Oxidation of Phenolic Compounds by Lactoperoxidase. Evidence for the Presence of a Low-Potential Compound II during Catalytic Turnover
- 1 February 1997
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 36 (7) , 1918-1926
- https://doi.org/10.1021/bi961868y
Abstract
The lactoperoxidase (LPO)-catalyzed oxidation of p-phenols by hydrogen peroxide has been studied. The behavior of the enzyme differs from that of other peroxidases in this reaction. In particular LPO shows several catalytic intermediates during the catalytic cycle because of its capability to delocalize an oxidizing equivalent on a protein amino acid residue. In the phenol oxidation the enzyme Compound I species, containing an iron-oxo and a protein radical, uses the iron-oxo group at acidic pH and the protein radical in neutral or basic medium. Kinetic and spectroscopic studies indicate that the ionization state of an amino acid residue with pKa 5.8 +/- 0.2, probably the distal histidine, controls the enzyme intermediate forms at different pH. LPO undergoes inactivation during the oxidation of phenols. The inactivation is reversible and depends on the easy formation of Compound III even at low oxidant concentration. The inactivation is due to the substrate redox potential since the best substrate is that with lowest redox potential, while the worst substrate has the highest potential. This strongly indicates that Compound II, formed during catalytic turnover, has a low redox potential, making easier its oxidation by hydrogen peroxide to Compound III. The dependence of LPO activity on the phenols redox potential suggests that the protein radical where an oxidizing equivalent can be localized is a tyrosyl residue.Keywords
This publication has 16 references indexed in Scilit:
- Spectroscopic investigations on the highly purified lactoperoxidase Fe(III)-heme catalytic siteJournal of Inorganic Biochemistry, 1995
- Evidence for a Radical Mechanism in Peroxidase-Catalyzed Coupling. I. Steady-State Experiments with Various PeroxidasesArchives of Biochemistry and Biophysics, 1994
- Reaction of cytochrome c with the radical in cytochrome c peroxidase compound IJournal of the American Chemical Society, 1993
- Catalytic Sites of Hemoprotein PeroxidasesAnnual Review of Pharmacology and Toxicology, 1992
- Binding of aromatic donor molecules to lactoperoxidase: proton NMR and optical difference spectroscopic studiesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989
- The formation of ES of cytochrome-c peroxidase: a comparison with lactoperoxidase and horseradish peroxidaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- The Role of Lactoperoxidase‐H2O2 Compounds in the Catalysis of Thyroglobulin Iodination and Thyroid Hormone SynthesisEuropean Journal of Biochemistry, 1982
- Structure of milk lactoperoxidase. A study using circular dichroism and difference absorption spectroscopyBiochimica et Biophysica Acta (BBA) - Protein Structure, 1980
- The prosthetic group of milk lactoperoxidase is protoheme IXBiochimica et Biophysica Acta (BBA) - Protein Structure, 1979
- Peroxidase-Catalyzed HalogenationAnnual Review of Biochemistry, 1976