Evidence for a peroxidatic oxidation of norepinephrine, a catecholamine, by lactoperoxidase

D Metodiewa; K Reszka; H B Dunford

doi:10.1016/s0006-291x(89)80128-7

Evidence for a peroxidatic oxidation of norepinephrine, a catecholamine, by lactoperoxidase

Biochem Biophys Res Commun. 1989 May 15;160(3):1183-8. doi: 10.1016/s0006-291x(89)80128-7.

Authors

D Metodiewa¹, K Reszka, H B Dunford

Affiliation

¹ Department of Chemistry, University of Alberta, Edmonton, Canada.

PMID: 2543391
DOI: 10.1016/s0006-291x(89)80128-7

Abstract

The electron spin resonance-spin stabilization technique has been applied to identify the o-semiquinone intermediate produced during the lactoperoxidase-catalyzed oxidation of the catecholamine norepinephrine. The results of a rapid scan and spectrophotometric investigation of the reaction clearly indicate a normal peroxidatic pathway of catecholamine degradation.

MeSH terms

Benzoquinones*
Chemical Phenomena
Chemistry
Cytochrome c Group / metabolism
Electron Spin Resonance Spectroscopy
Hydrogen Peroxide / metabolism
Lactoperoxidase / metabolism*
Norepinephrine / metabolism*
Oxidation-Reduction
Peroxidases / metabolism*
Quinones / metabolism
Spectrophotometry
Superoxide Dismutase / metabolism
Zinc / metabolism

Substances

Benzoquinones
Cytochrome c Group
Quinones
semiquinone radicals
Hydrogen Peroxide
Lactoperoxidase
Peroxidases
Superoxide Dismutase
Zinc
Norepinephrine