JBC Focus on PI3-Kinase with Echelon

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Action of the Murine Toxin of Pasteurella pestis on Enzyme Complexes of the Electron Transport System

Solomon Kadis 1 and Samuel J. Ajl 1

From the 1 From the Research Laboratories, Department of Biochemistry, Albert Einstein Medical Center, Philadelphia, Pennsylvania 19141, and Institute for Enzyme Research, University of Wisconsin, Madison, Wisconsin 53706

1. The murine toxin of Pasteurella pestis inhibits the reduced nicotinamide adenine dinucleotide-cytochrome c reductase activity of electron transport particles (ETPh) as well as that of the purified complex, and the percentage inhibition is essentially the same with each of these preparations.

2. The NADH-coenzyme Q (CoQ) reductase activity of ETPh particles and the purified complex is likewise inhibited by the toxin.

3. The Amytal-insensitive NADH-ferricyanide reductase activity exhibited by NADH-CoQ reductase is not altered upon the addition of toxin, suggesting that the toxin has no effect on the NADH dehydrogenase activity of this enzyme complex.

4. Difference spectra of toxin-treated NADH-CoQ reductase reveal that the toxin has no effect on the reduction of the flavoprotein moiety of this enzyme complex. Electron paramagnetic resonance spectroscopic studies with NADH-CoQ reductase have shown that its nonheme iron content is not modified by the toxin.

5. Plague murine toxin has little or no effect on the reduced CoQ-cytochrome c reductase activity of ETPh particles, whereas the enzymatic activity of the purified complex is inhibited to a significant extent by the toxin.

Submitted on October 20, 1965


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