Discrimination between duroquinol oxidase activity and the terminal oxidation step of the cyanide-resistant electron transport pathway of plant mitochondria |
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| Authors: | P Rustin M F Alin C Lance |
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| Affiliation: | 1. Center of Excellent in Natural Products Chemistry, Department of Chemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand;2. Natural Products and Synthesis Chemistry Research Laboratory, Department of Chemistry, Faculty of Science, Institut Teknologi Sepuluh Nopember, Kampus ITS-Sukolilo, Surabaya 60111, Indonesia;3. Natural Products Research Section, Research Division, National Cancer Institute, Bangkok 10400, Thailand |
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| Abstract: | Comparison of the cyanide-resistant duroquinol oxidase activity of sub-mitochondrial particles from Arum maculatum L. with their ability to carry out a cyanide-resistant oxidation of NADH and succinate shows that heat-inactivation of the duroquinol oxidase activity does not proportionally affect NADH and succinate oxidation. Moreover, 1 microM antimycin inhibits duroquinol oxidase activity by 50% while not decreasing the rates of NADH and succinate oxidation. Therefore, the cyanide-resistant electron transport does not appear to be mediated by a "duroquinol oxidase", and a convincing proof of the existence of a specific protein acting as a cyanide-resistant oxidase in plant mitochondria is still lacking. |
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