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PMID: 2555333 Published · ppublish English Journal Article

The oxidation of N-substituted aromatic amines by horseradish peroxidase.

The Journal of biological chemistry ·Vol. 264 ·No. 33 ·1989-11-25 ·Pages 19828-36

Van der Zee J, Duling DR, Mason RP, Eling TE

Abstract

The mechanism of N-dealkylation by peroxidases of the Ca2+ indicator quin2 and analogs was investigated and compared with the mechanism of N-dealkylation of some N-methyl-substituted aromatic amines. Nitrogen-centered cation radicals were detected by ESR spectroscopy for all the compounds studied. Further oxidation of the nitrogen-centered cation radicals, however, was dependent upon the structure of the radical formed. In the case of quin2 and analogs, a carbon-centered radical could be detected using the spin trap 5,5-dimethyl-1-pyrroline N-oxide. By using the spin trap 2-methyl-2-nitrosopropane (tert-nitrosobutane), it was determined that the carbon-centered radical was formed due to loss of a carboxylic acid group. This indicated that bond breakage most likely occurred through a rearrangement reaction. Furthermore, extensive oxygen consumption was detected, which was in agreement with the formation of carbon-centered radicals, as they avidly react with molecular oxygen. Thus, reaction of the carbon-centered radical with oxygen most likely led to the formation of a peroxyl radical. The peroxyl radical decomposed into superoxide that was spin trapped by 5,5-dimethyl-1-pyrroline N-oxide and an unstable iminium cation. The iminium cation would subsequently hydrolyze to the monomethyl amine and formaldehyde. In the case of N-methyl-substituted aromatic amines, carbon-centered radicals were not detected during the peroxidase-catalyzed oxidation of these compounds. Thus, rearrangement of the nitrogen-centered radical did not occur. Furthermore, little or no oxygen consumption was detected, whereas formaldehyde was formed in all cases. These results indicated that the N-methyl-substituted amines were oxidized by a mechanism different from the mechanism found for quin2 and analogs.

MeSH Terms
Aniline Compounds Egtazic Acid Electron Spin Resonance Spectroscopy Formaldehyde/analysis Free Radicals Horseradish Peroxidase/metabolism Kinetics Nitroso Compounds Oxidation-Reduction Oxygen Consumption Peroxidases/metabolism Spin Labels Substrate Specificity Toluidines
Chemicals
Aniline Compounds Free Radicals Nitroso Compounds Spin Labels Toluidines Formaldehyde Egtazic Acid N,N-dimethylaniline Horseradish Peroxidase Peroxidases tert-nitrosobutane 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid dimethyl-4-toluidine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Van der Zee J
Laboratory of Molecular Biophysics, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina 27709.
Duling D R
Mason R P
Eling T E
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1989-11-25
Pages
19828-36
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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