Some properties of external NADH oxidation by human placental mitochondria.
Isolated human term placenta mitochondria catalyse oxidation of external NADH in the presence of cytochrome c. This reaction is insensitive to the respiratory chain inhibitors such as rotenone and antimycin A, and is not coupled to phosphorylation. Comparison of the effect of Mg++ ion on NADH plus cytochrome c oxidation by human term placental, human skeletal muscle and rat skeletal mitochondria showed that Mg++ ion exerts an inhibitory effect in the case of human mitochondria and a stimulatory effect in the case of rat skeletal muscle mitochondria.
D000818:Animals; D000968:Antimycin A / Q000494:pharmacology; D003574:Cytochrome c Group / Q000494:pharmacology; D005260:Female; D006801:Humans; D008274:Magnesium / Q000494:pharmacology; D008928:Mitochondria / Q000187:drug effects / Q000378:metabolism*; D008931:Mitochondria, Muscle / Q000187:drug effects / Q000378:metabolism; D009243:NAD / Q000378:metabolism*; D010084:Oxidation-Reduction; D010920:Placenta / Q000187:drug effects / Q000378:metabolism*; D011247:Pregnancy; D051381:Rats; D012402:Rotenone / Q000494:pharmacology
D003574:Cytochrome c Group; D012402:Rotenone; D009243:NAD; D000968:Antimycin A; D008274:Magnesium