A kinetic study of the reaction of horseradish peroxidase with hydrogen peroxide
| Autor: | G. A. Newell, H. B. Dunford, D. Dolman, M. D. Thurlow |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
chemistry.chemical_classification
Cyanides biology Cytochrome c peroxidase Inorganic chemistry General Medicine Hydrogen Peroxide Buffers Hydrogen-Ion Concentration Plants Horseradish peroxidase chemistry.chemical_compound Kinetics Enzyme chemistry Models Chemical Peroxidases Spectrophotometry Ph range biology.protein Hydrogen peroxide Mathematics Nuclear chemistry Protein Binding |
| Zdroj: | Canadian journal of biochemistry. 53(5) |
| ISSN: | 0008-4018 |
| Popis: | A kinetic study has been carried out over the pH range of 2.63–9.37 for the reaction of horseradish peroxidase with hydrogen peroxide to form compound 1 of the enzyme. Analysis of the results, indicates that there are two kinetic influencing, ionizable groups on the enzyme with pKa values of 3.2 and 3.9. Protonation of these groups results in a decrease in the rate of reaction of the enzyme with H2O2.A previous study of the kinetics of cyanide binding to horseradish peroxidase (Ellis, W. D. &Dunford, H. B.: Biochemistry 7, 2054–2062 (1968)) has been extended down to pH 2.55, and analysis of these results also indicates the presence of two kinetically important ionizable groups on the enzyme with pKa values of 2.9 and 3.9. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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