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Steroid hydroxylation and oxidative phosphorylation in human adrenal cortex mitochondria.

The 11β-steroid hydroxylation and oxidative phosphorylation were examined in mitochondria isolated from adrenal glands surgically removed from 4 patients with Cushing's disease. With the substrates used (isocitrate, malate, and β-OH-butyrate), steroid hydroxylation was blocked by KCN but could be restored by ATP, indicating an energy requirement. Only a partial inhibition due to KCN was observed with isocitrate and malate and, in agreement with this, latent forms of both malic enzyme and the NADP-linked isocitrate dehydrogenase were present in the mitochondria. The latter enzyme had the higher specific activity. The conversion of 11-deoxycortisol to cortisol was about 2 times faster than the hydroxylation of deoxycorticosterone to corticosterone. Oxidative phosphorylation supported by several substrates was examined with the oxygen electrode. High ADP/O and respiratory control ratios and ADPstimulated respiratory rates were observed. (Endocrinology 88: 318, 1971)