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Journal of Plant Research

, Volume 121, Issue 1, pp 115–123 | Cite as

Effectiveness of phenoxyl radicals generated by peroxidase/H2O2-catalyzed oxidation of caffeate, ferulate, and p-coumarate in cooxidation of ascorbate and NADH

  • Vesna Hadži-Tašković Šukalović
  • Mirjana Vuletić
  • Željko Vučinić
  • Sonja Veljović-Jovanović
Regular Paper

Abstract

The rate of ascorbate and nicotinamide adenine dinucleotide plus hydrogen (NADH) cooxidation (i.e., their nonenzymic oxidation by peroxidase/H2O2-generated phenoxyl radicals of three hydroxycinnamates: caffeate, ferulate and p-coumarate) was studied in vitro. The reactions initiated by different sources of peroxidase (EC 1.11.1.7) [isolates from soybean (Glycine max L.) seed coat, maize (Zea mays L.) root-cell wall, and commercial horseradish peroxidase] were monitored. Native electrophoresis of samples and specific staining for peroxidase activity revealed various isoforms in each of the three enzyme sources. The peroxidase sources differed both in the rate of H2O2-dependent hydroxycinnamate oxidation and in the order of affinity for the phenolic substrates. The three hydroxycinnamates did not differ in their ability to cooxidize ascorbate, whereas NADH cooxidation was affected by substitution of the phenolic ring. Thus, p-coumarate was more efficient than caffeate in NADH cooxidation, with ferulate not being effective at all. Metal ions (Zn2+ and Al3+) inhibited the reaction of peroxidase with p-coumarate and affected the cooxidation rate of ascorbate and the peroxidase reaction in the same manner with all substrates used. However, inhibition of p-coumarate oxidation by metal ions did not affect NADH cooxidation rate. We propose that both the ascorbate and NADH cooxidation systems can function as mechanisms to scavenge H2O2 and regenerate phenolics in different cellular compartments, thus contributing to protection from oxidative damage.

Keywords

Ascorbate Hydroxycinnamates NADH Peroxidase Phenoxyl radicals 

Abbreviations

IEF

Isoelectric focusing

HRP

Horseradish peroxidase

PAGE

Polyacrylamide gel electrophoresis

PhO·/PhO

Redox pair phenolic phenoxyl radical/anion

UE

Equivalent unit of peroxidase activity

Notes

Acknowledgments

This work was supported by the Ministry of Science and Environmental Protection (Republic of Serbia), Projects 143020B and 143016B.

Supplementary material

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Fig. S1 (JPG 38 kb)
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Table S1 (DOC 45.5 kb)
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Table S2 (DOC 34.0 kb)
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Table S3 (DOC 29.0 kb)

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Copyright information

© The Botanical Society of Japan and Springer 2007

Authors and Affiliations

  • Vesna Hadži-Tašković Šukalović
    • 1
  • Mirjana Vuletić
    • 1
  • Željko Vučinić
    • 2
  • Sonja Veljović-Jovanović
    • 2
  1. 1.Maize Research Institute ‘Zemun Polje’BelgradeSerbia
  2. 2.Center for Multidisciplinary Studies of the Belgrade UniversityBelgradeSerbia

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