Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase
| Autor: | D.R. Biggs, Edna B. Kearney, E. Rocca, H. Nakamura, Thomas P. Singer |
|---|---|
| Rok vydání: | 1970 |
| Předmět: |
chemistry.chemical_classification
Phospholipase A biology Biophysics Respiratory chain NADH dehydrogenase Dehydrogenase Phospholipase Biochemistry Molecular biology chemistry.chemical_compound Enzyme chemistry biology.protein Piericidin A Branched-chain alpha-keto acid dehydrogenase complex Molecular Biology |
| Zdroj: | Archives of Biochemistry and Biophysics. 137:12-29 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/0003-9861(70)90406-6 |
| Popis: | The respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase of S. cerevisiae and C. utilis in mitochondrial and in membrane preparations has been investigated. Among methods tested, the highest activities for the dehydrogenase are obtained in the NADH-coenzyme Q1 reaction in S. cerevisiae, while the NADH-ferricyanide reaction provides the best activity determination for the enzyme from C. utilis. In several respects, including specificity for electron acceptor and substrate and inhibition by amytal, rotenone, and piericidin A, the dehydrogenase from C. utilis resembles its counterpart in mammalian mitochondria much more closely than does the enzyme from S. cerevisiae. The latter enzyme appears to be extensively solubilized on digestion of membrane preparations with N. naja venom phospholipase A, as is the case with the mammalian enzyme, whereas the dehydrogenase from C. utilis is not extracted by this treatment. The failure of phospholipase A to extract the C. utilis enzyme is not due to unusual phosphatide composition as shown by phosphatide analyses and by the fact that lecithin isolated from C. utilis mitochondria is readily hydrolyzed by phospholipase A, but may be due to the inaccessibility of the phospholipase to mitochondrial lipids in situ. NADH dehydrogenase from both types of yeasts is extensively inactivated by the heat-acid-ethanol method previously used by other workers for the isolation of “NADH dehydrogenase” from S. cerevisiae. During the O2-induced mitochondrial biogenesis in S. cerevisiae the respiratory chain-linked enzyme is formed considerably more rapidly than the overall NADH oxidase system; thus, the assembly of the components may be the rate-limiting step. On exposure of aerobic cells of S. cerevisiae to high glucose concentration, NADH dehydrogenase appears to undergo active destruction. |
| Databáze: | OpenAIRE |
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