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PLANT PHYSIOLOGY , Vol 108, Issue 4 1597-1605, Copyright © 1995 by American Society of Plant Biologists
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WHOLE PLANT, ENVIRONMENTAL, AND STRESS PHYSIOLOGY |
Localization and Characterization of Peroxidases in the Mitochondria of Chilling-Acclimated Maize Seedlings
T. K. Prasad, M. D. Anderson and C. R. Stewart
Department of Botany, Iowa State University, Ames, Iowa 50011
We present evidence of two peroxidases in maize (Zea mays L.) mitochondria.
One of these uses guaiacol and the other uses cytochrome c as the electron
donor. Treatments of fresh mitochondria with protease(s) indicate that
ascorbate and glutathione peroxidases are likely bound to the mitochondria
as cytosolic contaminants, whereas guaiacol and cytochrome peroxidases are
localized within the mitochondria. These two mitochondrial peroxidases are
distinct from contaminant peroxidases and mitochondrial electron transport
enzymes. Cytochrome peroxidase is present within the mitochondrial
membranes, whereas guaiacol peroxidase is loosely bound to the
mitochondrial envelope. Unlike other cellular guaiacol peroxidases,
mitochondrial guaiacol peroxidase is not glycosylated. Digestion of lysed
mitochondria with trypsin activated mitochondrial guaiacol peroxidase but
inhibited cytochrome peroxidase. Isoelectric focusing gel analysis
indicated guaiacol peroxidase as a major isozyme (isoelectric point 6.8)
that is also activated by trypsin. No change in the mobility of guaiacol
peroxidase due to trypsin treatment on native polyacrylamide gel
electrophoresis was observed. Although both peroxidases are induced by
chilling acclimation treatments (14[deg]C), only cytochrome peroxidase is
also induced by chilling (4[deg]C). Because chilling induces oxidative
stress in the maize seedlings and the mitochondria are a target for
oxidative stress injury, we suggest that mitochondrial peroxidases play a
role similar to catalase in protecting mitochondria from oxidative damage.
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