Enzymic oxidation of catechol to diphenylenedioxide-2,3-quinone

https://doi.org/10.1016/0003-9861(64)90210-3Get rights and content

Abstract

Acetone powders prepared from frozen spinach leaves contain an enzyme which oxidizes catechol to diphenylenedioxide-2,3-quinone. Standard fractionation procedures gave a preparation with a 112-fold increase in specific activity. The enzyme is specific for catechol, and has pH and temperature optima of 7.4 and 30 ° C, respectively. It is insensitive to DIECA and certain other metal chelating agents but is inhibited by cyanide. The activity of a purified preparation was increased by the addition of FAD, and inhibition by atebrin was reversed by this coenzyme. These and other properties distinguish the catechol oxidase of spinach from the copper-containing polyphenol oxidases.

References (10)

  • O.H. Lowry et al.

    J. Biol. Chem

    (1951)
  • E.A. Peterson et al.
  • W.C.G. Forsyth et al.

    Biochim. Biophys. Acta

    (1957)
  • W.C.G. Forsyth et al.

    Biochim. Biophys. Acta

    (1960)
  • P.M. Nair et al.

    Anal. Biochem

    (1964)
There are more references available in the full text version of this article.

Cited by (7)

  • Handbook of biotransformations of aromatic compounds

    2004, Handbook of Biotransformations of Aromatic Compounds
View all citing articles on Scopus

Issued as N.R.C. No. 0000.

2

National Research Council Postdoctoral Fellow 1962–1964.

View full text