
Author(s):  
David Michael Rayner ◽  
Donald Theodore Krajcarski ◽  
Arthur Gustav Szabo

Fluorescence attributable to the tyrosinate form of the amino acid tyrosine, previously only observed at pH > pK(S0) = 10.3 where tyrosinate exists in the ground state, has been observed at neutral pH in the presence of high buffer base concentrations. This observation is consistent with the large shift in pK(Sl) predicted from absorption measurements and confirms that proton transfer is indeed a mechanism by which carboxylate ions quench tyrosine fluorescence. The dependence of the fluorescence quantum yields of tyrosine and tyrosinate on pH does not fit a simple excited state acid–base equilibrium model but a more complicated system where carboxylate is also capable of simultaneously quenching tyrosine fluorescence by a mechanism not involving proton transfer. Kinetic analysis of the system allows calculation of pK(S1) = 4.2 for tyrosine. The quantum yield of tyrosinate fluorescence can be appreciably higher than that normally measured at alkaline pH where a separate quenching mechanism must operate. These results have significance in the interpretation of the fluorescence properties of proteins.







1998 ◽  
Vol 43 (5) ◽  
pp. 876-879 ◽  
Author(s):  
P. Alonso ◽  
J. L. Barriada ◽  
P. Rodríguez ◽  
I. Brandariz ◽  
M. E. Sastre de Vicente


1999 ◽  
Vol 477 (1-3) ◽  
pp. 113-118 ◽  
Author(s):  
Ewa Kaczmarczyk ◽  
Roman Wróbel ◽  
Adam Liwo ◽  
Lech Chmurzyński




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