The Inactivation and Catalytic Pathways of Horseradish Peroxidase with m-Chloroperoxybenzoic Acid
Open Access
- 1 February 1997
- journal article
- Published by Elsevier
- Vol. 272 (9) , 5469-5476
- https://doi.org/10.1074/jbc.272.9.5469
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Recombinant horseradish peroxidase isoenzyme C: the effect of distal haem cavity mutations (His42→Leu and Arg38→Leu) on compound I formation and substrate bindingJBIC Journal of Biological Inorganic Chemistry, 1996
- Role of Arginine 38 in Horseradish PeroxidaseJournal of Biological Chemistry, 1996
- Ascorbate is the natural substrate for plant peroxidasesFEBS Letters, 1996
- The inactivation of horseradish peroxidase by m-chloroperoxybenzoic acid, a xenobiotic hydroperoxideJournal of Molecular Catalysis A: Chemical, 1995
- Horseradish Peroxidase His-42 → Ala, His-42 → Val, and Phe-41 → Ala MutantsJournal of Biological Chemistry, 1995
- Elementary steps in the reaction of horseradish peroxidase with several peroxides: kinetics and thermodynamics of formation of compound 0 and compound IJournal of the American Chemical Society, 1992
- A kinetic study on the suicide inactivation of peroxidase by hydrogen peroxideBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- Inactivation of peroxidase by hydrogen peroxide and its protection by a reductant agentBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- Oxygen consumption and enzyme inactivation in the indolyl-3-acetic acid oxidation catalyzed by peroxidaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- Compound I Formation with Turnip Peroxidases and Peroxybenzoic AcidsEuropean Journal of Biochemistry, 1978