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Purification and Characterization of Tetrachloroethene Reductive Dehalogenase from

Neumann, Anke, Wohlfarth, Gert, Diekert, Gabriele·1996·Journal of Biological Chemistry
DOI 10.1074/jbc.271.28.16515
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Abstract

Tetrachloroethene reductive dehalogenase from the tetrachloroethene-utilizing anaerobe, Dehalospirillum multivorans, was purified approximately 100-fold to apparent homogeneity. The purified dehalogenase catalyzed the reductive dechlorination of tetrachloroethene (PCE) to trichloroethene and of trichloroethene to cis-1,2-dichloroethene with reduced methyl viologen as the electron donor at a specific activity of 2.6 microkatal/mg. The apparent Km values for tetrachloroethene and trichloroethene were 0.20 and 0.24 mM, respectively. The apparent molecular mass of the native enzyme was determined by gel filtration to be 58 kDa. Sodium dodecyl sulfate-gel electrophoresis revealed a single protein band with a molecular mass of 57 kDa. One mol of dehalogenase contained 1.0 mol of corrinoid, 9.8 mol of iron, and 8.0 mol of acid-labile sulfur. The pH optimum was about 8.0. The enzyme had a temperature optimum of 42 degrees C. It was slightly oxygen-sensitive and was thermolabile above 50 degrees C. The dechlorination of PCE was stimulated by ammonium ions. Chlorinated methanes severely inhibited PCE dehalogenase activity.

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Research works printed but not linked: 16

  1. Neumann, 1994, Arch. Microbiol., 162, 295, 10.1007/BF00301854 · DOI
  2. Scholz-Muramatsu, 1995, Arch. Microbiol., 163, 48, 10.1007/BF00262203 · DOI
  3. Holliger, 1994, Antonie Leeuwenhoek, 66, 239, 10.1007/BF00871642 · DOI
  4. Neumann, 1995, Arch. Microbiol., 163, 276, 10.1007/BF00393380 · DOI
  5. Zehnder, 1976, Science, 194, 1165, 10.1126/science.793008 · DOI
  6. Bradford, 1976, Anal. Biochem., 72, 248, 10.1016/0003-2697(76)90527-3 · DOI · Paper page
  7. Scopes, 1974, Anal. Biochem., 59, 277, 10.1016/0003-2697(74)90034-7 · DOI
  8. Fish, 1988, Methods Enzymol., 158, 357, 10.1016/0076-6879(88)58067-9 · DOI
  9. Rabinowitz, 1978, Methods Enzymol., 53, 275, 10.1016/S0076-6879(78)53033-4 · DOI
  10. Fischer, 1992, Arch. Microbiol., 158, 208, 10.1007/BF00290817 · DOI
  11. Fetzner, 1994, Microbiol. Rev., 58, 641, 10.1128/mr.58.4.641-685.1994 · DOI
  12. Janssen, 1994, Annu. Rev. Microbiol., 48, 163, 10.1146/annurev.mi.48.100194.001115 · DOI
  13. Ni, 1995, J. Bacteriol., 177, 5135, 10.1128/jb.177.17.5135-5139.1995 · DOI
  14. Harder, 1989, Biochemistry, 28, 9080, 10.1021/bi00449a019 · DOI
  15. Sato-Watanabe, 1995, FEBS Lett., 374, 265, 10.1016/0014-5793(95)01125-X · DOI
  16. Nicholls, 1992, 2, 76

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Metadata

Authors
Neumann, A., Wohlfarth, G., & Diekert, G.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1996-07
Volume
271
Issue
28
Pages
16515-16519
ISSN
0021-9258
DOI
10.1074/jbc.271.28.16515
Cited by
182
References
0
Language
en
Licence

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