Difference between revisions of "Hatefi 1962 J Biol Chem-XLII"
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{{Publication | {{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: 2661-2669. | |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: 2661-2669. | ||
|info=[http://www.jbc.org/content/237/8/2661.full.pdf+html PMID:13905326 Open Access] | |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 | |authors=Hatefi Y, Haavik AG, Fowler LR, Griffiths DE | ||
|year=1962 | |year=1962 | ||
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# 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 o f 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 o f 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. | ||
# The reconstituted activities are quite stable to repeated freezing, thawing, and storage at -2O°, 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. | # The reconstituted activities are quite stable to repeated freezing, thawing, and storage at -2O°, 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 | |keywords=electron transfer, DPNH-coenzyme Q reductase, succinic-coenzyme Q reductase, QH2-cytochrome c reductase, cytochrome c reductase | ||
}} | }} | ||
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|enzymes=Complex II; Succinate Dehydrogenase, Complex IV; Cytochrome c Oxidase | |enzymes=Complex II; Succinate Dehydrogenase, Complex IV; Cytochrome c Oxidase | ||
|kinetics=Reduced Substrate; Cytochrome c | |kinetics=Reduced Substrate; Cytochrome c | ||
|additional=Made history | |||
}} | }} | ||
Revision as of 17:59, 12 June 2012
| 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: 2661-2669. |
Hatefi Y, Haavik AG, Fowler LR, Griffiths DE (1962) J Biol Chem
Abstract:
- 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.
- The four enzyme systems that collectively comprise the complete machinery for transfer of electrons from reduced diphosphopyridine nucleotide (DPNH) 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 o f 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.
- The reconstituted activities are quite stable to repeated freezing, thawing, and storage at -2O°, 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
Labels:
Organism: Other Mammal"Other Mammal" is not in the list (Human, Pig, Mouse, Rat, Guinea pig, Bovines, Horse, Dog, Rabbit, Cat, ...) of allowed values for the "Mammal and model" property.
Tissue;cell: Cardiac muscle"Cardiac muscle" is not in the list (Heart, Skeletal muscle, Nervous system, Liver, Kidney, Lung;gill, Islet cell;pancreas;thymus, Endothelial;epithelial;mesothelial cell, Blood cells, Fat, ...) of allowed values for the "Tissue and cell" property.
Preparation: Isolated Mitochondria"Isolated Mitochondria" is not in the list (Intact organism, Intact organ, Permeabilized cells, Permeabilized tissue, Homogenate, Isolated mitochondria, SMP, Chloroplasts, Enzyme, Oxidase;biochemical oxidation, ...) of allowed values for the "Preparation" property.
Enzyme: Complex II; Succinate Dehydrogenase"Complex II; Succinate Dehydrogenase" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property., Complex IV; Cytochrome c Oxidase"Complex IV; Cytochrome c Oxidase" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property.
Made history
