Abstract
Studies have been carried out to determine the spectral changes occurring during succinate and malate oxidation by mitochondria from beef adrenal cortex. The content of cytochromes a + a 3, b, c + c 1, and P-450 have been determined. The spectral properties of reduced cytochrome P-450, its complex with CO, and the interaction of oxidized cytochrome P-450 with deoxycorticosterone have been determined. The changes in extinction coefficients, as well as the location of absorption maxima and minima occurring during cytochrome P-450's oxidation and reduction associated with hydroxylation of DOC, are described. The results obtained are compared with those for cytochrome P-450 of microsomes prepared from rabbit liver.
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