Plant Physiol. Drug Metab Dispos
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Plant Physiology 80:838-842 (1986)
© 1986 American Society of Plant Biologists

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Articles

Partial Purification and Characterization of the Quinol Oxidase Activity of Arum maculatum Mitochondria 1

Walter D. Bonner, Jr., Sonia D. Clarke and Peter R. Rich

Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, Department of Biochemistry, University of Cambridge, Cambridge, CB2 1QW, U.K.

The menadiol oxidase activity of Arum maculatum mitochondria has been solubilized and fractionated. A preparation has been obtained which has an increased specific activity and a greatly decreased polypeptide composition when compared to the mitochondria. This preparation retains normal inhibitor sensitivities in that the oxidation of menadiol remains insensitive to cyanide and is inhibited by aromatic hydroxamates. Metal analyses of the preparation showed that only iron was closely correlated with the oxidase activity. No unusual lipid components were detected in the preparation. The results are discussed in relation to chemical quinol oxidation mechanisms and to several recent hypotheses concerning the nature of the higher plant alternative oxidase.

1 The authors are indebted to the Burroughts Wellcome Fund for their support of this project. W. D. B. is also supported by grants from the National Science Foundation; S. D. C. and P. R. R. by a grant from the Venture Research Unit of British Petroleum plc.




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D. A. Berthold, N. Voevodskaya, P. Stenmark, A. Graslund, and P. Nordlund
EPR Studies of the Mitochondrial Alternative Oxidase. EVIDENCE FOR A DIIRON CARBOXYLATE CENTER
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[Abstract] [Full Text] [PDF]


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Copyright © 1986 by the American Society of Plant Biologists