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. 1986 Apr;80(4):838–842. doi: 10.1104/pp.80.4.838

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

Walter D Bonner Jr 1,2, Sonia D Clarke 1,2, Peter R Rich 1,2
PMCID: PMC1075216  PMID: 16664728

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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