Reductive dechlorination of trichloroethylene by the CO-reduced CO dehydrogenase enzyme complex from Methanosarcina thermophila

Peter E. Jablonski, James G. Ferry

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Abstract

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 Km and Vmax 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 Km and Vmax 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.

Original languageEnglish (US)
Pages (from-to)55-59
Number of pages5
JournalFEMS Microbiology Letters
Volume96
Issue number1
DOIs
Publication statusPublished - Sep 1 1992

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All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology
  • Genetics

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