[Characteristics of the interaction of adrenal lipoamide dehydrogenase with physiological and quinone electron acceptors].

Abstract

Lipoamide dehydrogenase (EC 1.6.4.3) from the ketoglutarate dehydrogenase complex of adrenals catalyzes the oxidation of NADH by lipoamide and quinone compounds according to the "ping-pong" scheme. The catalytic constants of these reactions are equal to 220 and 24 s-1, respectively (pH 7.0). The maximal quinone reductase activity is observed at pH 5.6, whereas the lipoamide reductase activity changes insignificantly at pH 7.5-5.5. The maximal dihydrolipoamide-NAD+ reductase activity is observed at pH 7.8. The oxidative constants of quinone electron acceptors vary from 6 X 10(6) to 4 X 10(2) M-1 s-1 and increase with their redox potential. The patterns of NAD+ inhibition in the quinone reductase reaction differ from that of lipoamide reductase reaction. The quinones are reduced by lipoamide dehydrogenase in the one-electron mechanism.

Cite this paper

@article{Chenas1987CharacteristicsOT, title={[Characteristics of the interaction of adrenal lipoamide dehydrogenase with physiological and quinone electron acceptors].}, author={N K Chenas and Aldona Butkus and Iu Iu Kanapenene and Iu Iu Kulis}, journal={Ukrainskiĭ biokhimicheskiĭ zhurnal}, year={1987}, volume={59 2}, pages={44-9} }