Aliphatic and aromatic inhibitors binding to the active site of catechol 2,3-dioxygenase from Pseudomonas putida mt-2.
The interaction of different classes of inhibitors with the extradiol cleaving catechol 2,3-dioxygenase from Pseudomonas putida mt-2 was monitored by longitudinal and transverse proton relaxation measurements as well as by kinetic activity studies in order to characterize the type of interaction of such inhibitors with the active site of the enzyme. The average distances of the inhibitors from the catalytic iron(II) ion have been estimated from the 1H longitudinal relaxation rates. Phenols and aliphatic ketones appear to be coordinated to the iron(II) ion in the active site.
Bertini
I
I
Dipartimento di Chimica, Università di Firenze, Italy.
Briganti
F
F
Scozzafava
A
A
D000438:Alcohols / Q000378:metabolism; D001665:Binding Sites; D002384:Catalysis; D050557:Catechol 2,3-Dioxygenase; D049308:Dioxygenases; D004791:Enzyme Inhibitors / Q000378:metabolism*; D007501:Iron / Q000378:metabolism; D007659:Ketones / Q000378:metabolism; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D010105:Oxygenases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D016958:Pseudomonas putida / Q000201:enzymology*
D000438:Alcohols; D004791:Enzyme Inhibitors; D007659:Ketones; D007501:Iron; D010105:Oxygenases; D049308:Dioxygenases; D050557:Catechol 2,3-Dioxygenase