Dehalogenation of lindane by a variety of porphyrins and corrins.
AUTOR(ES)
Marks, T S
RESUMO
The dehalogenation of lindane by a range of hemoproteins, porphyrins, and corrins has been tested under reducing conditions in the presence of dithiothreitol. In addition, a series of porphyrin-metal ion complexes have been prepared and have also been screened for the capacity to dehalogenate lindane. Hemoglobin, hemin, hematin, and chlorophyll alpha all catalyzed the dehalogenation of lindane, as did all of the corrins tested. The porphyrins which did not contain metal centers--coproporphyrin, hematoporphyrin, protoporphyrin, and uroporphyrin--were inactive. However, when these porphyrins were then complexed with Co, Fe, Mg, Mo, Ni, or V, lindane dehalogenation was observed. In all cases, the reaction proceeded by an initial dechlorination to produce tetrachlorocyclohexene, which was further dehalogenated to yield chlorobenzene as the end product.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=184286Documentos Relacionados
- Activation of the methylreductase system from Methanobacterium bryantii by corrins.
- Degradation of Lindane by Escherichia coli
- Sustained inhibition of rat myometrial gap junctions and contractions by lindane
- Degradation of lindane by cell-free preparations of Clostridium sphenoides.
- Inhibition by corrins of the ATP-dependent activation and CO2 reduction by the methylreductase system in Methanobacterium bryantii.