title: Versatile peroxidase of Bjerkandera fumosa: substrate and inhibitor specificity.
abstract: The inhibitor and substrate specificities of versatile peroxidase from Bjerkandera fumosa (VPBF) were studied. Two different effects were found: NaN(3), Tween-80, anthracene, and fluorene decreased the activity of VPBF, but p-aminobenzoic acid increased it. A mixed mechanism of effector influence on the activity of this enzyme was shown. The catalytic properties of VPBF in the oxidation of mono- and polycyclic aromatic compounds were studied also. 2,7-Diaminofluorene, ABTS, veratryl alcohol, and syringaldazine can be oxidized by VPBF in two ways: either directly by the enzyme or by diffusible chelated Mn(3+) as an oxidizing agent. During VPBF oxidation of 2,7-diaminofluorene, both with and without Mn(2+), biphasic kinetics with apparent saturation in both micromolar and millimolar ranges were obtained. In the case of ABTS, inhibition of VPBF activity by an excess of substrate was observed. Direct oxidation of p-aminobenzoic acid by versatile peroxidase was found for the first time. The oxidation of three- and four-ring PAHs by VPBF was investigated, and the oxidation of anthracene, phenanthrene, fluorene, pyrene, chrysene, and fluoranthene was shown. The products of PAH oxidation (9,10-anthraquinone, 9,10-phenanthrenequinone, and 9-fluorenone) catalyzed by VPBF were identified.
authors.affiliation: Institute of Biochemistry and Physiology of Plants and Microorganisms, Russian Academy of Sciences, 410049 Saratov, Russia. nataliapozdnyakova@yahoo.com
authors.forename: Natalia
authors.initials: N
authors.lastname: Pozdnyakova
authors.forename: Oleg
authors.initials: O
authors.lastname: Makarov
authors.forename: Marina
authors.initials: M
authors.lastname: Chernyshova
authors.forename: Olga
authors.initials: O
authors.lastname: Turkovskaya
authors.forename: Anna
authors.initials: A
authors.lastname: Jarosz-Wilkolazka
mesh_terms: D010129:4-Aminobenzoic Acid / Q000494:pharmacology; D000873:Anthracenes / Q000494:pharmacology; D055162:Biocatalysis; D020134:Catalytic Domain / Q000187:drug effects; D055453:Coriolaceae / Q000201:enzymology*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005449:Fluorenes / Q000494:pharmacology; D005656:Fungal Proteins / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D011084:Polycyclic Aromatic Hydrocarbons / Q000378:metabolism*; D011136:Polysorbates / Q000494:pharmacology; D011748:Pyrogallol / Q000031:analogs & derivatives / Q000378:metabolism; D019810:Sodium Azide / Q000494:pharmacology; D013379:Substrate Specificity
chemical_list: D000873:Anthracenes; D004791:Enzyme Inhibitors; D005449:Fluorenes; D005656:Fungal Proteins; D011084:Polycyclic Aromatic Hydrocarbons; D011136:Polysorbates; D011748:Pyrogallol; C041509:fluorene; C010120:pyrogallol 1,3-dimethyl ether; D019810:Sodium Azide; D010544:Peroxidases; C034020:anthracene; D010129:4-Aminobenzoic Acid