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 Modified |
Checkout Status |
NTIS |
PB93-169076 |
Some EPA libraries have a fiche copy filed under the call number shown. |
|
07/26/2022 |
|
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.) |