The role of electron–phonon interaction and non-Gaussian transport in spectral changes of trapped electrons in glasses

1979 ◽  
Vol 57 (2) ◽  
pp. 197-206 ◽  
Author(s):  
Koichi Funabashi ◽  
William H. Hamill

The continuous-time-random-walk (CTRW) model which was developed for electron scavenging reactions in polar glasses is extended to the phenomenon of spectral relaxation of electrons in shallow traps et− in a wider range of systems. The central role of electron-phonon coupling in understanding the initial electron localization, the "pre-existing trap", and electron transfer processes are emphasized. The reactivity of et− with scavengers, including protons, is discussed in terms of the theory of multi-phonon non-radiative transitions.

It has been realized for some time that simple electron-transfer processes play an important part in the mechanism of many oxidation-reduction reactions in solution. An attempt has been made to give a quantum-mechanical interpretation of these processes on the basis of the earlier theories of electron transfer in the gaseous state (Landau 1932; Bates & Massey 1943). The present treatment for solutions takes into account the role of the solvent, with particular reference to the operation of the Franck—Condon principle and it also leads to some definite picture of the transition state for the electron transfer process. A number of examples are discussed, including electron transfer between like ions of different valency and also reactions involving complex ions, e.g. metal porphyrins, the reactions of which are of importance in certain biochemical processes. It appears that the application of certain theoretical principles leads to a satisfactory understanding of electron-transfer processes in solution from a qualitative and, in some cases, also from a semi-quantitative point of view.


2002 ◽  
Vol 124 (16) ◽  
pp. 4212-4213 ◽  
Author(s):  
Sergei Smirnov ◽  
Ivan Vlassiouk ◽  
Olaf Kutzki ◽  
Michael Wedel ◽  
Franz-Peter Montforts

1995 ◽  
Vol 310 (3) ◽  
pp. 745-749 ◽  
Author(s):  
J P Eiserich ◽  
J Butler ◽  
A van der Vliet ◽  
C E Cross ◽  
B Halliwell

By utilizing a pulse-radiolytic technique, we demonstrate for the first time that the rate constant for the reaction of nitric oxide (.NO) with biologically relevant tyrosine and tryptophan radicals (Tyr. and Trp. respectively) in amino acids, peptides and proteins is of the order of (1-2) x 10(9) M-1.s-1. We also show that .NO effectively interferes with electron-transfer processes between tryptophan and tyrosine residues in proteins subjected to pulse radiolysis. The near diffusion-controlled rates of these reactions, coupled with the increasingly recognized role of protein radicals in enzyme catalysis and oxidative damage, suggest that Tyr. and Trp. are likely and important targets for .NO generated in vivo.


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