Abstract
Hydroxylation of progesterone was performed with intact cells, cell homogenate and with different subcellular fractions. The hydroxylating system in Rhizopus nigricans was found in post-mitochondrial supernatant. The reaction was inhibited by carbon monoxide and the inhibition was reversed by irradiation with light at a predominant wavelength of 450 nm thus indicating the involvement of cytochrome P-450 in the hydroxylation reaction. Using the reduced CO difference spectra, we have located the enzyme cytochrome P-450 in the membrane fraction sedimenting at 105.000 g.
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