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The purification and properties of p-cresol-(acceptor) oxidoreductase (hydroxylating), a flavocytochrome from Pseudomonas putida

D J Hopper, D G Taylor
Biochemical Journal Oct 01, 1977, 167 (1) 155-162; DOI: 10.1042/bj1670155
D J Hopper
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D G Taylor
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Abstract

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.

  • © 1977 London: The Biochemical Society
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October 1977

Volume: 167 Issue: 1

Biochemical Journal: 167 (1)
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The purification and properties of p-cresol-(acceptor) oxidoreductase (hydroxylating), a flavocytochrome from Pseudomonas putida
D J Hopper, D G Taylor
Biochemical Journal Oct 1977, 167 (1) 155-162; DOI: 10.1042/bj1670155
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The purification and properties of p-cresol-(acceptor) oxidoreductase (hydroxylating), a flavocytochrome from Pseudomonas putida
D J Hopper, D G Taylor
Biochemical Journal Oct 1977, 167 (1) 155-162; DOI: 10.1042/bj1670155

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