Inactivation of Glucose Oxidase by Diperoxovanadate-Derived Oxidants

Rao, Aparna VS and Sima, Paul D and Kanofsky, Jeffrey R and Ramasarma, T (1999) Inactivation of Glucose Oxidase by Diperoxovanadate-Derived Oxidants. In: Archives of Biochemistry and Biophysics, 369 (1). pp. 163-173.

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Abstract

Inactivation of glucose oxidase occurred in the presence of bromide, vanadate, $H_2O_2$, and phosphate (the bromide system), and this was prevented by NADH or phenol red, a bromine acceptor. Glucose oxidase present during the reaction between diperoxovanadate and a reduced form of vanadate, vanadyl (the vanadyl system), but not added after mixing the reactants, was inactivated, and this was accompanied by a loss of binding of the dye, Coomassie blue, to the protein. The transient intermediate of the type $OVOOV(O_2)$, known to form in these reactions and used in the oxidation of bromide ion and NADH, appears to be responsible for inactivating glucose oxidase. In both systems, the inactivation of the enzyme was prevented by histidine and DTT, known to quench singlet-oxygen. By direct measurement of 1270-nm emission of singlet-oxygen, its generation was demonstrated in the bromide system, and in the reaction of hypohalous acids with diperoxovanadate, but not in the vanadyl system. By themselves both hypohalous acids, HOCl and HOBr inactivated glucose oxidase, and their prior reaction with $H_2O_2$ during which singlet-oxygen was released, protected the enzyme. The results provide support for possible oxidative inactivation of glucose oxidase by diperoxovanadate-derived oxidants.

Item Type:	Journal Article
Publication:	Archives of Biochemistry and Biophysics
Publisher:	Academic Press
Additional Information:	Copyright of this article belongs to Academic Press.
Keywords:	Glucose;Oxidase;Vanadate;Diperoxovanadate;Vanadyl;Bromoperoxidation;Hypohalous acids.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	24 Oct 2007
Last Modified:	19 Sep 2010 04:40
URI:	http://eprints.iisc.ac.in/id/eprint/12182

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