Reductive Dechlorination Catalyzed by Bacterial Transition-Metal Coenzymes

Charles J. Gantzer, Lawrence P Wackett

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The bacterial transition-metal coenzymes vitamin B12 (Co), coenzyme F430 (Ni), and hematin (Fe) catalyzed the reductive dechlorination of polychlorinated ethylenes and benzenes, whereas the electron-transfer proteins four-iron ferredoxin, two-iron ferredoxin, and azurin (Cu) did not. For vitamin B12 and coenzyme F430, reductive dechlorination rates for different classes of perchlorinated compounds had the following order: carbon tetrachloride > tetrachloroethylene > hexachlorobenzene. For hematin, the order of reductive dechlorination rates was carbon tetrachloride > hexachlorobenzene > tetrachloroethylene. Within each class of compounds, rates of dechlorination decreased with decreasing chlorine content. Regio- and stereospecificity were observed in these reactions. In the reductive dechlorination of trichloroethylene, cis-l,2-dichloroethylene was the predominant product formed with vitamin B12, coenzyme F430, and hematin. Pentachlorobenzene and pentachlorophenol were each dechlorinated by vitamin B12 to yield two out of three possible isomeric tetrachlorobenzenes. Similar relative kinetics and dechlorination products have been observed in anaerobic cultures, suggesting a possible role of transition-metal coenzymes in the reductive dechlorination of polychlorinated compounds in natural and engineered environments.

Original languageEnglish (US)
Pages (from-to)715-722
Number of pages8
JournalEnvironmental Science and Technology
Issue number4
StatePublished - Apr 1 1991


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