title: The purification and properties of p-cresol-(acceptor) oxidoreductase (hydroxylating), a flavocytochrome from Pseudomonas putida.
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 x 10(-6) M and that for 4-hydroxybenzyl alcohol is 47.6 x 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.
mesh_terms: D003408:Cresols; D003580:Cytochromes; D005415:Flavins / Q000032:analysis; D006418:Heme / Q000032:analysis; D007700:Kinetics; D006899:Mixed Function Oxygenases / Q000302:isolation & purification*; D008970:Molecular Weight; D011506:Proteins / Q000032:analysis; D011549:Pseudomonas / Q000201:enzymology*; D013057:Spectrum Analysis
chemical_list: D003408:Cresols; D003580:Cytochromes; D005415:Flavins; D011506:Proteins; D006418:Heme; D006899:Mixed Function Oxygenases