Oxidation reactions catalyzed by vanadium chloroperoxidase from Curvularia inaequalis.
Vanadium haloperoxidases have been reported to mediate the oxidation of halides to hypohalous acid and the sulfoxidation of organic sulfides to the corresponding sulfoxides in the presence of hydrogen peroxide. However, traditional heme peroxidase substrates were reported not to be oxidized by vanadium haloperoxidases. Surprisingly, we have now found that the recombinant vanadium chloroperoxidase from the fungus Curvularia inaequalis catalyzes the oxidation of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS), a classical chromogenic heme peroxidase substrate. The enzyme mediates the oxidation of ABTS in the presence of hydrogen peroxide with a turnover frequency of 11 s(-1) at its pH optimum of 4.0. The Km of the recombinant enzyme for ABTS was observed to be approximately 35 microM at this pH value. In addition, the bleaching of an industrial sulfonated azo dye, Chicago Sky Blue 6B, catalyzed by the recombinant vanadium chloroperoxidase in the presence of hydrogen peroxide is reported.
ten Brink
H B
HB
E. C. Slater Institute, University of Amsterdam, The Netherlands.
Dekker
H L
HL
Schoemaker
H E
HE
Wever
R
R
D002711:Chloride Peroxidase / Q000737:chemistry*; D006861:Hydrogen Peroxide / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D003904:Mitosporic Fungi / Q000201:enzymology*; D010084:Oxidation-Reduction; D011994:Recombinant Proteins; D013379:Substrate Specificity
D011994:Recombinant Proteins; D006861:Hydrogen Peroxide; C418625:vanadium chloroperoxidase; D002711:Chloride Peroxidase