The radiation inactivation of glutamate dehydrogenase.
Pulse radiolysis and 60Co gamma radiolysis were used to study the effects of ionizing radiations on the activity of glutamate dehydrogenase. Hydroxyl radicals are considerably more effective than hydrated electrons in causing loss of enzymatic activity. Evidence is also presented that the free radical anions (SCN)-.2, (Br)-.2, and (I)-.2 react with the enzyme and cause a loss of enzymatic activity. The results implicate the possible involvement of cysteine, tyrosine, and tryptophan residues in the activity of glutamate dehydrogenase.
D001665:Binding Sites; D003545:Cysteine; D004583:Electrons; D004789:Enzyme Activation / Q000528:radiation effects; D005609:Free Radicals; D005720:Gamma Rays; D005969:Glutamate Dehydrogenase / Q000378:metabolism / Q000528:radiation effects*; D006863:Hydrogen-Ion Concentration; D009243:NAD / Q000378:metabolism; D011675:Pulse Radiolysis; D014364:Tryptophan; D014443:Tyrosine
D005609:Free Radicals; D009243:NAD; D014443:Tyrosine; D014364:Tryptophan; D005969:Glutamate Dehydrogenase; D003545:Cysteine