Aminoethylcysteine Ketimine Decarboxylated Dimer Inhibits Mitochondrial Respiration by Impairing Electron Transport at Complex I Level
| Autor: | G. Montefoschi, Mario Fontana, Laura Pecci, Doriano Cavallini |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Cellular respiration
Stereochemistry Morpholines Dimer Submitochondrial Particles Biophysics Mitochondria Liver Biochemistry Mitochondria Heart Electron Transport chemistry.chemical_compound Electron transfer Oxygen Consumption Menadione Multienzyme Complexes NAD(P)H Dehydrogenase (Quinone) Animals NADH NADPH Oxidoreductases Submitochondrial particle Molecular Biology biology Chemistry NADH dehydrogenase Succinates Cell Biology NAD Electron transport chain Rats Kinetics biology.protein Cattle NAD+ kinase Oxidation-Reduction |
| Zdroj: | Biochemical and Biophysical Research Communications. 199:755-760 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1994.1293 |
| Popis: | The product of the spontaneous dimerization and decarboxylation of aminoethylcysteine ketimine (simply named the dimer in this note) has been investigated for a possible biochemical activity. It has been found that the dimer inhibits the ADP-dependent oxidation of NAD + -linked substrates in rat liver mitochondria and electron transport from NADH to O 2 in bovine heart submitochondrial particles (SMP). Oxidation of succinate by SMP is not impaired by concentrations of the dimer inhibiting almost totally NADH oxidation. Furthermore, the dimer did not affect the rotenone-insensitive electron transfer from NADH to menadione. These results give a preliminary indication suggesting that the dimer inhibits electron flow from NADH dehydrogenase to ubiquinone at or near the rotenone binding site(s). The dimer inhibition falls in the same range exibited by some neurotoxins which are known to interact with the rotenone binding site. |
| Databáze: | OpenAIRE |
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