A Cytochrome Peroxidase From Pseudomonas Fluorescens

A CRUDE extract of Pseudomonas fluorescens was found to oxidize a reduced dye, 2,6-dichlorobenz-enoneindo-3′-chlorophenol. The activity in the crude extracts seemed similar to the ‘dye oxidase’ activity described by Smith and Stotz in plant tissues1. On partial purification, the ‘dye oxidase’ activity was always associated with a pigmented component. Spectral analysis of this pigment in the reduced and oxidized state indicated that it had an absorption similar to the respective states of cytochrome c. However, this pigment is not reduced by reduced triphosphopyridine nucleotide using purified tri-phosphopyridine cytochrome c reductase obtained from liver2.