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Oxoglutarate dehydrogenase complex

About: Oxoglutarate dehydrogenase complex is a research topic. Over the lifetime, 2067 publications have been published within this topic receiving 69249 citations. The topic is also known as: GO:0045252 & dihydrolipoamide S-succinyltransferase complex.


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Journal ArticleDOI
TL;DR: It is emphasised in this article that these three dehydrogenases appear only to be regulated by calcium ions in vertebrates and that this raises some interesting and potentially important developmental issues.

713 citations

Journal ArticleDOI
TL;DR: The discovery that the activity of the multienzyme pyruvate dehydrogenase complex from beef kidney mitochondria is regulated by a phosphorylation-dephosphorylation reaction sequence is reported.
Abstract: This paper reports the discovery that the activity of the multienzyme pyruvate dehydrogenase complex from beef kidney mitochondria is regulated by a phosphorylation-dephosphorylation reaction sequence. The site of this regulation is the pyruvate dehydrogenase component of the complex. Phosphorylation and concomitant inactivation of pyruvate dehydrogenase are catalyzed by an ATP-specific kinase (i.e., a pyruvate dehydrogenase kinase), and dephosphorylation and concomitant reactivation are catalyzed by a phosphatase (i.e., a pyruvate dehydrogenase phosphatase). The kinase and the phosphatase appear to be regulatory subunits of the pyruvate dehydrogenase complex.

594 citations

Journal ArticleDOI
TL;DR: In mitochondria, electrons are transferred from NADH to O2 through a chain of three large enzyme complexes, namely NADH: ubiquinone oxidoreductase (NADH dehydrogenase or complex I), ubiquinol: ferricytochrome c oxidore ductase (cytochrome reductase orcomplex III), and ferrocy tochrome c:O2 oxidoreductionase (Cytochrome oxid enzyme or complex IV).
Abstract: In mitochondria, electrons are transferred from NADH to O2 through a chain of three large enzyme complexes, namely NADH: ubiquinone oxidoreductase (NADH dehydrogenase or complex I), ubiquinol: ferricytochrome c oxidoreductase (cytochrome reductase or complex III), and ferrocytochrome c:O2 oxidoreductase (cytochrome oxidase or complex IV). The function of these enzyme complexes is to link electron transfer with proton translocation out of the mitochondrion. In doing so, they generate a transmembraneous proton motive force which subsequently drives ATP synthesis by the H+-ATPase (complex V, for a review see [1]).

491 citations

Journal ArticleDOI
TL;DR: It is concluded that β‐amyloid can directly disrupt mitochondrial function, inhibits key enzymes and may contribute to the deficiency of energy metabolism seen in Alzheimer's disease.
Abstract: Disrupted energy metabolism, in particular reduced activity of cytochrome oxidase (EC 1.9.3.1), alpha-ketoglutarate dehydrogenase (EC 1.2.4.2) and pyruvate dehydrogenase (EC 1.2.4.1) have been reported in post-mortem Alzheimer's disease brain. beta-Amyloid is strongly implicated in Alzheimer's pathology and can be formed intracellularly in neurones. We have investigated the possibility that beta-amyloid itself disrupts mitochondrial function. Isolated rat brain mitochondria have been incubated with the beta-amyloid alone or together with nitric oxide, which is known to be elevated in Alzheimer's brain. Mitochondrial respiration, electron transport chain complex activities, alpha-ketoglutarate dehydrogenase activity and pyruvate dehydrogenase activity have been measured. Beta-amyloid caused a significant reduction in state 3 and state 4 mitochondrial respiration that was further diminished by the addition of nitric oxide. Cytochrome oxidase, alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase activities were inhibited by beta-amyloid. The K(m) of cytochrome oxidase for reduced cytochrome c was raised by beta-amyloid. We conclude that beta-amyloid can directly disrupt mitochondrial function, inhibits key enzymes and may contribute to the deficiency of energy metabolism seen in Alzheimer's disease.

454 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20222
20214
20207
20197
20186
201712