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RECORD NUMBER: 12 OF 15

OLS Field Name OLS Field Data
Main Title Oxidation of Nitrapyrin to 6-Chloropicolinic Acid by the Ammonia-Oxidizing Bacterium 'Nitrosomonas europaea'.
Author Vannelli, T. ; Hooper, A. B. ;
CORP Author Minnesota Univ., St. Paul. Dept. of Genetics and Cell Biology.;Environmental Research Lab., Gulf Breeze, FL.;Minnesota Sea Grant Program, Duluth.
Publisher cJul 92
Year Published 1992
Report Number EPA-R-816157-0-10 ;NA86AA-D-56112; EPA/600/J-93/073;
Stock Number PB93-169076
Additional Subjects Ammonia ; Biodeterioration ; Oxidation ; Hydrazines ; Hydroxylamines ; Mass spectroscopy ; Gas chromatography ; Liquid chromatography ; Oxygen ; Membrane proteins ; Reprints ; Nitrosomonas europaea ; Nitrapyrin ; 6-chloropicolinic acid
Holdings
Library Call Number Additional Info Location Last
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Status
NTIS  PB93-169076 Most EPA libraries have a fiche copy filed under the call number shown. Check with individual libraries about paper copy. 08/23/1993
Collation 7p
Abstract
Suspensions of Nitrosomonas europaea catalyzed the oxidation of the commercial nitrification inhibitor nitrapyrin (2-chloro-6-(trichloromethyl)-pyridine). Rapid oxidation of nitrapyrin (at a concentration of 10 microM) required the concomitant oxidation of ammonia, hydroxylamine, or hydrazine. The turnover rate was highest in the presence of 10 mM ammonia (0.8 nmol of nitrapyrin per min/mg of protein). The product of the reaction was 6-chloropicolinic acid. By the use of (18)O2, it was shown that one of the oxygens in 6-chloropicolinic acid came from diatomic oxygen and that the other came from water. Approximately 13% of the radioactivity of (2,6-(14)C) nitrapyrin was shown to bind to cells. Most (94%) of the latter was bound indiscriminately to membrane proteins. The nitrapyrin bound to membrane proteins may account for the observed inactivation of ammonia oxidation. (Copyright (c) 1992, American Society for Microbiology.)