Abstract:
:The membrane-bound 3-chloro-4-hydroxyphenylacetate (Cl-OHPA) reductive dehalogenase from the chlorophenol-reducing 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-PAGE revealed 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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Christiansen N,Ahring BK,Wohlfarth G,Diekert Gdoi
10.1016/s0014-5793(98)01114-4subject
Has Abstractpub_date
1998-10-02 00:00:00pages
159-62issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(98)01114-4journal_volume
436pub_type
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