J. Gutierrezcorrea et Aom. Stoppani, INACTIVATION OF GLUTATHIONE-REDUCTASE BY FENTON-SYSTEMS - METALLIC ION SPECIFICITY AND THE FUNCTION OF OXYGEN RADICALS, Anales de la Asociacion Quimica Argentina, 85(3-4), 1997, pp. 99-110
Yeast glutathione reductase (GR) was inactivated by Fenton Systems (FS
), Cu(II)/H2O2, Fe(II)/H2O2, Ni(II)/H2O2 and Co(II)/H2O2, being most e
ffective. Ascorbate enhanced GR inactivation. The effect of Cu(II)/H2O
2 was relatively slow and depended on Cu(II) and H2O2 concentration. C
atalase, serum albumin, benzoate (Na) and ethanol prevented GR inactiv
ation. EDTA and DETAPAC protected GR but did not activate the inactiva
te enzyme. L-Histidine protected GR or enhanced Cu(II)H2O2 effect, acc
ording to its concentration. GR damage by Cu(II)H2O2 involved tryptoph
an and tyrosine residues, as indicated by GR fluorescence. Cu(II)/NADP
H (orNADH) system also inactivated GR, an effect depending on oxygen r
adicals.