European Journal of Biochemistry · 1983 · 10 citations · 15 references
Life SciencesBiochemistryMolecular BiologyCellular MetabolismMetabolismMicrobial MetabolismCellular RespirationEnergy MetabolismMitochondrial BioenergeticsMitochondrial MetabolismNadh MetabolismOxidative PhosphorylationAlcohol Dehydrogenase InhibitionAlternative Nadh DehydrogenaseAlternative Oxidative PathwaysGlucose RepressionMitochondrial Nadh MetabolismNadh In Cellular RespirationNadh OxidationNadh Reoxidation
A yeast strain (SP1) resistant to glucose repression modified simultaneously in the fermentative and in the oxidative pathways (loss of alcohol dehydrogenase I and over production of cytochrome a + a3, being insensitive to the glucose effect) developed a secondary mitochondrial hydrogen pathway. Oxidative phosphorylation was measured with exogenous NADH as substrate on mitochondria derived from repressed or derepressed cells. In this strain, antimycin A promotes a partial inhibition of NADH oxidation but a complete inhibition of phosphorylation. Amytal partially inhibits oxidation of NADH but not phosphorylation. KCN inhibits NADH oxidation in a biphasic way (first level 0.1 mM, second level 5 mM) but phosphorylation was fully inhibited by 0.1 mM KCN. This alternative but non-phosphorylating pathway is insensitive to salicyl hydroxamate. The external NADH dehydrogenase, like cytochrome c oxidase is partially insensitive to catabolite repression. These results provide evidence for the presence in strain SP1 of an alternative mitochondrial pathway, going from the external NADH dehydrogenase to an oxidase, different from the normal NADH dehydrogenase ubiquinone pathway.
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Paracoccus denitrificans and the evolutionary origin of the mitochondrion
F. R. Whatley · Nature · 1975 · 382 citations
Life Sciences, Biology, Microbiology +14