Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-7-9
pubmed:abstractText
Trichloroethylene was oxidized by purified toluene dioxygenase obtained from recombinant E. coli strains. The major oxidation products were formic acid and glyoxylic acid. Other potential products, dichloroacetic acid, chloral, phosgene, carbon monoxide, and carbon dioxide, were not detected. [14C]trichloroethylene became covalently attached to protein components and NADPH suggesting non-specific alkylation by reactive products. Oxidation of deuterated trichloroethylene yielded 50.2% deuterated formate. Oxidation of trichloroethylene in D2O yielded 43.7% deuterated formate. These data indicate that both carbon atoms are giving rise to formic acid. The results are consistent with a mechanism of TCE oxygenation not involving epoxide, dioxetane, or dihydroxy intermediates and indicate significant differences from those previously proposed for cytochrome P-450 (Miller, R.E. & Guengerich, F.P. (1982) Biochemistry 21, 1090-1097) or methane monooxygenase (Fox, B.G., Borneman, B.G., Wackett, L.P., & Lipscomb, J.D. (1990) Biochemistry 29, 6419-6227).
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
185
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
443-51
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Trichloroethylene oxidation by toluene dioxygenase.
pubmed:affiliation
Department of Biochemistry, University of Minnesota, Navarre, MN 55392.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.