Plant Physiology 94:531-537 (1990)
© 1990 American Society of Plant Biologists
Membranes and Bioenergetics
Ascorbate Free-Radical Reduction by Glyoxysomal Membranes 1
Mark l. Bowditch2 and
Robert P. Donaldson
Department of Biological Sciences, George Washington University, Washington, DC 20052
Glyoxysomal membranes from germinating castor bean (Ricinus communis L. cv Hale) endosperm contain an NADH dehydrogenase. This enzyme can utilize extraorganellar ascorbate free-radical as a substrate and can oxidize NADH at a rate which can support intraglyoxysomal demand for NAD+. NADH:ascorbate free-radical reductase was found to be membrane-associated, and the activity remained in the membrane fraction after lysis of glyoxysomes by osmotic shock, followed by pelleting of the membranes. In whole glyoxysomes, NADH:ascorbate free-radical reductase, like NADH:ferricyanide reductase and unlike NADH:cytochrome c reductase, was insensitive to trypsin and was not inactivated by Triton X-100 detergent. These results suggest that ascorbate free-radical is reduced by the same component which reduces ferricyanide in the glyoxysomal membrane redox system. NADH:ascorbate free-radical reductase comigrated with NADH:ferricyanide and cytochrome c reductases when glyoxy-somal membranes were solubilized with detergent and subjected to rate-zonal centrifugation. The results suggest that ascorbate free-radical, when reduced to ascorbate by membrane redox system, could serve as a link between glyoxysomal metabolism and other cellular activities.
2 Present address: Wiley, Rein and Fielding, Attorneys, 1776 K Street, NW, Washington, DC 20006.
1 Supported by National Science Foundation grant NSF DMB 8716740.
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