Title : Porin and cytochrome oxidase containing contact sites involved in the oxidation of cytosolic NADH.

Pub. Date : 2005 Apr 1

PMID : 15752713






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Cytochrome c (cyto-c) added to isolated mitochondria promotes the oxidation of extra-mitochondrial NADH and the reduction of molecular oxygen associated to the generation of an electrochemical membrane potential available for ATP synthesis. NAD cytochrome c, somatic Homo sapiens
2 Cytochrome c (cyto-c) added to isolated mitochondria promotes the oxidation of extra-mitochondrial NADH and the reduction of molecular oxygen associated to the generation of an electrochemical membrane potential available for ATP synthesis. NAD cytochrome c, somatic Homo sapiens
3 Dextran sulfate (500 kDa), known to interact with porin (the voltage-dependent anion channel), other than to inhibit the release of ATP synthesized inside the mitochondria, greatly decreases the activity of exogenous NADH/cyto-c system of intact mitochondria but has no effect on the reconstituted system made of mitoplasts and external membrane preparations. NAD cytochrome c, somatic Homo sapiens
4 The proposal is put forward that the bi-trans-membrane electron transport chain activated by cytosolic cyto-c becomes, in physio-pathological conditions: (i) functional in removing the excess of cytosolic NADH; (ii) essential for cell survival in the presence of an impairment of the first three respiratory complexes; and (iii) an additional source of energy at the beginning of apoptosis. NAD cytochrome c, somatic Homo sapiens