Studies on bacterial urate:oxygen oxidoreductase

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Abstract 1. 1.Some properties of Arthrobacter pascens urate oxidase (urate:oxygen oxido-reductase, EC 1.7.3.3) were investigated in regard to its active site. The addition of Fe 3+ can partially protect the enzyme from inactivation at low pH or at low ionic strength and stimulate reactivation. 2. 2.The addition of Cu 2+ inactivated the enzyme, but this inactivation was counteracted by the presence of uric acid, the substrate. 3. 3.The inhibitory and inactivating actions of Cu 2+ on the enzyme were counteracted by the addition of Fe 3+ . 4. 4.Cyanide inhibited the enzyme activity. The binding site of cyanide to the enzyme was the site to which the oxygen was supposed to bind. 5. 5.The iron and copper contenst of the enzyme were less than 0.2 mole per mole of enzyme protein. But many observations made it possible to consider that the iron, not the copper, may act as one of the prosthetic groups of the enzyme. 6. 6.The kientic data suggested the existence of a ternary complex consisting of the enzyme and the two substrates, uric acid and oxygen.

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