The relation between the activity of urease and the oxidation-reduction potential

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Abstract
The activity of urease preparations was investigated under the influence of reversible oxidation-reduction systems. The enzyme activity was unaffected by the addition, of methylene blue, leucomethylene blue, or ferro-ferricya-nide. A stream of air or H bubbling through the solution while the hydrolysis was in progress had no influence on the rate of hydrolysis; H activated by palladized asbestos was likewise without influence. The inhibition of the urease by quinol, which was observed by Quastel, could be prevented by treatment with active H. This indicates that the quinol inhibition is due, as Quastel has suggested, to the action of traces of quinone rather than to the quinol itself. It is concluded that the reaction of the enzyme with the quinone is a specific one and, if it is oxidative in nature, is not reversible in the thermodynamic sense.

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