Difference between revisions of "Hatefi 1962 J Biol Chem-XLII"

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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.

» PMID:13905326 Open Access

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 °C, 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. • 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: ETS"ETS" is not in the list (LEAK, ROUTINE, OXPHOS, ET) of allowed values for the "Coupling states" property.

Made history

Electron transfer-pathway versus electron transport chain

More details: »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. - »Open Access 2014 edition«

@@ Line 1: / Line 1: @@
 {{Publication
-|title=Hatefi Y, Haavik AG, Fowler LR, Griffiths DE (1962) Studies on the electron transfer system XLII. Reconstitution of the electron transfer system. J Biol Chem 237:2661-9.
+|title=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.
 |info=[http://www.jbc.org/content/237/8/2661.full.pdf+html PMID:13905326 Open Access]
 |authors=Hatefi Y, Haavik AG, Fowler LR, Griffiths DE
 |year=1962
 |journal=J Biol Chem
-|abstract=1. It has been shown that the electron transfer system 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.
+|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.
 . 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.
-. 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 system, are essentially the same  as those found for the same activities in the intact mitochondria and in the  integrated particles derived therefrom.
+. 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.
 . The reconstituted activities are quite stable to repeated freezing, thawing, and storage at -2O °C, 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.
@@ Line 24: / Line 24: @@
 }}
 [[File:Hatefi 1962 NS 2012.jpg|right|500px|Q-junction]]
-== Electron transfer system versus electron transport chain ==
+== Electron transfer-pathway versus electron transport chain ==
-* ''More details:'' »[[Electron transfer system]]
+* ''More details:'' »[[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 2014 MitoPathways |»Open Access 2014 edition«]]