Lipoamide dehydrogenase, a component of the bovine adrenal ketoglutarate dehydrogenase complex, catalyzes the oxidation of NADH by p-quinones and ferricyanide. The kinetics of oxidation obey the ping-pong mechanism. At pH 7.0, the constants for the active center oxidation by quinones (kox) are equal to 1.1 X 10(4)-5.3 X 10(5) M-1s-1 and increase as the acceptor potential rises. The values of kox for quinones change insignificantly within the pH range of 7.7-5.0, whereas that for ferricyanide increases 10-fold with a decrease of pH from 7.0 to 5.0. The value of the catalytic constant for the enzyme (kcat) reaches its maximum at pH 5.5. The quinones interact with the thiol groups of lipoamide dehydrogenase by inhibiting the fluorescence of FAD and diaphorease activity. The reaction is catalyzed by a basic amino acid (pK 6.7) within the composition of the enzyme.