o-Diphenol: Oxygen oxidoreductase from leaves of sugar cane

James Coombs, Carl Baldry, Christopher Bucke, Stephen P. Long

Research output: Contribution to journalArticlepeer-review


A non-particulate o-diphenol: O2 oxidoreductase (phenolase) has been isolated from leaves of sugar cane. Gel filtration produced two fractions MW 32000 and 130000. The preferred substrate was chlorogenic acid. Other o-diphenols (caffeic acid, catechol, pyrogallol, dihydroxyphenylalanine) all of which were slowly oxidized when tested alone, increased the rates of O2 consumption obtained with catalytic amounts of chlorogenic acid. Both enzyme fractions were inhibited by thiols; thioglycollate, which acted in a non-competitive manner, was most effective.

Original languageEnglish (US)
Pages (from-to)2703-2708
Number of pages6
Issue number12
StatePublished - Dec 1974
Externally publishedYes


  • Gramineae
  • MW determination, chlorogenic acid, substrate specificity, inhibition, thioglycollic acid.
  • Saccharum sp.
  • phenoloxidase
  • sugar cane

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Plant Science
  • Horticulture


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