Hatefi 1962 J Biol Chem-XLII: Difference between revisions
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[[File:Hatefi 1962 NS 2012.jpg|right|500px|Q-junction]] | [[File:Hatefi 1962 NS 2012.jpg|right|500px|Q-junction]] | ||
== Electron transfer-pathway versus electron transport chain == | == Electron transfer-pathway versus electron transport chain == | ||
* ''More details:'' ยป[[Electron transfer-pathway]] | :::* ''More details:'' ยป[[Electron transfer-pathway]] | ||
* Gnaiger E (2012) Mitochondrial pathways and respiratory control. An introduction to OXPHOS analysis. 3rd ed. Mitochondr Physiol Network 17.18. OROBOROS MiPNet Publications, Innsbruck:64 pp. - [[Gnaiger | :::* Gnaiger E (2014) Mitochondrial pathways and respiratory control. An introduction to OXPHOS analysis. 4th ed. Mitochondr Physiol Network 19.12. Oroboros MiPNet Publications, Innsbruck:80 pp.ย - [[Gnaiger 2014 MitoPathways |ยปBioblast linkยซ]] | ||
:::* Gnaiger E (2012) Mitochondrial pathways and respiratory control. An introduction to OXPHOS analysis. 3rd ed. Mitochondr Physiol Network 17.18. OROBOROS MiPNet Publications, Innsbruck:64 pp. - [[Gnaiger 2012 MitoPathways |ยปBioblast linkยซ]] |
Revision as of 21:36, 19 April 2020
Hatefi Y, Haavik AG, Fowler LR, Griffiths DE (1962) Studies on the Electron transfer-pathway XLII. Reconstitution of the Electron transfer-pathway. J Biol Chem 237:2661-9. |
Hatefi Y, Haavik AG, Fowler LR, Griffiths DE (1962) J Biol Chem
Abstract: 1. It has been shown that the Electron transfer-pathway in beef heart mitochondria may be reconstituted either totally or in any desired sequential segment by appropriate combinations of two or more of the four primary complexes that have been isolated in highly purified form in this laboratory.
2. The four enzyme systems that collectively comprise the complete machinery for transfer of electrons from reduced diphosphopyridine nucleotide (DPNH; =NADH) and succinate to oxygen re: I, DPNH-coenzyme Q reductase; II, succinic-coenzyme Q reductase; III, QH2-cytochrome c reductase; and IV, cytochrome c reductase. The specific inhibitors of each complex have been studied.
3. By appropriate combinations of the primary complexes the following secondary activities have been reconstituted: V, DPNH-cytochrome c reductase; VI, succinic-cytochrome c reductase; VII, DPNH, succinic-cytochrome c reductase; VIII, DPNH oxidase; IX, succinic oxidase; and X, DPNH, succinic oxidase activity. The general oxidation-reduction properties of the reconstituted systems, both in the presence and the absence of the usual specific inhibitors of the Electron transfer-pathway, are essentially the same as those found for the same activities in the intact mitochondria and in the integrated particles derived therefrom.
4. The reconstituted activities are quite stable to repeated freezing, thawing, and storage at -2O ยฐC, and for the most part, when once formed, are not dissociated by dilution of the mixture or by centrifugation. The evidence supporting the conclusion that reconstitution necessarily involves a particle-particle interaction is discussed. โข Keywords: Electron transfer, DPNH-coenzyme Q reductase, Succinic-coenzyme Q reductase, QH2-cytochrome c reductase, Cytochrome c reductase, Beef heart
Labels:
Organism: Bovines
Tissue;cell: Heart
Preparation: Isolated mitochondria
Enzyme: Complex II;succinate dehydrogenase, Complex IV;cytochrome c oxidase
Regulation: Substrate
Coupling state: ET
Made history
Electron transfer-pathway versus electron transport chain
- More details: ยปElectron transfer-pathway
- Gnaiger E (2014) Mitochondrial pathways and respiratory control. An introduction to OXPHOS analysis. 4th ed. Mitochondr Physiol Network 19.12. Oroboros MiPNet Publications, Innsbruck:80 pp. - ยปBioblast linkยซ
- Gnaiger E (2012) Mitochondrial pathways and respiratory control. An introduction to OXPHOS analysis. 3rd ed. Mitochondr Physiol Network 17.18. OROBOROS MiPNet Publications, Innsbruck:64 pp. - ยปBioblast linkยซ