Abstract
Cell wall ionically bound peroxidase isolated from 14-day-old maize roots ( Zea mays L.) exhibited peroxidase activity, detected as the oxidation of p-coumaric, ferulic acids and coniferyl alcohol, naturally occurring phenolics of maize apoplast. Although p-coumaric acid was the least oxidised substrate with H 2O 2, only its phenoxy radical (derived as the oxidation product) was able to sustain NADH oxidation or linoleic acid peroxidation. Cell wall isolates generated H 2O 2 in the oxidative cycle of the peroxidases by using NADH as substrate and Mn 2+ and p-coumaric acid as cofactors. In such a reaction, coniferyl alcohol and ferulic acid showed no catalytic effect; moreover, they inhibited the reaction when p-coumaric acid was used as cofactor. According to the result presented, only p-coumaric acid participates in both the peroxidative and oxidative cycles catalysed by the peroxidase. These results point to numerous physiological roles for p-coumaric acid catalysed peroxidase reactions through its multiple control mechanisms.
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