Abstract
Growth of a Xanthobacter sp. on cyclohexane as the sole carbon and energy source gives rise to the induction of a soluble, NADPH-dependent, cytochrome P -450-containing cyclohexane hydroxylase. Studies with this enzyme (gel filtration and ion-exchange chromatography) have indicated it to be a three-component enzyme system comprised of a ferredoxin reductase, a ferredoxin and a cytochrome P -450 as the terminal electron acceptor. Incubations of semi-purified cyclohexane hydroxylase following gel filtration with various substrates gave rise to the corresponding hydroxylated product.
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