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Hydroquinone peroxidase activity of maize root mitochondria

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Summary.

The oxidation of hydroquinone with H2O2 in the presence of mitochondria isolated from maize (Zea mays L.) roots was studied. The results indicate that a reduced form of quinone may be a substrate of mitochondrial peroxidases. Specific activities in different mitochondrial isolates, the apparent K m for hydrogen peroxide and hydroquinone, and the influence of some known peroxidase inhibitors or effectors are presented. Zymographic assays revealed that all mitochondrial peroxidases, which were stained with 4-chloro-1-naphthol, were capable of oxidizing hydroquinone. A possible antioxidative role of hydroquinone peroxidase in H2O2 scavenging within the mitochondria, in cooperation with ascorbate or coupled with mitochondrial NAD(P)H dehydrogenases, is proposed.

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Abbreviations

BQ:

benzoquinone

HQ:

hydroquinone

HRP:

horseradish peroxidase

POD:

peroxidase

ROS:

reactive oxygen species

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Authors and Affiliations

  1. Laboratory of Plant Physiology, Maize Research Institute Zemun Polje, Belgrade

    Vesna Hadži-Tašković Šukalović & M. Vuletić

  2. Center for Multidisciplinary Studies, Belgrade University, Belgrade

    B. Kukavica

Authors
  1. Vesna Hadži-Tašković Šukalović
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  2. B. Kukavica
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  3. M. Vuletić
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Corresponding author

Correspondence to M. Vuletić.

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Correspondence: M. Vuletić, Laboratory of Plant Physiology, Maize Research Zemun Polje, P.O. Box 89, 11185 Belgrade, Serbia.

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Hadži-Tašković Šukalović, V., Kukavica, B. & Vuletić, M. Hydroquinone peroxidase activity of maize root mitochondria. Protoplasma 231, 137–144 (2007). https://doi.org/10.1007/s00709-007-0260-0

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  • DOI: https://doi.org/10.1007/s00709-007-0260-0

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