Ernster 1969 Eur J Biochem: Difference between revisions
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|title=Ernster L, Lee IY, Norling B, Persson B (1969) Studies with ubiquinone-depleted submitochondrial particles. Essentiality of ubiquinone for the interaction of succinate dehydrogenase, NADH dehydrogenase, and cytochrome ''b''. Eur J Biochem 9:299-310. | |title=Ernster L, Lee IY, Norling B, Persson B (1969) Studies with ubiquinone-depleted submitochondrial particles. Essentiality of ubiquinone for the interaction of succinate dehydrogenase, NADH dehydrogenase, and cytochrome ''b''. Eur J Biochem 9:299-310. | ||
|info=[https://pubmed.ncbi.nlm.nih.gov/4307591/ PMID: 4307591] | |info=[https://pubmed.ncbi.nlm.nih.gov/4307591/ PMID: 4307591 Open Access] | ||
|authors=Ernster L, Lee IY, Norling B, Persson B | |authors=Ernster L, Lee IY, Norling B, Persson B | ||
|year=1969 | |year=1969 | ||
|journal=Eur J Biochem | |journal=Eur J Biochem | ||
|abstract=1. Submitochondrial particles were prepared from beefāheart mitochondria by sonication in the presence of EDTA. The particles were lyophilized and repeatedly extracted with pentane until no ubiquinone was found in the extract. Treatment of the ubiquinoneādepleted particles with pentane containing a suitable concentration of ubiquinone (ubiquinoneā50) and subsequent quick washing with ubiquinoneāfree pentane resulted in a āreāincorporationā of ubiquinone in an amount similar to that present in the original particles (3ā6 nmoles/mg protein). | |||
2. The ubiquinoneādepleted particles exhibited very low or no succinate and NADH oxidase activities, which were restored upon the reāincorporation of ubiquinone to the levels found in the lyophilized particles before extraction with pentane. Partial (about 50 %) extraction of ubiquinone resulted in markedly decreased succinate and NADH oxidase activities. | |||
3. Added cytochrome ''c'' did not replace ubiquinone in restoring the succinate or NADH oxidase activity of ubiquinoneādepleted particles. It stimulated the NADH oxidase, but not the succinate oxidase, activity of the āubiquinoneāincorporatedā particles, but the same stimulation occurred with the lyophilized particles before ubiquinone extraction. The normal, lyophilized, and āubiquinoneāincorporatedā particles contained equal amounts of both total and enzymatically reducible cytochromes. | |||
4. In the presence of KCN, NADH reduced the cytochromes, including cytochrome ''b'', only at insignificant rates in the ubiquinoneādepleted particles as compared to the normal and lyophilized preparations, and these rates were greatly stimulated upon the reāincorporation of ubiquinone. Succinate caused a rapid partial (about 25 %) reduction of cytochrome ''b'', but not of the rest of the cytochromes, in the ubiquinoneādepleted particles. This reduction occurred also in the absence of KCN, and the fraction of cytochrome ''b'', so reduced was not reoxidized when succinate oxidation was inhibited by malonate. Evidence for the occurrence of such an enzymatically nonāoxidizable form of cytochrome ''b'' was also obtained in the normal, lyophilized and āubiquinoneāincorporatedā particles, but, in those cases, this cytochrome ''b'' was reduced by both succinate and NADH. In the presence of antimycin A, all cytochrome ''b'' in the ubiquinoneādepleted particles was rapidly reduced by succinate but not by NADH. | |||
5. The normal and lyophilized particles catalyzed a rotenoneāsensitive oxidation of NADH by fumarate. This reaction was completely absent from the ubiquinoneādepleted particles and was restored upon the reāincorporation of ubiquinone. | |||
6. N,N,Nā²,Nā²āTetramethylāpāphenylenediamine catalyzed an NADH and succinate oxidase activity in antimycin Aāinhibited particles. This NADH oxidase activity was partially sensitive to rotenone in the normal, lyophilized and āubiquinoneāincorporatedā particles, but completely rotenoneāinsensitive in the ubiquinoneādepleted particles. All four types of particles were active in catalyzing the antimycin Aāsensitive oxidation of menadiol. | |||
7. It is concluded that uniquinone is essential for the interaction of succinate dehydrogenase, NADH dehydrogenase and cytochrome ''b'', and that this interaction is a requisite for the normal function of the respiratory chain. Functionally modified forms of cytochrome ''b'', arising as a consequence of structural damage or antimycin A treatment, are discussed in relation to existing information and proposals concerning the role of cytochrome ''b'' and ubiquinone in electron transport. | |||
|editor=Komlodi T | |editor=Komlodi T | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|organism=Bovines | |||
|tissues=Heart | |||
|preparations=SMP | |||
|topics=Cyt c, Redox state, Q-junction effect | |||
|pathways=N, S | |||
|additional=MitoFit 2021 CoQ | |additional=MitoFit 2021 CoQ | ||
}} | }} | ||
== Cited by == | |||
{{Template:Cited by Komlodi 2021 MitoFit CoQ}} |
Revision as of 16:47, 2 April 2021
Ernster L, Lee IY, Norling B, Persson B (1969) Studies with ubiquinone-depleted submitochondrial particles. Essentiality of ubiquinone for the interaction of succinate dehydrogenase, NADH dehydrogenase, and cytochrome b. Eur J Biochem 9:299-310. |
Ernster L, Lee IY, Norling B, Persson B (1969) Eur J Biochem
Abstract: 1. Submitochondrial particles were prepared from beefāheart mitochondria by sonication in the presence of EDTA. The particles were lyophilized and repeatedly extracted with pentane until no ubiquinone was found in the extract. Treatment of the ubiquinoneādepleted particles with pentane containing a suitable concentration of ubiquinone (ubiquinoneā50) and subsequent quick washing with ubiquinoneāfree pentane resulted in a āreāincorporationā of ubiquinone in an amount similar to that present in the original particles (3ā6 nmoles/mg protein).
