Studies on nitrate reductase of Clostridium perfringens. II. Purification and some properties of ferredoxin.:II. Purification and Some Properties of Ferredoxin

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  • SEKI Sachiko
    Department of Chemical Microbiology, Faculty of Pharmaceutical Sciences, Hokkaido University
  • HAGIWARA Masako
    Department of Chemical Microbiology, Faculty of Pharmaceutical Sciences, Hokkaido University
  • KUDO Kumiko
    Department of Chemical Microbiology, Faculty of Pharmaceutical Sciences, Hokkaido University
  • ISHIMOTO Makoto
    Department of Chemical Microbiology, Faculty of Pharmaceutical Sciences, Hokkaido University

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Description

A ferredoxin was purified from Clostridium perfringens by DEAE-cellulose chromatography and Sephadex G-50 gel filtration. It had absorption maxima at 390 and 280nm. The molecular weight was estimated to be 6, 000 by Sephadex gel filtration and from the results of amino acid analysis. The isoelectric point was 3.0. It contained four atoms of iron, four atoms of labile sulfur, and six cysteine residues. This ferredoxin as well as ferredoxin from C. pasteuri-anum acted as an electron donor for nitrate reductase from C. perfringens. The ferredoxin could also act as an electron donor for the hydrogenase from C. pasteurianum in hydrogen evolution.

Journal

  • J Biochem (Tokyo)

    J Biochem (Tokyo) 85 (3), 833-838, 1979

    The Japanese Biochemical Society

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