Electron spin resonance-spin stabilization in enzymatic systems: Detection of semiquinones produced during peroxidatic oxidation of catechols and catecholamines

1982 ◽  
Vol 106 (4) ◽  
pp. 1119-1125 ◽  
Author(s):  
B. Kalyanaraman ◽  
R.C. Sealy
1987 ◽  
Vol 42 (11-12) ◽  
pp. 1343-1344 ◽  
Author(s):  
Grzegorz Bartosz ◽  
Gabriele Christ ◽  
Harald Bosse ◽  
Roland Stephan ◽  
Helmut Gärtner

Thermal lability of bovine erythrocyte membrane proteins was studied by electron spin resonance using maleimide spin label. The temperature of the sample during measurements could be varied for the first time be­ tween 0 and 60 °C with an accuracy of ± 0.1 °C. Our results show that “old” erythrocyte membrane proteins are less stable against thermal denaturation then “young” cells.


1988 ◽  
Vol 66 (1) ◽  
pp. 76-80 ◽  
Author(s):  
Andrea Maldotti ◽  
Rossano Amadelli ◽  
Vittorio Carassiti

The oxidation of azide has been studied on TiO2 powder suspensions in water, methanol, and mixtures of the two solvents. The esr spin trapping technique has been employed to provide evidence for the formation of azidyl radicals [Formula: see text]. The results show that an aqueous alkaline medium is necessary to obtain a high production of [Formula: see text] radicals. A mechanism is proposed whereby the oxidation of [Formula: see text] is mainly due to reaction with OH• radicals which are in turn generated upon capture of holes by OH− groups adsorbed on TiO2. Azidyl anions adsorb weakly on TiO2 and do not displace adsorbed OH− from the surface.


Sign in / Sign up

Export Citation Format

Share Document