Difference between revisions of "Chance 1961 J Biol Chem-IV"
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|organism=Guinea pig | |organism=Guinea pig, Birds | ||
|tissues=Heart, Liver, Kidney | |tissues=Heart, Liver, Kidney | ||
|preparations=Isolated mitochondria | |preparations=Isolated mitochondria |
Latest revision as of 09:54, 9 November 2016
Chance B, Hollunger G (1961) The interaction of energy and electron transfer reactions in mitochondria IV. The pathway of electron transfer. J Biol Chem 236:1562-8. |
Chance B, Hollunger G (1961) J Biol Chem
Abstract:
- The pathway of electron transfer from succinate to pyridine nucleotide shows a sensitivity to antimycin A, suggesting that carriers of the respiratory chain up to and including the antimycin-sensitive point are involved in succinate-linked reduction of pyridine nucleotide.
- The sensitivity of succinate-linked reduction of pyridine nucleotide to Amytal suggests that a reverse of the flavoprotein-pyridine nucleotide interaction observed in the oxidation of pyridine nucleotide in phosphorylating mitochondria is also part of the electron transfer pathway.
- Mechanisms indicating the interconnection of electrons from the antimycin-sensitive point to this flavoprotein via electron carriers such as cytochrome b and ubiquinone are considered. These mechanisms appear to apply to both aerobic and anaerobic (terminally inhibited) energy-linked reduction of pyridine nucleotide.
- Three mechanisms for increased reduction of pyridine nucleotide in succinate-treated mitochondria that do not involve the above pathway fail to show responses of the experimentally observed sensitivity to Amytal or to antimycin A.
- The properties of the energy-linked pool of pyridine nucleotide in metabolism are considered. Its participation is likely to be small in state 3 and of some consequence in state 4.
β’ Keywords: Electron transfer, Succinate, Pyridine nucleotide, Antimycin A
Labels:
Organism: Guinea pig, Birds
Tissue;cell: Heart, Liver, Kidney
Preparation: Isolated mitochondria
Enzyme: Complex II;succinate dehydrogenase, Complex III
Coupling state: OXPHOS
Made history