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Reductive dechlorination catalyzed by bacterial transition-metal coenzymes

Journal Article · · Environmental Science and Technology; (United States)
DOI:https://doi.org/10.1021/es00016a017· OSTI ID:5259999
;  [1]
  1. Univ. of Minnesota, Navarre (United States)

The bacterial transition-metal coenzymes vitamin B{sub 12} (Co), coenzyme F{sub 430} (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 B{sub 12} and coenzyme F{sub 430}, 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-1,2-dichloroethylene was the predominant product formed with vitamin B{sub 12}, coenzyme F{sub 430}, and hematin. Pentachlorobenzene and pentachlorophenol were each dechlorinated by vitamin B{sub 12} 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 poly-chlorinated compounds in natural and engineered environments.

OSTI ID:
5259999
Journal Information:
Environmental Science and Technology; (United States), Journal Name: Environmental Science and Technology; (United States) Vol. 25:4; ISSN ESTHA; ISSN 0013-936X
Country of Publication:
United States
Language:
English