Rao A V, Ravishankar H N, Ramasarma T
Department of Biochemistry, Indian Institute of Science, Bangalore 560 012, India.
Biochim Biophys Acta. 1998 Jul 23;1381(2):249-55. doi: 10.1016/s0304-4165(98)00038-5.
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.
