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ENZYMES AND PROTEINS

Characterization of the Chlorate Reductase from Pseudomonas chloritidismutans

Arthur F. W. M. Wolterink, Emile Schiltz, Peter-Leon Hagedoorn, Wilfred R. Hagen, Servé W. M. Kengen, Alfons J. M. Stams
Arthur F. W. M. Wolterink
1Laboratory of Microbiology, Wageningen University, 6703 CT Wageningen
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Emile Schiltz
2Institute for Organic Chemistry and Biochemistry, University of Freiburg, D-79104 Freiburg, Germany
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Peter-Leon Hagedoorn
3Kluyver Department of Biotechnology, University of Delft, 2628 BC Delft, The Netherlands
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Wilfred R. Hagen
3Kluyver Department of Biotechnology, University of Delft, 2628 BC Delft, The Netherlands
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Servé W. M. Kengen
1Laboratory of Microbiology, Wageningen University, 6703 CT Wageningen
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Alfons J. M. Stams
1Laboratory of Microbiology, Wageningen University, 6703 CT Wageningen
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  • For correspondence: fons.stams@wur.nl
DOI: 10.1128/JB.185.10.3210-3213.2003
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    FIG. 1.

    Electron paramagnetic resonance spectra of P. chloritidismutans chlorate reductase. The enzyme concentration was 2.3 mg/ml or 14 μM. Trace A is from the enzyme isolated anaerobically; trace B is from dithionite-reduced enzyme. The amplification for trace B is 25 times that for trace A. Electron paramagnetic resonance conditions: microwave frequency, 9.43 GHz; microwave power, 126 mW; modulation frequency, 100 kHz; modulation amplitude, 0.63 mT; temperature, 16 K.

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  • TABLE 1.

    Summary of the purification of chlorate reductase from P. chloritidismutans

    StepVol (ml)Protein concn (mg/ml)Total activity (U)Sp act (U/mg)Yield (%)Purification (fold)
    Soluble fraction1327.572621001
    Q-Sepharose202.8335646.13
    Hydroxyapatite53.51558.721.44.4
    Mono-Q23.39514.413.17.2
    Superdex 200100.18754210.321
  • TABLE 2.

    Summary of enzyme characteristics

    EnzymeLocalizationElectron acceptor(s)Subunits (kDa)Native enzyme compositionEPR of Mo(V) (g values)ClO3−
    Vmax (U/mg)Km (μM)
    P. mirabilis chlorate reductase CMembraneChloratea75, 63, 56Heterotrimer (α1β1γ1)
    GR-1 (per)chlorate reductasePeriplasmPerchlorate, chlorate, nitrate, iodate, bromate95, 40Trimers of heterodimers     (α3β3)2.002, 2.01713.2<5
    P. chloritidismutans chlorate reductaseCytoplasmChlorate, bromateb97, 38, 34Heterotrimer (α1β1γ1)2.002, 2.024, 2.07651.3159
    • ↵ a Electron acceptors other than chlorate and nitrate were not tested.

    • ↵ b ClO4−, ClO2−, NO3−, NO2−, IO4−, IO3−, SO42−, and SeO42− were tested but did not show reductase activity.

  • TABLE 3.

    Localization of chlorate reductase, chlorite dismutase, and catalase activity in cell fractions of strain AW-1

    FractionClO3− reductase (U/mg)ClO3− reductase (U total)ClO2− dismutase (U/mg)ClO2− dismutase (U total)Catalase (U/mg)Catalase (U total)
    Periplasmic6.27.5236284NAaNA
    Cytoplasmic29.647.220.632.715.724.9
    Membrane3.829.34.83.31.7
    • ↵ a NA, no activity.

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Characterization of the Chlorate Reductase from Pseudomonas chloritidismutans
Arthur F. W. M. Wolterink, Emile Schiltz, Peter-Leon Hagedoorn, Wilfred R. Hagen, Servé W. M. Kengen, Alfons J. M. Stams
Journal of Bacteriology May 2003, 185 (10) 3210-3213; DOI: 10.1128/JB.185.10.3210-3213.2003

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Characterization of the Chlorate Reductase from Pseudomonas chloritidismutans
Arthur F. W. M. Wolterink, Emile Schiltz, Peter-Leon Hagedoorn, Wilfred R. Hagen, Servé W. M. Kengen, Alfons J. M. Stams
Journal of Bacteriology May 2003, 185 (10) 3210-3213; DOI: 10.1128/JB.185.10.3210-3213.2003
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KEYWORDS

oxidoreductases
Pseudomonas

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