Complex I binds several mitochondrial NAD-coupled dehydrogenases

Research output: Contribution to journalArticle

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Abstract

NADH:ubiquinone reductase (complex I) of the mitochondrial inner membrane respiratory chain binds a number of mitochondrial matrix NAD-linked dehydrogenases. These include pyruvate dehydrogenase complex, α-ketoglutarate dehydrogenase complex, mitochondrial malate dehydrogenase, and β-hydroxyacyl-CoA dehydrogenase. No binding was detected between complex I and cytosolic malate dehydrogenase, glutamate dehydrogenase, NAD-isocitrate dehydrogenase, lipoamide dehydrogenase, citrate synthase, or fumarase. The dehydrogenases that bound to complex I did not bind to a preparation of complex II and III, nor did they bind to liposomes. The binding of pyruvate dehydrogenase complex, α-ketoglutarate dehydrogenase complex, and mitochondrial malate dehydrogenase to complex I is a saturable process. Based upon the amount of binding observed in these in vitro studies, there is enough inner membrane present in the mitochondria to bind the dehydrogenases in the matrix space. The possible metabolic significance of these interactions is discussed.

Original languageEnglish
Pages (from-to)15040-15045
Number of pages6
JournalJournal of Biological Chemistry
Volume259
Issue number24
Publication statusPublished - 1984

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NAD
Malate Dehydrogenase
Oxidoreductases
Ketoglutarate Dehydrogenase Complex
Pyruvate Dehydrogenase Complex
Fumarate Hydratase
Dihydrolipoamide Dehydrogenase
Membranes
Electron Transport Complex I
Isocitrate Dehydrogenase
Citrate (si)-Synthase
Glutamate Dehydrogenase
Mitochondria
Mitochondrial Membranes
Coenzyme A
Electron Transport
Liposomes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Complex I binds several mitochondrial NAD-coupled dehydrogenases. / Sümegi, B.; Srere, P.

In: Journal of Biological Chemistry, Vol. 259, No. 24, 1984, p. 15040-15045.

Research output: Contribution to journalArticle

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