The enzyme that catalyses the hydroxylation of the methyl group of p-cresol was purified from Pseudomonas putida. It has mol.wt. 115000 and appears to contain two subunits of equal molecular weight. One subunit is a c-type cytochrome and the other is a flavoprotein. Reduction of the cytochrome occurred on addition of substrate. The same enzyme catalyses both p-cresol hydroxylation and the further oxidation of the product, 4-hydroxybenzyl alcohol. The stoicheiometry of acceptor reduced per molecule of substrate oxidized is that for two dehydrogenation reactions. The Km for p-cresol is 7.3 × 10(-6) M and that for 4-hydroxybenzyl alcohol is 47.6 × 10(-6) M. The enzyme, which is assayed with phenazine methosulphate as electron acceptor, was stimulated by particulate material, which probably contains the acceptor in vivo.
The purification and properties of p-cresol-(acceptor) oxidoreductase (hydroxylating), a flavocytochrome from Pseudomonas putida
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D J Hopper, D G Taylor; The purification and properties of p-cresol-(acceptor) oxidoreductase (hydroxylating), a flavocytochrome from Pseudomonas putida. Biochem J 1 October 1977; 167 (1): 155–162. doi: https://doi.org/10.1042/bj1670155
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