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Plant Physiology 72:151-155 (1983)
© 1983 American Society of Plant Biologists

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Articles

Glyceollin: A Site-Specific Inhibitor of Electron Transport in Isolated Soybean Mitochondria 1

Rick Boydston, Jack D. Paxton and David E. Koeppe

Department of Plant Pathology, University of Illinois, Urbana, Illinois 61801, Department of Agronomy, University of Illinois, Urbana, Illinois 61801

The glyceollin inhibition of electron transport by isolated soybean and corn mitochondria was similar to that of rotenone, acting at site I between the internal NADH dehydrogenase and coenzyme Q. Coupled state 3 malate oxidation was inhibited by glyceollin and rotenone with apparent Ki values of about 15 and 5 micromolar, respectively. Carbonylcyanide m-chlorophenyl hydrazone uncoupled state 4 malate oxidation was also inhibited by glyceollin and rotenone, but uncoupled succinate and exogenous NADH state 4 oxidation was only slightly inhibited by both compounds. Glyceollin also inhibited ferricyanide reduction with malate as the electron donor, with an apparent Ki of 5.4 micromolar, but failed to inhibit such reduction with succinate or externally added NADH as electron donors. Glyceollin did not inhibit state 4 oxidation of malate, succinate, or exogenous NADH. Glyceollin did not act as a classical uncoupler or as an inhibitor of oxidative phosphorylation.

1 Supported by funds from the Illinois Agricultural Experiment Station and United States Department of Agriculture/Science and Education Administration Grant No. 59-2181-1-2-011-0.




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T. L. Graham, M. Y. Graham, S. Subramanian, and O. Yu
RNAi Silencing of Genes for Elicitation or Biosynthesis of 5-Deoxyisoflavonoids Suppresses Race-Specific Resistance and Hypersensitive Cell Death in Phytophthora sojae Infected Tissues
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[Abstract] [Full Text] [PDF]


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Copyright © 1983 by the American Society of Plant Biologists