Identification of intermediates of in vivo trichloroethylene oxidation by the membrane-associated methane monooxygenase

Abstract The rate and products of trichloroethylene (TCE) oxidation by Methylomicrobium album BG8 expressing membrane-associated methane monooxygenase (pMMO) were determined using 14C radiotracer techniques. [14C]TCE was degraded at a rate of 1.24 nmol (min mg protein)−1 with the initial production...

Full description

Saved in:
Bibliographic Details
Published inFEMS microbiology letters Vol. 186; no. 1; pp. 109 - 113
Main Authors Lontoh, Sonny, Zahn, James A., DiSpirito, Alan A., Semrau, Jeremy D.
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Publishing Ltd 01.05.2000
Blackwell
Oxford University Press
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:Abstract The rate and products of trichloroethylene (TCE) oxidation by Methylomicrobium album BG8 expressing membrane-associated methane monooxygenase (pMMO) were determined using 14C radiotracer techniques. [14C]TCE was degraded at a rate of 1.24 nmol (min mg protein)−1 with the initial production of glyoxylate and then formate. Radiolabeled CO2 was also found after incubating M. album BG8 for 5 h with [14C]TCE. Experiments with purified pMMO from Methylococcus capsulatus Bath showed that TCE could be mineralized to CO2 by pMMO. Oxygen uptake studies verified that M. album BG8 could oxidize glyoxylate and that pMMO was responsible for the oxidation based on acetylene inactivation studies. Here we propose a pathway of TCE oxidation by pMMO-expressing cells in which TCE is first converted to TCE-epoxide. The epoxide then spontaneously undergoes HCl elimination to form glyoxylate which can be further oxidized by pMMO to formate and CO2.
Bibliography:1
Chemistry Research Technologies and Protein, Lilly Corporate Center, DC1533, Eli Lilly and Company, Indianapolis, IN 46285, USA.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.2000.tb09090.x