Discrimination between duroquinol oxidase activity and the terminal oxidation step of the cyanide-resistant electron transport pathway of plant mitochondria

Rustin, P.; Alin, M.F.; Lance, C.

Biochemical and Biophysical Research Communications 135(2): 677-682

1986


ISSN/ISBN: 0006-291X
PMID: 3964265
DOI: 10.1016/0006-291x(86)90046-x
Accession: 039841392

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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.