Horseradish peroxidase catalyses the oxidation of NAD dimers, (NAD)2, to NAD+ in accordance with a reaction that is pH-dependent and requires 1 mol of O2 per 2 mol of (NAD)2. Horseradish peroxidase also catalyses the peroxidation of (NAD)2 to NAD+. In contrast, bacterial NADH peroxidase does not catalyse the peroxidation or the oxidation of (NAD)2. A free-radical mechanism is proposed for both ...

horseradish peroxidase was encapsulated in calcium alginate for the purpose of phenol removal. considering enzyme encapsulation efficiency, retention activity and enzyme leakage of the capsules, the best gelation condition was found to be 1 % w/v of sodium alginate solution and 5.5 % w/v of calcium chloride hexahydrate. upon immobilization, ph profile of enzyme activity changes as it shows high...

Chloroperoxidase and horseradish peroxidase use NaClOz as both the oxidant and the halogen donor for the peroxidative chlorination of monochlorodimedone. Previous studies have shown that both horseradish peroxidase and chloroperoxidase can catalyze iodination reactions with hydrogen peroxide as the oxidant; however, only chloroperoxidase catalyzes chlorination reactions under these conditions. ...

Horseradish peroxidase can be reconstituted with cobalt porphyrin to give a cobaltic holoenzyme having physicochemical properties quite similar to those of the native ferric protein. The cobaltic protein (Co3+HRP) can be reduced to the cobaltous form (CoHRP), the analogue of ferroperoxidase and the reduced cobalt protein can bind O2 to form an analogue of oxyferroperoxidase (Compound III). Sinc...

Abbreviations: Ab, antibody; ALP, alkaline phospha atrazine conjugated with horseradish peroxidase; CE, c nanotubes; CV, cyclic voltammetry; ELISA, enzyme-linke high-density polyethylene; HRP, horseradish peroxid magnetic beads; NP, nanoparticle; PAP, p-aminoph phosphate; PET, polyethylene terephthalate; POC, point electrode; RT, room temperature; TMB, 3,3′,5,5′-tetramet tetramethylbenzidine di...

The kinetics of the oxidation of p-cresol by Compound II of horseradish peroxidase has been studied by the stopped flow technique at an ionic strength of 0.11 from pH 2 to 11. In acid solution the reaction is kinetically first order in jcresol, but in the alkaline region a saturation effect attributable to complex formation is observed. At very high pH an additional second order reaction betwee...

We obtained spectroscopic evidence in support of salicylate-dependent inactivation of horseradish peroxidase-C. Addition of salicylate to the enzyme arrested at a temporal inactive state (Compound III) in the presence of H2O2, resulted in rapid and irreversible inactivation of the enzyme yielding verdohemoproteins (P-670). Multiple roles for salicylate in peroxidase-catalyzed reactions are disc...