Oxidation of aniline to nitrobenzene by nonheme bromoperoxidase.
Nonheme bromoperoxidase found in Pseudomonas putida catalyzed the bromination of aniline with hydrogen peroxide and bromide ions to give o- and p-bromoanilines. However, in the absence of bromide ions, it oxidized aniline via azobenzene and azoxybenzene finally into nitrobenzene. This is the first report of the biological oxidation of an arylamine to the corresponding nitrocompound at the enzyme level. In addition, nitrobenzene was not formed by a nonheme bromoperoxidase from Corallina pilulifera (marine alga), implying that the alga enzyme has a different reaction mechanism.
Itoh
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N
Department of Applied Chemistry and Biotechnology, Faculty of Engineering, Fukui University, Japan.
Morinaga
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N
Kouzai
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T
D000409:Alanine / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D056890:Eukaryota / Q000201:enzymology*; D008401:Gas Chromatography-Mass Spectrometry; D009578:Nitrobenzenes / Q000378:metabolism*; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism*; D016958:Pseudomonas putida / Q000201:enzymology*; D013379:Substrate Specificity
D009578:Nitrobenzenes; C036077:nitrobenzene; D010544:Peroxidases; C026195:bromide peroxidase; D000409:Alanine