Open AccessReductive dechlorination of trichloroethylene by the CO‐reduced CO dehydrogenase enzyme complex from Methanosarcina thermophila
Author(s) -
Jablonski Peter E.,
Ferry James G.
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05393.x
Subject(s) - carbon monoxide dehydrogenase , chemistry , corrinoid , trichloroethylene , methanosarcina , sulfur , enzyme , reductive dechlorination , medicinal chemistry , inorganic chemistry , organic chemistry , biochemistry , methanogenesis , biodegradation , carbon monoxide , catalysis , methane , methylation , methyltransferase , gene
Trichloroethylene (TCE) was reductively dechlorinated to cis ‐dichloroethylene, trans ‐dichloroethylene, 1,1‐dichloroethylene, vinyl chloride, and ethylene by the CO‐reduced CO dehydrogenase enzyme complex from Methanosarcina thermophila ; the apparent K m and V max values were 1.7 ± 0.3 mM TCE and 26.2 ± 1.7 mol TCE dechlorinated/min/mmol factor III. Factor III also catalysed the dechlorination of TCE when in the presence of titanium(III) citrate; the apparent K m and V max values were 1.2 ± 0.3 mM TCE and 34.9 ± 3.6 mol TCE dechlorinated/min/mmol factor III. The enzyme complex was resolved into the two‐subunit nickel/iron‐sulfur (Ni/Fe‐S) component and the two‐subunit factor III‐containing corrinoid/iron‐sulfur (Co/Fe‐S) component. The Ni/Fe‐S component was unable to dechlorinate TCE in the presence of CO; however, reconstitution with the Co/Fe‐S component yielded the same dichlorinated products as with the CO dehydrogenase enzyme complex.