Journal article
Purification and characterization of the 3-chloro-4-hydroxy-phenylacetate reductive dehalogenase of Desulfitobacterium hafniense
The membrane-bound 3-chloro-4-hydroxyphenylacetate (Cl-OHPA) reductive dehalogenase from the chlorophenol- educing anaerobe Desulfitobacterium hafniense was purified 11.3-fold to apparent homogeneity in the presence of the detergent CHAPS. The purified dehalogenase catalyzed the reductive dechlorination of Cl-OHPA to 4-hydroxyphenylacetate with reduced methyl viologen as the electron donor at a specific activity of 103.2 nkat/mg protein.
SDS-PAGErevealed a single protein band with an apparent molecular mass of 46.5 kDa. The enzyme contained 0.68±0.2 mol corrinoid, 12.0±0.7 mol iron, and 13.0±0.7 mol acid-labile sulfur per mol subunit. The N-terminal amino acid sequence of the enzyme was determined and no significant similarity was found to any protein present in the gene bank.
| Language: | English |
|---|---|
| Year: | 1998 |
| Pages: | 159-162 |
| ISSN: | 00145793 and 18733468 |
| Types: | Journal article |
| DOI: | 10.1016/s0014-5793(98)01114-4 |
3-Chloro-4-hydroxyphenylacetate reductive dehalogenase Corrinoid protein Desulfitobacterium hafniense Iron-sulfur protein N-terminal amino acid sequence Tetrachloroethene dehalogenase
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate 3-chloro-4-hydroxyphenoxyacetic acid 3-chloro-4-hydroxyphenylacetate reductive dehalogenase Acetates Cholic Acids Chromatography, Ion Exchange Cl-OHPA, 3-chloro-4-hydroxyphenylacetate Detergents Electrophoresis, Polyacrylamide Gel Gram-Negative Anaerobic Bacteria Molecular Weight Oxidoreductases PCE, tetrachloroethene Phenols Phenoxyacetates Spectrophotometry Substrate Specificity
