Interaction of a cytoplasmic factor with electron and ion transfer coupled functions of mitochondria
Intramitochondrial Mg 2+ is labilized by uncouplers of oxidative phosphorylation or by valinomycin. This effect of uncouplers and of valinomycin exhibits ADP dependence, while the Mg 2+ labilizing action of valinomycin requires K + also. A trace amount (∼ 10 −6 M) of a purified cytoplasmic factor (C...
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Veröffentlicht in: | Biochemical and biophysical research communications 1970-03, Vol.38 (6), p.1002-1008 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Intramitochondrial Mg
2+ is labilized by uncouplers of oxidative phosphorylation or by valinomycin. This effect of uncouplers and of valinomycin exhibits ADP dependence, while the Mg
2+ labilizing action of valinomycin requires K
+ also. A trace amount (∼ 10
−6 M) of a purified cytoplasmic factor (CMF) prevents the induction of mitochondrial Mg
2+ ejection by both uncouplers and valinomycin and simultaneously activates mitochondrial metabolism. Oxidizable substrates protect mitochondrial Mg
2+ in a transient manner against labilization by uncouplers but not against valinomycin. It is concluded that the CMF-sensitive bound Mg
2+ containing system of mitochondria regulates energy coupled electron and K
+ transfer as an energy transducer. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/0006-291X(70)90339-6 |