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Properties of tetrachloroethene and trichloroethene dehalogenase of Dehalospirillum multivorans

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Abstract

Some properties of tetrachloroethene and trichloroethene dehalogenase of the recently isolated, tetrachloroethene-utilizing anaerobe, Dehalospirillum multivorans, were studied with extracts of cells grown on pyruvate plus fumarate. The dehalogenase catalyzed the oxidation of reduced methyl viologen with tetrachloroethene (PCE) or trichloroethene (TCE) as electron acceptor. All other artificial or physiological electron donors tested were ineffective. The PCE and TCE dehalogenase activity was insensitive towards oxygen in crude extracts. When extracts were incubated under anoxic conditions in the presence of titanium citrate as reducing agent, the dehalogenase was rapidly inactivated by propyl iodide (50 μM). Inactivation did not occur in the absence of titanium citrate. The activity of propyl-iodide-treated extracts was restored almost immediately by illumination. The dehalogenase was inhibited by cyanide. The inhibition profile was almost the same under oxic and anoxic conditions independent of the presence or absence of titanium citrate. In addition, N2O, nitrite, and ethylene diamine tetra-acetate (EDTA) were inhibitors of PCE and TCE dehalogenase. Carbon monoxide and azide had no influence on the dehalogenase activity. Trans-1,2-dichloroethene or 1,1-dichloroethene, both of which are isomers of the dechlorination product cis-1,2-dichloroethene, neither inhibited nor inactivated the dehalogenase. PCE and TCE dechlorination appeared to be mediated by the same enzyme since the inhibitors tested had nearly the same effects on the PCE and TCE dehalogenating activity. The data indicated the involvement of a corrinoid and possibly of an additional transition metal in reductive PCE and TCE dechlorination.

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Abbreviations

PCE :

Tetrachloroethene

TCE :

Trichloroethene

DCE :

Dichloroethene

EDTA :

Ethylene diamine tetra-acetate

MV :

Methyl viologen

BV :

Benzyl viologen

PI :

Propyl iodide, 1-iodopropane

TC :

Titanium(III) citrate

References

  • Banerjee RV, Harder SR, Ragsdale SW, Matthews RG (1990) Mechanism of reductive activation of cobalamin-dependent methionine synthase: an electron paramagnetic resonance spectroelectrochemical study. Biochemistry 29:1129–1135

    Google Scholar 

  • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:925–931

    Google Scholar 

  • Bruschi M, Guerlesquin F (1988) Structure, function and evolution of bacterial ferredoxins. FEMS Microbiol Rev 54:155–176

    Google Scholar 

  • Egli C, Strohmeyer S, Cook AM, Leisinger T (1990) Transformation of tetra- and trichloromethane to CO2 is a non-enzymic process. FEMS Microbiol Lett 68:207–212

    Google Scholar 

  • Eikmanns B, Thauer RK (1985) Evidence for the involvement and role of a corrinoid enzyme in methane formation from acetate in Methanosarcina barkeri. Arch Microbiol 142:175–179

    Google Scholar 

  • Friedrich W (1975) Vitamin B12 und verwandte Corrinoide. Thieme, Stuttgart

    Google Scholar 

  • Harder SR, Lu WP, Feinberg BA, Ragsdale SW (1989) Spectroelectrochemical studies of the corrinoid/iron-sulfur protein involved in acetyl coenzyme A synthesis by Clostridium thermoaceticum. Biochemistry 28:9080–9087

    Google Scholar 

  • Holliger C, Schumacher W (1994) Reductive dehalogenation as a respiratory process. Antonie Van Leeuwenhoek 66:239–246

    Google Scholar 

  • Holliger C, Schraa G, Stupperich E, Stams AJM, Zehnder AJB (1992) Evidence for the involvement of corrinoids and factor F430 in the reductive dechlorination of 1,2-dichloroethane by Methanosarcina barkeri. J Bacteriol 174:4427–4434

    Google Scholar 

  • Holliger C, Schraa G, Stams AJM, Zehnder AJB (1993) A highly purified enrichment culture couples the reductive dechlorination of tetrachloroethene to growth. Appl Environ Microbiol 59:2991–2997

    Google Scholar 

  • Jablonski PE, Ferry JG (1992) Reductive dechlorination of trichloroethylene by the CO-reduced CO dehydrogenase enzyme complex from Methanosarcina thermophila. FEMS Microbiol Lett 96:55–60

    Google Scholar 

  • Krone UE, Laufer K, Thauer RK, Hogenkamp HPC (1989a) Coenzyme F430 as a possible catalyst for the reductive dehalogenation of chlorinated C1 hydrocarbons in methanogenic bacteria. Biochemistry 28:10061–10065

    Google Scholar 

  • Krone UE, Thauer RK, Hogenkamp HPC (1989b) Reductive dehalogenation of chlorinated C1-hydrocarbons mediated by corrinoids. Biochemistry 28:4908–4914

    Google Scholar 

  • Krone UE, Thauer RK, Hogenkamp HPC, Steinbach K (1991) Reductive formation of carbon monoxide from CCl4 and FREONs 11, 12, and 13 catalyzed by corrinoids. Biochemistry 30:2713–2719

    Google Scholar 

  • Neumann A, Scholz-Muramatsu H, Diekert G (1994) Tetrachloroethene metabolism of Dehalospirillum multivorans. Arch Microbiol 162:295–301

    Google Scholar 

  • Pratt JM (1993) Making and breaking the Co-alkyl bond in B12 derivatives. In: Sigel H, Sigle A (eds) Metal ions in biological systems, vol 29. Dekker, New York Basel, pp 229–286

    Google Scholar 

  • Scholz-Muramatsu H, Neumann A, Meßmer M, Moore E, Diekert G (1995) Isolation and characterization of Dehalospirillum multivorans gen. nov. sp. nov., a tetrachloroethene-utilizing, strictly anaerobic bacterium. Arch Microbiol 163:48–56

    Google Scholar 

  • Schrauzer GN, Stadlbauer EA (1975) Ethanolamine ammonialyase: inactivation of the holoenzyme by N2O and the mechanism of action of coenzyme B12. Bioinorg Chem 4:185–189

    Google Scholar 

  • Stupperich E (1993) Recent advances in elucidation of biological corrinoid functions. FEMS Microbiol Rev 12:349–366

    Google Scholar 

  • Vogel TM, Criddle CS, McCarty PL (1987) Transformations of halogenated aliphatic compounds. Oxidation, reduction, substitution, and dehydrohalogenation reactions occur abiotically or in microbial and mammalian systems. Environ Sci Technol 21:722–736

    Google Scholar 

  • Zehnder AJB, Wuhrmann K (1976) Titanium(III) citrate as a nontoxic, oxidation-reduction buffering system for the culture of obligate anaerobes. Science 194:1165–1166

    Google Scholar 

Download references

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Authors and Affiliations

  1. Institut für Mikrobiologie, Universität Stuttgart, Allmandring 31, D-70550, Stuttgart, Germany

    Anke Neumann, Gert Wohlfarth & Gabriele Diekert

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  1. Anke Neumann
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  2. Gert Wohlfarth
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  3. Gabriele Diekert
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Correspondence to Gabriele Diekert.

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Neumann, A., Wohlfarth, G. & Diekert, G. Properties of tetrachloroethene and trichloroethene dehalogenase of Dehalospirillum multivorans . Arch. Microbiol. 163, 276–281 (1995). https://doi.org/10.1007/BF00393380

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  • DOI: https://doi.org/10.1007/BF00393380

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