Molecular and Cellular Biochemistry

, Volume 7, Issue 2, pp 131–135 | Cite as

The effect of azide on the spectral and catalytic properties of ascorbate oxidase

  • Bruno Mondovi'
  • Luciana Avigliano
  • Giuseppe Rotilio
  • Alessandro Finazzi Agro'
  • Paolo Gerosa
  • Carlo Giovagnoli
Review and General Articles b. general articles


  1. (1)

    45% of the total copper of green zucchini ascorbate oxidase is EPR-detectable. At least two species of copper are present, one with a small A (Type 1) and one with a large A (Type 2). Computer simulated spectra indicated 50% contribution by each type of copper.

  2. (2)

    Azide inhibited ascorbate oxidase activity by an uncompetitive mechanism. EPR and optical spectra performed on titration of ascorbate oxidase with azide indicated the formation of a copper-azide complex. The Type 2 copper appears to be the binding site of azide. The involvement of the EPR non-detectable copper as an anion binding site with high affinity toward azide can not be excluded.



Copper Binding Site Azide Catalytic Property Oxidase Activity 
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Copyright information

© Dr. W. Junk b.v. Publishers 1975

Authors and Affiliations

  • Bruno Mondovi'
    • 1
    • 2
  • Luciana Avigliano
    • 1
  • Giuseppe Rotilio
    • 1
  • Alessandro Finazzi Agro'
    • 1
  • Paolo Gerosa
    • 1
  • Carlo Giovagnoli
    • 1
  1. 1.Institutes of Applied Biochemistry and of Biological ChemistryUniversity of Rome, and Centre for Molecular Biology, C.N.R.RomeItaly
  2. 2.Istituto di Biochimica ApplicataUniversità di Roma, Città UniversitariaRomaItaly

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