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Metal-catalyzed inactivation of bovine glucose-6-phosphate dehydrogenase - role of thiols.
FEBS Lett. 396, 95-98 (1996)
The role of thiols as oxidant scavengers during inactivation of bovine glucose-6-phosphate dehydrogenase by metal-catalyzed oxidation systems has been studied in vitro. Partial inactivation of the enzyme was achieved by the metal-catalyzed oxidation systems Fe(II)/H202/EDTA or Fe(II)/H202/ADP under specific conditions. When EDTA as chelator was present in the oxidation system, both cysteine and N-acetylcysteine at low concentrations (0.1-1 mM) drastically enhanced inactivation, while cysteinyl-glycine and glutathione did not. The thiol-mediated inactivation was inhibitable by superoxide dismutase. Depletion of enzyme activity by cysteine was paralleled by an increase of the carbonyl content, which indicates oxidative injury. However, when EDTA as chelator was replaced by the natural chelator ADP, all thiols studied acted as antioxidants. It is therefore concluded that the nature of the chelator as a constituent of the metal-catalyzed oxidation systems determines whether the antioxidative function of some thiols is shifted to a prooxidative function against glucose-6-phosphate dehydrogenase.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
ISSN (print) / ISBN
0014-5793
e-ISSN
1873-3468
Zeitschrift
FEBS Letters
Quellenangaben
Band: 396,
Heft: 1,
Seiten: 95-98
Verlag
Elsevier
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Lung Biology (LHI)