Horseradish peroxidase. Complex formation with anions and hydrocyanic acid.
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چکیده
منابع مشابه
Horseradish peroxidase. Complex formation with anions and hydrocyanic acid.
Equilibrium binding experiments have been performed with perchlorate, chloride, and acetate in the presence of horseradish peroxidase. The binding of perchlorate and acetate appears to be like that of nitrate, at a site other than the sixth coordination position of the heme iron. Competitive experiments using both nitrate and cyanide demonstrate that two different binding sites are present on t...
متن کاملFormation and decay of hydroperoxo-ferric heme complex in horseradish peroxidase studied by cryoradiolysis.
Using radiolytic reduction of the oxy-ferrous horseradish peroxidase (HRP) at 77 K, we observed the formation and decay of the putative intermediate, the hydroperoxo-ferric heme complex, often called "Compound 0." This intermediate is common for several different enzyme systems as the precursor of the Compound I (ferryl-oxo pi-cation radical) intermediate. EPR and UV-visible absorption spectra ...
متن کاملIn Vitro Study of Acriflavine Interaction with Horseradish Peroxidase C
Acriflavine (3,6-diaminoacridine) is an anticeptic drug developed in 1912. Previous research has focused on investigation of the intercalating features of acriflavine, but little is known about its interaction with proteins. Drug-receptor interaction is of major interest in clinical science. The aim of the present study was to evaluate the ability of acriflavine to induce alterations in conform...
متن کاملRemoval of Phenols with Encapsulated Horseradish Peroxidase in Calcium Alginate
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 ...
متن کاملCobalt-substituted horseradish peroxidase.
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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1981
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)68748-x