2. The ubiquinoneādepleted particles exhibited very low or no succinate and NADH oxidase activities, which were restored upon the reāincorporation of ubiquinone to the levels found in the lyophilized particles before extraction with pentane. Partial (about 50 %) extraction of ubiquinone resulted in markedly decreased succinate and NADH oxidase activities.
3. Added cytochrome c did not replace ubiquinone in restoring the succinate or NADH oxidase activity of ubiquinoneādepleted particles. It stimulated the NADH oxidase, but not the succinate oxidase, activity of the āubiquinoneāincorporatedā particles, but the same stimulation occurred with the lyophilized particles before ubiquinone extraction. The normal, lyophilized, and āubiquinoneāincorporatedā particles contained equal amounts of both total and enzymatically reducible cytochromes.
4. In the presence of KCN, NADH reduced the cytochromes, including cytochrome b, only at insignificant rates in the ubiquinoneādepleted particles as compared to the normal and lyophilized preparations, and these rates were greatly stimulated upon the reāincorporation of ubiquinone. Succinate caused a rapid partial (about 25 %) reduction of cytochrome b, but not of the rest of the cytochromes, in the ubiquinoneādepleted particles. This reduction occurred also in the absence of KCN, and the fraction of cytochrome b, so reduced was not reoxidized when succinate oxidation was inhibited by malonate. Evidence for the occurrence of such an enzymatically nonāoxidizable form of cytochrome b was also obtained in the normal, lyophilized and āubiquinoneāincorporatedā particles, but, in those cases, this cytochrome b was reduced by both succinate and NADH. In the presence of antimycin A, all cytochrome b in the ubiquinoneādepleted particles was rapidly reduced by succinate but not by NADH.
5. The normal and lyophilized particles catalyzed a rotenoneāsensitive oxidation of NADH by fumarate. This reaction was completely absent from the ubiquinoneādepleted particles and was restored upon the reāincorporation of ubiquinone.
6. N,N,Nā²,Nā²āTetramethylāpāphenylenediamine catalyzed an NADH and succinate oxidase activity in antimycin Aāinhibited particles. This NADH oxidase activity was partially sensitive to rotenone in the normal, lyophilized and āubiquinoneāincorporatedā particles, but completely rotenoneāinsensitive in the ubiquinoneādepleted particles. All four types of particles were active in catalyzing the antimycin Aāsensitive oxidation of menadiol.
7. It is concluded that uniquinone is essential for the interaction of succinate dehydrogenase, NADH dehydrogenase and cytochrome b, and that this interaction is a requisite for the normal function of the respiratory chain. Functionally modified forms of cytochrome b, arising as a consequence of structural damage or antimycin A treatment, are discussed in relation to existing information and proposals concerning the role of cytochrome b and ubiquinone in electron transport.
ā¢ Bioblast editor: Komlodi T
Labels:
Organism: Bovines
Tissue;cell: Heart
Preparation: SMP
Regulation: Cyt c, Redox state, Q-junction effect
Pathway: N, S
MitoFit 2021 CoQ
Cited by
- KomlĆ³di T, Cardoso LHD, Doerrier C, Moore AL, Rich PR, Gnaiger E (2021) Coupling and pathway control of coenzyme Q redox state and respiration in isolated mitochondria. Bioenerg Commun 2021.3. https://doi.org/10.26124/bec:2021-0003