Diperoxovanadate participates in peroxidation reactions of H2O2 in presence of abundant catalase.
Vanadate forms a stable complex with H2O2 at pH 7.0 in competition with catalase and the product, diperoxovanadate, resists scavenger action of catalase. Diperoxovanadate can act as a substrate in a H2O2-user reaction, horseradish peroxidase and can take the place of H2O2 far more effectively in oxidatively inactivating glyceraldehyde-3-phosphate dehydrogenase. By forming peroxo-complexes vanadate can provide a way of preserving cellular H2O2 in presence of abundant catalase and make it available for its functions.
Department of Biochemistry, Indian Institute of Science, Bangalore 560 012, India.
A V
AV
Rao
H N
HN
Ravishankar
T
T
Ramasarma
D000818:Animals; D001667:Binding, Competitive; D002374:Catalase / Q000378:metabolism*; D002417:Cattle; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000037:antagonists & inhibitors / Q000378:metabolism; D006735:Horseradish Peroxidase / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D009682:Magnetic Resonance Spectroscopy; D010545:Peroxides / Q000378:metabolism* / Q000494:pharmacology; D011817:Rabbits; D013379:Substrate Specificity; D014638:Vanadates / Q000378:metabolism* / Q000494:pharmacology
D004791:Enzyme Inhibitors; D010545:Peroxides; C091767:diperoxovanadate; D014638:Vanadates; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase; D002374:Catalase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases