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Study of the new electron transfer mediators in glucose oxidase catalysis

  • J. Kulys
  • , T. Buch-Rasmussen
  • , K. Bechgaard
  • , V. Razamas
  • , J. Kazlauskaite
  • , J. Marcinkeviciene
  • , J.B. Christensen
  • , H.E. Hansen

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    The steady-state oxidation of glucose oxidase from Aspergillus niger by phenothiazines, phenoxazines, Wurster's salts, dithia- and tetrathiaaromatic compounds, and nickelocene was investigated spectrophotometrically and electrochemically. At pH 7.0 the determined oxidation rate constants (TN/Km) vary in the range 103 to 108 M−1·s−1. For phenothiazines, phenoxazine and Wurster's salts oxidation constants depend on the redox potential of the electron acceptors, and results were interpreted in the framework of the outer sphere electron transfer theory (Marcus and Sutin, Biochim. Biophys. Acta, 811 (1985) 265). The interpretation of the kinetic results concerning thiaaromatic compounds and metallocenes are complicated due to complex formation with the enzyme active center and aggregation of their oxidized form in buffer solution.
    Original languageEnglish
    JournalJournal of Molecular Catalysis
    Volume91
    Issue number3
    Pages (from-to)407-420
    ISSN0304-5102
    DOIs
    Publication statusPublished - 1994

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