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J. Biol. Chem., Vol. 259, Issue 24, 15040-15045, Dec, 1984
B Sumegi and PA Srere
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,
alpha-ketoglutarate dehydrogenase complex, mitochondrial malate
dehydrogenase, and beta-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,
alpha-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.
Complex I binds several mitochondrial NAD-coupled dehydrogenases
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